|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1928 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1456.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 848 TRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEM 927
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 928 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEER 1007
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1008 ISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAK 1087
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1088 KEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQE 1167
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1168 LRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAK 1247
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1248 QEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEE 1327
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1328 TRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1407
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1408 YEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALS 1487
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1488 LARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEV 1567
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1568 NMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQL 1647
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1648 RKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNAL 1727
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1728 QDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGA 1807
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1808 VKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLE 1887
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 13124875 1888 EAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKL 1928
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1322.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGF 338
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 339 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 499 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSII 578
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 13124875 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-771 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1319.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSIT-GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYT-FLSNGFVPIPAAQDDEMFQETVEAMAIM 336
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 337 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 416
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 417 ADFAVEALAKATYERLFRWILTRVNKALDKThRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 497 EEYQREGIEWNFIDFGLDLQPCIELIERPNnpPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK-FQKPKQLKDKTEF 575
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPN--MGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtESSLPSASKTKKGMFRTVGQ 655
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 656 LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 13124875 736 IPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1300.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGF 338
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 339 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 499 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSII 578
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 13124875 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1209.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSIT----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMA 334
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 335 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 415 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 495 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE 574
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTEsSLPSASKTKKGMFRTVG 654
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 13124875 735 AIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1157.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGF 338
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 339 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 499 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSII 578
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 658
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 13124875 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-771 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1141.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTS----ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMA 334
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 335 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 415 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 495 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTEssLPSASKTKKGMFRTVG 654
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 13124875 735 AIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1129.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASS---------HKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 250 FDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQET 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 330 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 409
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKpKQL 569
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 570 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrIVGLDQMAkMTESSLpsASKTKKGM 649
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF--GARTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 730 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-771 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1124.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 87 VEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 167 QDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFI 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN----VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 247 RINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN-GFVPIPAAQDDEM 325
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 326 FQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGR 405
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 406 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 485
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 486 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 565
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 566 PKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVgldqMAKMTESSLPSASKT 645
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAE----SAAANESGKSTPKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 13124875 726 QRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1080.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAaQDDEMFQETVEAMAIMGF 338
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 339 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 499 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSII 578
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESslPSASKTKKGMFRTVGQLYK 658
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 738
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 13124875 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-783 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1005.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 80 NPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIAD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 160 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKkdtsitGELEKQLLQANPILEAFGNAKTVKNDNS 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 240 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPA 319
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 320 AQDD-EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNT-AAQKVCHLMGINVTDFTRSIL 397
Cdd:smart00242 235 GIDDaEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 398 TPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCIN 477
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 478 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQ 557
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 558 GSHPKFQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmakmtes 637
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG--------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 638 slpSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 717
Cdd:smart00242 535 ---VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 718 RIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERD 783
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1191 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 887.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 36 VWVPSEKQGFEAASIKEEKGDEVVVEL---VENGKKVTVGKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLRERYF 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 111 SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 191 VIQYLAVVASSHkgkkdTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 270
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 271 AIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKV 349
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 350 VSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATY 429
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 430 ERLFRWILTRVNKALDKTHRQGaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 509
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 510 DFgLDLQPCIELIERpNNPPGVLALLDEECWFPKATDKSFVEKLCT--EQGSHPKFQKPKQLKDKteFSIIHYAGKVDYN 587
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 588 ASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVgldqmakmtesslpsasktKKGMFRTVGQLYKEQLGKLMTT 667
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 668 LRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA----IPKGFMDG 743
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 744 KQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLTAMKVIQRNC 823
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 824 AAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKED---ELQKTKERQQKAeNELKELEQKHsqltEEKNLLQEqlqaet 900
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLAciiKLQKTIKREKKL-RETEEVEFSL----KAEVLIQK------ 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 901 elYAEAEEMRVRLAAKKQelEEILHEMEARLEEEEDRGQQLQAERKKMAQqmldleeqleeeeAARQKLQLEKVTAEAKI 980
Cdd:COG5022 851 --FGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDVKSISS-------------LKLVNLELESEIIELKK 913
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 981 KKLEDEILVMDDQNNKLSKERKLLEER--ISDLTTNLAEEEEKAKNLTKLKNKHESmISELEVRLKKEE-------KSRQ 1051
Cdd:COG5022 914 SLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEYVKLPELNKLHEVESKLKET-SEEYEDLLKKSTilvregnKANS 992
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1052 ELEKLKRKLEGdasdFHEQIADLQAQIAELKmQLAKKEEELQAALARLDDEIAQKNNaLKKIRELEghisdlqedldser 1131
Cdd:COG5022 993 ELKNFKKELAE----LSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTELSI-LKPLQKLK-------------- 1052
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1132 aarNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHE 1191
Cdd:COG5022 1053 ---GLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLV 1109
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-771 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 882.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDTSiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL-----SNGFVPIPAAQDDEMFQETVEA 332
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 333 MAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNT--DQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 410
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 411 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQ-GASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 490 TMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQl 569
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 570 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkdvdrivgldqmakmtesslpsasktkkgm 649
Cdd:cd00124 476 KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 650 frtvgqlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 730 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 786.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKD------TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKkaqflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETV 330
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 331 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 410
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 411 AQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 490 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKP-- 566
Cdd:cd14927 398 HMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrp 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 567 -KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKmtESSLPSASKT 645
Cdd:cd14927 475 dKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDSTED--PKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14927 550 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 13124875 726 QRYEILAANAIPK-GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 769.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVASSH--KGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETVEAMAI 335
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 336 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 415 EQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVVKGR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGldqmakmtESSLPSASKTKKGMF 650
Cdd:cd14913 475 AEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA--------DSGKKKVAKKKGSSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14913 547 QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14913 627 LNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 757.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 418 DFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 498 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLK---DKT 573
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslpSASKTKKGMFRTV 653
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAK-------GGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 13124875 734 NAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 744.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASShkGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAK-EKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 418 DFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 498 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK---T 573
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkdvdriVGLDQMAKMTESSLPSASKTKKGM-FRT 652
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 13124875 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-771 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 713.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSG-LIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKkdTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGE--TQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETVEAMAIMG 337
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 417
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 418 DFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 497 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK--FQKPKQlkDKTE 574
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRF--SNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNassdkfvadlwkdvdrivgldqmakmtesslpsASKTKKgmfRTVG 654
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLK---------------------------------ASKNRK---KTVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaan 734
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL--- 590
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 13124875 735 aIPKGF---MDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01380 591 -LPSKEwlrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-771 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 710.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEkmRSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETVEAMAIM 336
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 337 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 416
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 417 ADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 496 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDKTE 574
Cdd:cd14929 394 QEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKFE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 575 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLW-KDVdrivgldqmakMTESSLPSASKT-KKGM- 649
Cdd:cd14929 471 ahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFeNYI-----------STDSAIQFGEKKrKKGAs 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14929 540 FQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYC 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 13124875 730 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14929 620 ILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 698.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVAS-SHKGKKDTSI-TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTPgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETVEAMAI 335
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELL-DMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 336 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 415 EQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 495 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDKT 573
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 574 E--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKmtesslPSASKTKKG-MF 650
Cdd:cd14917 476 EahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGADAPIE------KGKGKAKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14917 547 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14917 627 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-771 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 696.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 101 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 181 GAGKTENTKKVIQYLAVVASSHKGKKDTS--ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 416
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 417 ADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 496
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 497 EEYQREGIEWNFIDFGLDLQPCIELIERpnnPPGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDKTE- 574
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEK---PLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVVKGKAEa 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 575 -FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqMAKMTESSLPSASKTKKGMFRTV 653
Cdd:cd14918 478 hFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14918 550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 13124875 734 NAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14918 630 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 688.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVASSHKGKKD---TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 257 VGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETVEAMA 334
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 335 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 413
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 414 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslPSASKTKKGMF 650
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGS------KKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 687.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVASSHKGKKDT----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMA 334
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 335 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 413
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 414 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGMF 650
Cdd:cd14910 477 VEahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA-------AAAEAEEGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 684.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVAS-SHKGKKD--TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 256
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 257 VGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEgfNN---YTFLSNGFVPIPAAQDDEMFQETVEAM 333
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 334 AIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 412
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 413 TKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 493 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKD 571
Cdd:cd14916 398 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 572 KTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGM 649
Cdd:cd14916 475 KQEahFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14916 548 FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 13124875 730 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14916 628 ILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 683.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVASSHKGKKDT----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMA 334
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 335 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 413
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 414 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 494 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 572
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVVKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 573 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGldqmaKMTESSLPSASKTKKGMF 650
Cdd:cd14912 477 AEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG-----ASAGGGAKKGGKKKGSSF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14912 552 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 731 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14912 632 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-771 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 676.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFNNYTF--LSNGFVPIPAAQDDEMFQETVEAM 333
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 334 AIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 412
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 413 TKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 493 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKD 571
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 572 KTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivglDQMAKMTESSLPSASKTKKGM 649
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 13124875 730 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-771 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 659.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVASSHKgkkdtsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 260 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKE--KMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQETVEAMAIM 336
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 337 GFSEEEQLSILKVVSSVLQLGNIVFKK-ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 415
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 416 QADFAVEALAKATYERLFRWILTRVNKALDK---THRqgasFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPgqkNSR----FIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 493 ILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDK 572
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVD--RIVGLDQMAKMTESSlpsaSKTKKGMf 650
Cdd:cd14883 466 TEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDllALTGLSISLGGDTTS----RGTSKGK- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 13124875 731 LAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14883 621 LDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-771 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 650.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVASSHKGkkdtsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 260 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQETVEAMAIMGF 338
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 339 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 418
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 419 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 498
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 499 YQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKpkqlKDKTEFSII 578
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----ERGGAFTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 579 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLwkdvdRIVGLDQMAKMTESSLPSASKTKKgmfRTVGQLYK 658
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF-----ASKMLDASRKALPLTKASGSDSQK---QSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 659 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIpK 738
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-S 614
|
650 660 670
....*....|....*....|....*....|...
gi 13124875 739 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01383 615 ASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-771 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 644.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVASSHkgkkDTSItGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS----ESEV-ERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 260 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEM-FQETVEAMAIMGF 338
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAAdFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 339 SEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG---RDVVQKAQTKE 415
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 416 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 496 QEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFP-KATDKSFVEKLCTEQGSHPKFQKPKQLKD--K 572
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakmtesslpsaSKTKKGMFRT 652
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV-------------------DLDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 13124875 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-771 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 615.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAvvassHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA-----YMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFvPIPAAQDDEMFQETVEAMAI 335
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 336 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPD---NTAAQKVCHLMGINVTDFTRSiLTPRIKVGRD-VVQKA 411
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 412 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 491
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 492 FILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKqlKD 571
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 572 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtesslpsaSKTKKGM-F 650
Cdd:cd01384 468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------------EGTSSSSkF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 651 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 730
Cdd:cd01384 530 SSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 13124875 731 LAANAiPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd01384 610 LAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-771 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 603.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHkgkkdTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQH-----SWI----EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKK--ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 415
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 416 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFL--GILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSRTsiGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 494 LEQEEYQREGIEWNFIDFgLDLQPCIELI-ERPNNppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDk 572
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLN- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 573 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkDVDRIVGLDqmakmtesslpSASKTKkgmfrT 652
Cdd:cd01381 467 TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TRKKSP-----T 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 653 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd01381 530 LSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLV 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 13124875 733 ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01381 610 PGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-771 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 592.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAVVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG--------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLegfnnytflsngfvpIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNT-------DQASMPDNTAAQKvchLMGINVTDF-----TRSILTPRIKVGR 405
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 406 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALdkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 485
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCI--PFETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 486 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 565
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 566 P--------KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldqmAKMTES 637
Cdd:cd01382 450 PrksklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF------------ESSTNN 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 638 SLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 717
Cdd:cd01382 518 NKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 13124875 718 RIVFQEFRQRYEILAANAIPKgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-771 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 572.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASShkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS---------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSnGFVPIPAAQDDEMFQETVEAMAIMGF 338
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLS-GCIEVEGVDDVADFEEVVLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 339 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQAS---MPDNTAAQKVCHLMGINVTDFTRSILTPRIKV-GRDVVQKAQTK 414
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 415 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 494
Cdd:cd14872 311 AQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 495 EQEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE 574
Cdd:cd14872 391 EEALYQSEGVKFEHIDF-IDNQPVLDLIE--KKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 575 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFvadlwkdvdrivgldqMAKMTESSLPSaSKTKKGmfrTVG 654
Cdd:cd14872 468 FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKL----------------IAVLFPPSEGD-QKTSKV---TLG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 655 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAn 734
Cdd:cd14872 528 GQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK- 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 13124875 735 AIPKGFM-DGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14872 607 TIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-771 |
2.23e-178 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 556.31 E-value: 2.23e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 174 ILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSIT----------GELEKQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 244 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDD 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 324 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmpDNTAAQ---KVCHLMGINVTDFTRSILTPR 400
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 401 IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTN 480
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 481 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIE-RPNNPPGVLALLDeECWFPKAT--DKSFVEKL---- 553
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 554 ---------CTEQGSHPKFQKPKQLKDKtEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkdvdr 624
Cdd:cd14890 476 grksgsggtRRGSSQHPHFVHPKFDADK-QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 625 ivgldqmakmteSSLPSASktkkgmfrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGV 704
Cdd:cd14890 542 ------------RSIREVS---------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 705 LEGIRICRQGFPNRIVFQEFRQRYEILAANAipkgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-771 |
3.85e-174 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 544.73 E-value: 3.85e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASShkgkKDTSITgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR----RNNLVT----EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 415 EQADFAVEALAKATYERLFRWILTRVN----KALDKTHRqgasfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNaivySGTQDTLS-----IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlk 570
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 571 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldQMAKMTESSLPSASK----TK 646
Cdd:cd01387 462 PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPRLGKgrfvTM 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 647 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd01387 533 KPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFID 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 13124875 727 RYEILAANAIPKGfMDGKQACILMIKALELDP-NLYRIGQSKIFFR 771
Cdd:cd01387 613 RYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-771 |
4.89e-171 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 535.43 E-value: 4.89e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKK-RHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAvvasshkgKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLM--------KLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDE-------MFQETV 330
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEeleyyrqMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 331 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 410
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 411 AQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 486
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 487 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKP 566
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 567 KqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmakmtesslpsasktk 646
Cdd:cd14897 470 P--GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 647 kgmfrtvgQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14897 522 --------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 13124875 727 RYEILAANAiPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-769 |
7.37e-171 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 535.91 E-value: 7.37e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY------KGKKRHEMPPHIYAIADTAYRSMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 171 --DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 249 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFVPIPAAQDDEMF 326
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 327 QETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-KKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGR 405
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 406 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAS-FLGILDIAGFEIFEVNSFEQLCINYTNEKLQ 484
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 485 QLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSH 560
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEA--RPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 561 PKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADlwkdvdrivgldqmakmtesslp 640
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 641 sasktkkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 13124875 721 FQEFRQRYEILAANAIPKGFMDGKQACILMIKA------LELDPNLYrIGQSKIF 769
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-771 |
1.66e-170 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 536.19 E-value: 1.66e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLavVASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGSG-----VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLsNGFVPIPAAQDDEM--FQETVEAMAIM 336
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYL-NQSDCYTLEGEDEKyeFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 337 GFSEEEQLSILKVVSSVLQLGNIVFKKER-NTDQASMPDNTAAQK-VCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 414
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 415 EQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQGASfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 491 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPkQLK 570
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 571 DkTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLwkdvdriVGLD---------------QMAKMT 635
Cdd:cd01385 468 E-PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDpvavfrwavlraffrAMAAFR 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 636 ESSLPSASKT-------------------KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVL 696
Cdd:cd01385 540 EAGRRRAQRTaghsltlhdrttksllhlhKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVL 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13124875 697 EQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaanaIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd01385 620 RQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-771 |
5.06e-169 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 530.89 E-value: 5.06e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAVVASshkGKKDTSItgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFlSNGFVPIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALSLIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASM--PDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 415
Cdd:cd14903 232 VSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 416 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14903 312 QAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 496 QEEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLcteQGSHPKFQK----PKqlKD 571
Cdd:cd14903 391 QIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKL---SSIHKDEQDviefPR--TS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 572 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrIVGLDQMAKMTESSLPSASKTKKGMFR 651
Cdd:cd14903 462 RTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALTTT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 652 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14903 539 TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 13124875 732 AANAiPKGFMDGKQACILMIKALELD-PNLYRIGQSKIFFR 771
Cdd:cd14903 619 LPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-732 |
5.28e-169 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 531.19 E-value: 5.28e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKgKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL-----VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 254 -----GYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP------------ 316
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 317 ------------IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQ---KV 381
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 382 CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIA 461
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 462 GFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWF 541
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 542 PKATDKSFVEKLCTEQGSHPKFQKPKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 622 -VDRIVGldqmakmtesslpsaSKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLR 700
Cdd:cd14888 550 yLRRGTD---------------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|..
gi 13124875 701 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 732
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL 646
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-771 |
8.13e-168 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 526.84 E-value: 8.13e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVasshkGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANN---RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 260 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSD---LLLEGFNNYTFLSNGFVPIPAAQDD--EMFQETVEAMA 334
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 335 IMGFSEEEQLSILKVVSSVLQLGNIVFK---KERNTDQASM-PDNTAAQKVCHLMGINVTDFtRSILTPRIKVGR-DVVQ 409
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVVTRgETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL--DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 487
Cdd:cd01379 313 RNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 488 NHTMFILEQEEYQREGIEWNFIDFGlDLQPCIE-LIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPkFQKP 566
Cdd:cd01379 393 NQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 567 KqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVadlwkdvdrivgldqmaKMTESSlpsasktk 646
Cdd:cd01379 468 K--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-----------------RQTVAT-------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 647 kgMFRtvgqlY--KEQLGKLMTtlrnTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 724
Cdd:cd01379 521 --YFR-----YslMDLLSKMVV----GQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADF 589
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 13124875 725 RQRYEILA--ANAIPKGfmdGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd01379 590 LKRYYFLAfkWNEEVVA---NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-771 |
1.89e-166 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 523.59 E-value: 1.89e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQETVEAMAIM 336
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 337 GFSEEEQLSILKVVSSVLQLGNIVFKkerNTDQASMPDNTAAQKVCHLMGINVTDFTrSILTPRIKVGR-DVVQKAQTKE 415
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLT-DALTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 416 QADFAVEALAKATYERLFRWILTRVNKALDKthRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 495
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRIKG--KEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 496 QEEYQREGIEWNFIDFgLDLQPCIELIERpnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlkDKTEF 575
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEK---KLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV--AVNNF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmAKMTESSLPSASKTKKgmfRTVGQ 655
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSKHRR---PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 656 LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 13124875 736 IPKGFMDGKqaCILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-771 |
4.29e-163 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 514.69 E-value: 4.29e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEM---PPHIYAIADTAYRSMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 172 QSILCTGESGAGKTENTKKVIQYLAV----VASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATasklAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMF 326
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 327 QETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVCHLMGINVTDFTRSILTPRIK 402
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 403 VGR-DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQ---------GASFLGILDIAGFEIFEVNSFE 472
Cdd:cd14892 319 TARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 473 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFP-KATDKSFVE 551
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 552 KL-CTEQGSHPKFQKPKQLKDktEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkdvdrivgldq 630
Cdd:cd14892 476 IYhQTHLDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 631 makmtesslpsasktkkgmFRTvgqlykeQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRI 710
Cdd:cd14892 536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 711 CRQGFPNRIVFQEFRQRYEILAAN-AIPKGFMDGKQACILMIKALE-----LDPNLYRIGQSKIFFR 771
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-771 |
4.19e-152 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 484.80 E-value: 4.19e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 101 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 177 TGESGAGKTENTKKVIQYLAVVASSHKgkkdtsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 257 VGANIETYLLEKSRAIRQARDERTFHIFYYMIAG--AKEKMRSDLLLEGFnnYTFLSNGFvpipaAQDDEM------FQE 328
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA-----GCKREVqywkkkYDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 329 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFkkERNTDQASMPDNTA---AQKVCHLMGINVTDFTRSiLTPRIKVGR 405
Cdd:cd14889 226 VCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSngwLKAAAGQFGVSEEDLLKT-LTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 406 -DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQG--ASFLGILDIAGFEIFEVNSFEQLCINYTNEK 482
Cdd:cd14889 303 gEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 483 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIerPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK 562
Cdd:cd14889 383 LQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 563 FQKPKQLKDKteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWK-DVDRIVGLDQMAKMTESSLPS 641
Cdd:cd14889 460 YGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 642 ASKTKKgmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVF 721
Cdd:cd14889 538 FNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 13124875 722 QEFRQRYEILAANAIPKGfmdGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14889 615 AEFAERYKILLCEPALPG---TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
2.53e-146 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 469.13 E-value: 2.53e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRH--------EMPPHIYAIADTAYRSMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 170 EDQSILCTGESGAGKTENTKKVIQYLaVVASSHKGKKDTSITGE------------LEKQLLQANPILEAFGNAKTVKND 237
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFL-TQLSQQEQNSEEVLTLTssiratskstksIEQKILSCNPILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 238 NSSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEG---FNNYTFLS-N 312
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKkS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 313 GFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQA--SMPDNTAAQKVCHLMGINVT 390
Cdd:cd14907 240 NCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 391 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL------DKTHRQGASF-LGILDIAGF 463
Cdd:cd14907 320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 464 EIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWF 541
Cdd:cd14907 400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLD--KPPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 542 PKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTeFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkd 621
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 622 vdriVGLDQMAKMTESSLPSASKTKKgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRC 701
Cdd:cd14907 554 ----SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|...
gi 13124875 702 NGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 734
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-771 |
2.56e-142 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 457.20 E-value: 2.56e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERyfSGLI----YTYSGLFCVVVNPYKHLPiysEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 172 QSILCTGESGAGKTENTKKVIQYL---AVVASSHKG-------KKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSR 241
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttrAVGGKKASGqdieqssKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 242 FGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPA 319
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 320 AQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKK----ERNTDQASMPDNTAAQKVCHLMGINVTDFTRS 395
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 396 ILTPRIkVGRDVVQKAQ-TKEQADFAVEALAKATYERLFRWILTRVNKALDKtHRQGASFLGILDIAGFEIFE-VNSFEQ 473
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFEtKNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 474 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELI-ERPNnppGVLALLDEECWFPKATDKSFVEK 552
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPN---GILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 553 LCTEQGSHPKFQKPKQlKDKTE-FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLnASSDKFvadlwkdvdrivgLDQM 631
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLL-ASSAKF-------------SDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 632 AkmtesslpsasktkkgmfrtvgqlykeqlgKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRIC 711
Cdd:cd14891 535 Q------------------------------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 712 RQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIK-ALELDPNLYRIGQSKIFFR 771
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-737 |
1.93e-139 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 448.60 E-value: 1.93e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMY-----------KGKKRHEMPPHIYAIADTAYRSM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAVV------ASSHKGKKDTSITGelekQLLQANPILEAFGNAKTVKND 237
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 238 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEkmrsdlllegfnnytflsngfvpi 317
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 318 pAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTD-QASMPDNTAAQKV------CHLMGINVT 390
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 391 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD----KTHRQGASFLGILDIAGFEIF 466
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmddsSKSHGGLHFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 467 EVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATD 546
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQ--RPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 547 KSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVtsllnassdkfvadlwkdVDriv 626
Cdd:cd14900 450 TTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEA------------------VD--- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 627 gldqmakmtesslpsasktkkgMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLE 706
Cdd:cd14900 509 ----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660 670
....*....|....*....|....*....|.
gi 13124875 707 GIRICRQGFPNRIVFQEFRQRYEILAANAIP 737
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-728 |
1.10e-137 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 447.03 E-value: 1.10e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYK--------GKKRHEMPPHIYAIADTAYRSMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 169 REDQSILCTGESGAGKTENTKKVIQYLAVV-ASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN---GFVPIPAAQDD- 323
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKy 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 324 -EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVCHLMGINVTDFTRSILTP 399
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 400 RIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD--------KTHRQGASFLGILDIAGFEIFEVNSF 471
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 472 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVE 551
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFD--DKSNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 552 KLCTEQGShpkfqkpkqlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkDVDRIVGLDQM 631
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVAIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 632 AKMTESSLPSASKTKKGMFRT--VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIR 709
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650
....*....|....*....
gi 13124875 710 ICRQGFPNRIVFQEFRQRY 728
Cdd:cd14902 618 IARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-771 |
6.32e-137 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 444.40 E-value: 6.32e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPiyseKIVDMYKgkKRHEMP------PHIYAIADTAYRSMLQ------ 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP----GLYDLHK--YREEMPgwtalpPHVFSIAEGAYRSLRRrlhepg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 168 -DREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTS----ITGElekQLLQANPILEAFGNAKTVKNDNSSRF 242
Cdd:cd14895 76 aSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKrrraISGS---ELLSANPILESFGNARTLRNDNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 243 GKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTF--LSNG-- 313
Cdd:cd14895 153 GKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFqyISGGqc 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 314 FVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERntDQASMPDNTAAQKVCHLMGINVTDFT 393
Cdd:cd14895 233 YQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASS--EDEGEEDNGAASAPCRLASASPSSLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 394 -------------------RSILTPR-IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL--------- 444
Cdd:cd14895 311 vqqhldivsklfavdqdelVSALTTRkISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnp 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 445 -DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIELIE 523
Cdd:cd14895 391 nKAANKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 524 RpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNV 603
Cdd:cd14895 470 Q--RPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 604 TSLLNASSDKFVADLWKDVDRIVGldqmAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNH 683
Cdd:cd14895 548 FSVLGKTSDAHLRELFEFFKASES----AELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 684 EKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELdpnlyri 763
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------- 696
|
....*...
gi 13124875 764 GQSKIFFR 771
Cdd:cd14895 697 GKTRVFLR 704
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-771 |
2.70e-136 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 440.92 E-value: 2.70e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAVVASshkGKKDTSITgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFVPIPAAQDDEMFQETVEAMAI 335
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 336 MGFSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKVCHLMGINVTDF-----TRSILT--PRIKVGRDVV 408
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIeealcNRSVVTrnESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 409 QKAQTKeqadfavEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 488
Cdd:cd14904 312 EAEENR-------DALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 489 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCT---EQGSHPKFQK 565
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIRTnhqTKKDNESIDF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 566 PKQlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakMTESSLPSASKT 645
Cdd:cd14904 461 PKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----------APSETKEGKSGK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 646 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 725
Cdd:cd14904 529 GTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELA 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 13124875 726 QRYEILAANAIPKGfmDGKQACILMIKAL-ELDPNLYRIGQSKIFFR 771
Cdd:cd14904 609 TRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-771 |
9.57e-135 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 436.13 E-value: 9.57e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQ--------TEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFV-PIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVCHLMGINvTDFTRSILTPRIKV-GRDVVQKAQTK 414
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 415 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 493
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 494 LEQEEYQREGIEWNFIDfGLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlkDKT 573
Cdd:cd14896 391 QEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 574 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslpsasktkkgmfrTV 653
Cdd:cd14896 466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 654 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 733
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS 607
|
650 660 670
....*....|....*....|....*....|....*...
gi 13124875 734 NAIPkGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14896 608 ERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
64-814 |
3.29e-134 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 441.01 E-value: 3.29e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 64 ENGKKVTVGKDDIQKMNPP-KFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY 142
Cdd:PTZ00014 74 PTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 143 KGKKRHE-MPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAvvaSSHKGKKDTSItgelEKQLLQA 221
Cdd:PTZ00014 154 RDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 222 NPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL 301
Cdd:PTZ00014 227 NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 302 EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF--KKERNTDQASM--PDNTA 377
Cdd:PTZ00014 307 KSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 378 A-QKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKThrQG-ASFL 455
Cdd:PTZ00014 387 VfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPP--GGfKVFI 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 456 GILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALL 535
Cdd:PTZ00014 465 GMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSIL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 536 DEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKtEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFV 615
Cdd:PTZ00014 542 EDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLV 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 616 ADLWKDVdrivgldqmaKMTEsslpsaSKTKKGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLV 695
Cdd:PTZ00014 621 RDLFEGV----------EVEK------GKLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKV 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 696 LEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFF-RTGV 774
Cdd:PTZ00014 683 LIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLkKDAA 762
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 13124875 775 --LAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLT 814
Cdd:PTZ00014 763 keLTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLV 804
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-771 |
5.16e-134 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 435.59 E-value: 5.16e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKkdtsITGElekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE---KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNytflSNGFVPIPAAQDDEM------FQETVEA 332
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 333 MAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSI------------LTPR 400
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 401 IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEifevN----------S 470
Cdd:cd01386 310 GQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGFQ----NpahsgsqrgaT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 471 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPN------------NPPGVLALLDEE 538
Cdd:cd01386 385 FEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdeDRRGLLWLLDEE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 539 CWFPKATDKSFVEKLCTEQG--SHPKFQKPKQLKDKT-EFSIIHYAGK--VDYNASAWLTK-NMDPLNDNVTSLLNASSD 612
Cdd:cd01386 465 ALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 613 KFVAdlwkdvdrivgldqmakmtesslpsasKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRCIIPNH--EKRSGK- 689
Cdd:cd01386 545 ETAA---------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERSt 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 690 ---------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGF-----MDGKQACILMIKALE 755
Cdd:cd01386 594 sspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELD 673
|
730
....*....|....*.
gi 13124875 756 LDPNLYRIGQSKIFFR 771
Cdd:cd01386 674 LEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-757 |
2.58e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 430.87 E-value: 2.58e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYK--GKKRHE-------MPPHIYAIADTAYRSMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 169 REDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSitGELEK-----QLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEG--EELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 244 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRS--------DLLLEGFNNYTFLSNGFV 315
Cdd:cd14908 159 KFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 316 P-IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQK----VCHLMGINVT 390
Cdd:cd14908 239 PdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 391 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVN 469
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 470 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFP-KATDKS 548
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 549 FVEKL--------CTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNA-SAWLTKNMDPLndnvtsllnassdkfvadlw 619
Cdd:cd14908 475 YASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI-------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 620 kdvdrivgldqmakmtesslpsaSKTKKGMFRTvGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQL 699
Cdd:cd14908 535 -----------------------PLTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 700 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnAIPK----GFMDGKQACILMIKALELD 757
Cdd:cd14908 591 RYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKD 651
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-769 |
7.51e-129 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 419.78 E-value: 7.51e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAvvaSSHKGKKDTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKErntDQASMPDntAA----------QKVCHLMGINVTDFTRSILTPRIKVGRDV 407
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 408 VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAsFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 487
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 488 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFqKPK 567
Cdd:cd14876 388 IDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 568 QLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmaKMTesslpsASKTKK 647
Cdd:cd14876 464 KVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV----------VVE------KGKIAK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 648 GMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 727
Cdd:cd14876 528 GSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQ 605
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 728 YEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIF 769
Cdd:cd14876 606 FKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-732 |
1.76e-119 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 393.45 E-value: 1.76e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKR-HEMPPHIYAIADTAYRSMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 175 LCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGfvpiPAAQDDEMFQETVEAMA 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 335 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKV---CHLMGINVTDFTRSILTPRIKVGRD--VVQ 409
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVrtsALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 489
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 490 TMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQL 569
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 570 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtESSLPSASKTKKGM 649
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
...
gi 13124875 730 ILA 732
Cdd:cd14880 623 LLR 625
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-767 |
2.09e-119 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 395.50 E-value: 2.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKR-HEMPPHIYAIADTAYRSMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 177 TGESGAGKTENTKKVIQYLaVVASSHKGKKDTSITG---ELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT 253
Cdd:cd14906 81 SGESGSGKTEASKTILQYL-INTSSSNQQQNNNNNNnnnSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 254 GYIV-GANIETYLLEKSR-AIRQARDERTFHIFYYMIAGAKEKMRSDLLLEG-FNNYTFL--------------SNGFVP 316
Cdd:cd14906 160 DGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 317 IPAAQD-DEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVCHLMGINVTDF 392
Cdd:cd14906 240 HNNKTEsIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 393 TRSILTPRIKVG---------RDVVQKAQTKEqadfaveALAKATYERLFRWILTRVNKALDK----------THRQGAS 453
Cdd:cd14906 320 KQALLNRNLKAGgrgsvycrpMEVAQSEQTRD-------ALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 454 FLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLA 533
Cdd:cd14906 393 FIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 534 LLDEECWFPKATDKSFVEKlCTEQgSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDK 613
Cdd:cd14906 470 LLDDECIMPKGSEQSLLEK-YNKQ-YHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 614 FVADLWkdvdrivgldqmaKMTESSLPSASKTKKGMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAF 693
Cdd:cd14906 548 LKKSLF-------------QQQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNV 613
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 694 LVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSK 767
Cdd:cd14906 614 HVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-771 |
9.27e-113 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 374.53 E-value: 9.27e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERyFSGLIYTYS--GLFCVVVNPYKHLPIYSEKIVDMY-KGKKRHEMPPHIYAIADTAYRSM-LQDREDQSI 174
Cdd:cd14875 1 ATLLHCIKER-FEKLHQQYSlmGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 175 LCTGESGAGKTENTKKVIQYLAVVASSHKGK-KDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-V 252
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDL----------LLEGFNnyTFLSNGfVPIPAAQD 322
Cdd:cd14875 160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgglktaqdykCLNGGN--TFVRRG-VDGKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 323 DEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILtprIK 402
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 403 VGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNE 481
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 482 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTE-QGSH 560
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKRT--GIFSMLDEECNFKGGTTERFTTNLWDQwANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 561 PKFQKPKQLKdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldqmakmteSSLP 640
Cdd:cd14875 470 PYFVLPKSTI-PNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL-----------------STEK 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 641 SASKTKKgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIV 720
Cdd:cd14875 532 GLARRKQ----TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRP 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 721 FQEF-RQRYEILAANAIpKGFMDGK--QACILMIKALE-----LDPNlYRIGQSKIFFR 771
Cdd:cd14875 608 IEQFcRYFYLIMPRSTA-SLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-771 |
4.65e-110 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 366.13 E-value: 4.65e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRH-----EMPPHIYAIADTAYRSMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 173 SILCTGESGAGKTENTKKVIQYLAVVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS--------STDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFQETVE 331
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASkCYDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 332 AMAIMgFSEEEQLSILKVVSSVLQLGNIVFKKERN--TDQASMPDNTAA-QKVCHLMGINVTDFTRSILTPRIKVGRDVV 408
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 409 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 488
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 489 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKlCTEQGSHPKF--QKP 566
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSS-CKSKIKNNSFipGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 567 KQLKdkteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVadlwkdvdrivgldqmaKMTESSLPSASKTK 646
Cdd:cd14886 467 SQCN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-----------------NKAFSDIPNEDGNM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 647 KGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 726
Cdd:cd14886 526 KGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFH 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 13124875 727 RYEILA--ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14886 604 RNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-728 |
3.28e-109 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 366.34 E-value: 3.28e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMY----------KGKKRHEMPPHIYAIADTAYRSMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 168 DREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE---------LEKQLLQANPILEAFGNAKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 239 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAG-----AKEKMRSDLLLEGFNNYTFLSN 312
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 313 GFVPI--PAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 378
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 379 QKVCHLMGINvTDFTRSILTPR--------IKVGRDVVQKAQTKEqadfaveALAKATYERLFRWILTRVNKAL------ 444
Cdd:cd14899 321 TKAAELLGVS-TEALDHALTKRwlhasnetLVVGVDVAHARNTRN-------ALTMECYRLLFEWLVARVNNKLqrqasa 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 445 --------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQ 516
Cdd:cd14899 393 pwgadesdVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 517 PCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTE---QGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLT 593
Cdd:cd14899 472 ACLELFE--HRPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 594 KNMDPLNDNVTSLLNASSDKFVADLWK-DVDRIVGLDQMAKMTESSLPSASKTKKGMFrTVGQLYKEQLGKLMTTLRNTT 672
Cdd:cd14899 550 KNKDSFCESAAQLLAGSSNPLIQALAAgSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATT 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 673 PNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 728
Cdd:cd14899 629 PRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-771 |
5.26e-98 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 333.92 E-value: 5.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFS--------GLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 171 DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 251 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLsngfvpipaaqddemfQET 329
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGDPESTDL----------------RRI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 330 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTA--------AQKVCHLM-------GINVTDFTR 394
Cdd:cd14887 221 TAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 395 SILTPRIK------------------VGRDV--VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHR----- 449
Cdd:cd14887 301 KHLKTVARllglppgvegeemlrlalVSRSVreTRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesd 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 450 --------QGASFLGILDIAGFEIFE---VNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQ 516
Cdd:cd14887 381 sdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 517 PCIELIERPNN----------------------PPGVLALLDEECWFPKATDKSFVEKLCTEQGSHP-------KFQKPK 567
Cdd:cd14887 461 LASTLTSSPSStspfsptpsfrsssafatspslPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNiinsakyKNITPA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 568 QLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkDVDRIVGLDQmakmteSSLPSASKTKK 647
Cdd:cd14887 541 LSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACS---------TYTRLVGSKK------NSGVRAISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 648 gmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 727
Cdd:cd14887 606 ---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRR 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 13124875 728 YEILAANAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 771
Cdd:cd14887 683 YETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-770 |
2.66e-97 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 329.13 E-value: 2.66e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 96 LNEASVLHNLRERYFSGLIYTY---SGLfcVVVNPYKHLPI--------YSEKIVDMYKGKKRHEMPpHIYAIADTAYRS 164
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLPP-HAYDLAARAYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 165 MLQDREDQSILCTGESGAGKTENTKKVI-QYLAVVASSHKGKKdtsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14879 78 MRRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 244 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGF--VPIPA 319
Cdd:cd14879 151 RYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGPG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 320 AQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF--KKERNTDQASMpDNTAA-QKVCHLMGINVTDFtRSI 396
Cdd:cd14879 231 SDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 397 LTPRIK-VGRDVV----QKAQTKEQADfaveALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIF---EV 468
Cdd:cd14879 309 LTYKTKlVRKELCtvflDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 469 NSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIELIERPnnPPGVLALLDEEC-WFP 542
Cdd:cd14879 385 NSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDDQTrRMP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 543 KATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE---FSIIHYAGKVDYNASAWLTKNMDPLndnvtsllnaSSDkFVAdlw 619
Cdd:cd14879 457 KKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN--- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 620 kdvdrivgldqmakmtesslpsasktkkgMFRTVGQLyKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQL 699
Cdd:cd14879 523 -----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQI 572
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 700 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgFMDGKQACILMIKALELDPNLYRIGQSKIFF 770
Cdd:cd14879 573 RSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-771 |
2.18e-94 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 320.99 E-value: 2.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 176 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITgelekqllQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFK--------HVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 255 YIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAA---QDDEMFQETV 330
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREdVSTAersLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 331 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINvTDFTRSILTPRIKVGR-DVVQ 409
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVS-TDELASALTTDIQYFKgDMII 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 410 KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 486
Cdd:cd14878 312 RRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 487 FNHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKLCT 555
Cdd:cd14878 392 INEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLQS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 556 --EQGSHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdri 625
Cdd:cd14878 459 llESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 626 vgldqmAKMTesslpsasktkkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVL 705
Cdd:cd14878 534 ------SKLV----------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVL 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 706 EGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14878 592 EMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-735 |
4.20e-94 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 317.61 E-value: 4.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHempPHIYAIADTAYRSMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE---PHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAvvasshkgkKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 260 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLlegfNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGFS 339
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYKMTCSAMKSLGIANFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 340 EEEQLSIlkvvsSVLQLGNIVFKKERNTDQASmpdNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADF 419
Cdd:cd14898 223 SIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 420 AVEALAKATYERLFRWILTRVNKALDKThrqGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 499
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 500 QREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLcteqgsHPKFQKPKQLKDKTEFSIIH 579
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI------KKYLNGFINTKARDKIKVSH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 580 YAGKVDYNASAWLTKNMDplndnvtsllnassdkfvadlwKDVDRIVGLDQMAkmTESSLPSASKtkkgmfrtvgqLYKE 659
Cdd:cd14898 442 YAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN--DEGSKEDLVK-----------YFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 660 QLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA 735
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
9.61e-88 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 301.16 E-value: 9.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPiysekiVDM--YKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILC 176
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVID------VDIneYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIII 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 177 TGESGAGKTENTKKVIQ-YLAVVasshkgKKDTSITgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd14937 75 SGESGSGKTEASKLVIKyYLSGV------KEDNEIS----NTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 256 IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAI 335
Cdd:cd14937 145 IVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 336 MGFSEEEQlSILKVVSSVLQLGNIVFK---KERNTDQASMPDNT--AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 410
Cdd:cd14937 225 MNMHDMKD-DLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 411 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 490
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 491 MFILEQEEYQREGIEWNFIDFGLDlQPCIELIeRPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKqlK 570
Cdd:cd14937 383 VYEKETELYKAEDILIESVKYTTN-ESIIDLL-RGKT--SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTK--K 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 571 DKTE-FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakMTESslpsasktkKGM 649
Cdd:cd14937 457 DINKnFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSES---------LGR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 650 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYE 729
Cdd:cd14937 518 KNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFE 596
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 13124875 730 ILAANAIPKGFMDGKQACILMIKAlELDPNLYRIGQSKIFFR 771
Cdd:cd14937 597 YLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-758 |
7.81e-79 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 274.68 E-value: 7.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYkhlpiysekivdMYKGKKRH-------EMPPHIYAIADTAYRSMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 173 SILCTGESGAGKTENTKKVIQYLAVVASshkGKKDTsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFdV 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG---GGPET----DAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 253 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETV 330
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 331 EAMAIMG--FseeeqLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSiLTPRIK-VGRDV 407
Cdd:cd14881 222 ACLGILGipF-----LDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 408 VQKAQTKEQADFAVEALAKATYERLFRWILTRVN--KALDKTHRQGAS--FLGILDIAGFEIFEVNSFEQLCINYTNEKL 483
Cdd:cd14881 295 VKSVCDANMSNMTRDALAKALYCRTVATIVRRANslKRLGSTLGTHATdgFIGILDMFGFEDPKPSQLEHLCINLCAETM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 484 QQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIELIErpNNPPGVLALLDEECwFPKATDKSFVEKLCTEQGSHPK 562
Cdd:cd14881 375 QHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNPR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 563 FQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFvadlwkdvdrivgldqmakmtesslpsa 642
Cdd:cd14881 451 LFEAKP-QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF---------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 643 sktkkgMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 722
Cdd:cd14881 502 ------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFK 575
|
650 660 670
....*....|....*....|....*....|....*...
gi 13124875 723 EFRQRYEILAANAIPKGFMDGKQAC--ILMIKALELDP 758
Cdd:cd14881 576 AFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQPP 613
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-723 |
1.66e-78 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 275.63 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHE-------MPPHIYAIADTAYRSMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 171 DQSILCTGESGAGKTENTKKVIQYLavvassHKGKKDTSITgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF------HYIQTDSQMT-ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 251 D---------VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAG-AKEKMRSDLLLEGFNNYTFL---------- 310
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 311 ----------SNGFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKerntdqasmpdntaaqk 380
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 381 VCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-------- 452
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 453 ---SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnnpp 529
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 530 gVLALLDE-----ECWFPKATDKSF-----------VEKLCTEQGSHPKFQK---PKQLKDKTEFSIIHYAGKVDYNASA 590
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFryllnnerqqqLEGKVSYGFVLNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 591 WLTKNMDPLNDNVTSLLNASSDKFVADlwkdvdrivgldqmakmtesslpSASKTKKGMFRTVGQLYKEQLGKLMTTLRN 670
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 13124875 671 TTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 723
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-724 |
2.71e-73 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 259.64 E-value: 2.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVasshkgkkDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 258
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTT--------DLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 259 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN-GFVPIPAAQDDEMFQETVEAMAIMG 337
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 338 FSEEEQLSILKVVSSVLQLGNIVFKKERNtdQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAqtkeqa 417
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 418 dfavEALAKATYERLFRWILTRVNKALDKThrQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 497
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 498 EYQREGIEW-NFIDFGlDLQPCIELIERpnnppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKF-QKPKQlkdkteF 575
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------F 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 576 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDK--FVADLWKDVDRIVG-LDQMAKMTESSLPSASKTKKGMFrT 652
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKylFSRDGVFNINATVAeLNQMFDAKNTAKKSPLSIVKVLL-S 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 653 VGQLYKEQL-----------------------GKLMTTLRNTTP---------NFVRCIIPNHEKRSGKLDAFLVLEQLR 700
Cdd:cd14905 524 CGSNNPNNVnnpnnnsgggggggnsgggsgsgGSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660
....*....|....*....|....*...
gi 13124875 701 CNGVLEGIRICRQGFP----NRIVFQEF 724
Cdd:cd14905 604 SLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-731 |
3.10e-73 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 258.26 E-value: 3.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYkgkkrhemppHIYAIADTAYRSMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 178 GESGAGKTENTKKVIQYLAvvaSSHKGKKDTsitgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTT-------KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 258 GANIE-TYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIM 336
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 337 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTD---QASMPDNTAAQK-VCHLMGINVTDFTrSILTPRIKVGRDVvqkaq 412
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDGTTI----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 413 TKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAsfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 492
Cdd:cd14874 294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 493 ILEQEEYQREGIEWNF-IDFGLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlKD 571
Cdd:cd14874 372 HDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 572 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmakmtesslpSASKTKKGMFR 651
Cdd:cd14874 449 RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--------------------SYSSNTSDMIV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 652 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 731
Cdd:cd14874 509 SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-771 |
7.73e-73 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 257.36 E-value: 7.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 180 SGAGKTENTKKVIQYLAVVAsshKGKKDTSitgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG---DGNRGAT------GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 260 NIETYLLEKSRAIRQARDERTFHIFYYMIAG--AKEKMRsDLLLEGFNNYTFL----SNGFVPIPAAQDD-----EMFQE 328
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLrippEVPPSKLKYRRDDpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 329 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKerNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 408
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 409 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHrqgaSFLG------ILDIAGFEIFEVNSFEQLCINYTNEK 482
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR----AVFGdkysisIHDMFGFECFHRNRLEQLMVNTLNEQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 483 LQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciELIERPNnppGVLALLDEECwfPKATDKSFVekLCTEQGS 559
Cdd:cd14882 386 MQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYI--MDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 560 HPKFQKPKQlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivglDQMAKMtessl 639
Cdd:cd14882 456 HSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM----- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 640 psasktkkgmfRTVGQLYKEQLGKLMTTLRNTTPN----FVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGF 715
Cdd:cd14882 521 -----------RTLAATFRATSLELLKMLSIGANSggthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 716 PNRIVFQEFRQRYEILAANAIPKGFMDgKQACILMIKALELDPnlYRIGQSKIFFR 771
Cdd:cd14882 590 SYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-729 |
5.60e-69 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 248.73 E-value: 5.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 102 LHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIY----------SEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 172 QSILCTGESGAGKTENTKKVIQYLAVVASS----HKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 247
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 248 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKE--KMRSDLLL-EGFNNYTFLSNGFVPIPA-AQDD 323
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMnKCVNEFVMLKQADPLATNfALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 324 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVCHLMGIN 388
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAKLLEVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 389 --VTD---FTRSILTpriKVGRDVVQ--KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQG----AS 453
Cdd:cd14893 324 pvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 454 FLGILDIAGFEIFE--VNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIELIER 524
Cdd:cd14893 401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 525 PnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE------------FSIIHYAGKVDYNASAWL 592
Cdd:cd14893 481 K--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 593 TKNMDPLNDNVTSLLNASSDKfvadlwkdVDRIVGLDQM--------AKMTESSLPSASKTKKGMFR----------TVG 654
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMaaassekaAKQTEERGSTSSKFRKSASSaresknitdsAAT 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13124875 655 QLYKeQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 729
Cdd:cd14893 631 DVYN-QADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-255 |
1.27e-62 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 211.43 E-value: 1.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 121 FCVVVNPYKHLPIYSEKIVD-MYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIvFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 200 SSHKGKKD-------TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 255
Cdd:cd01363 81 FNGINKGEtegwvylTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-769 |
4.39e-55 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 206.61 E-value: 4.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYK-GKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQ---------------LLQANPILEAFGNAKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIhneentdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 244 KFIRINFDvTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDD 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 324 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 377
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 378 AQKV-CHLMGINVTDFTRSILTPRIkVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHR--QGASF 454
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 455 LGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNppGVLAL 534
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 535 LDEECWFPKATDKSFVEKLCTEQGSH-PKFQKPKQLK-DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSD 612
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRnSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 613 KFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQ----LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRS- 687
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 688 GKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgfmDGKQACILMIKALELDPNLYRIGQSK 767
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 13124875 768 IF 769
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
863-1677 |
3.60e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 144.04 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 863 KTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMrVRLAAKKQELEEI-LHEMEARLEEEEDRGQQL 941
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLK---SLERQAEKA-ERYKELKAELRELeLALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 942 QAERKKMAQQmldleeqleeeeaaRQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1021
Cdd:TIGR02168 245 QEELKEAEEE--------------LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1022 AKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDD 1101
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1102 EIAQKNNALKKIRELEGHISDLQ---EDLDSERAARNKA--EKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEdrrERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1177 TVLKKALDEEtrshEAQVQEMRQKHAqAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRV-----------LGQ 1245
Cdd:TIGR02168 471 EEAEQALDAA----ERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVdegyeaaieaaLGG 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1246 AKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHK--------LQNEVESVTGMLNEAEGKAIKLAKDVASLSSQ- 1316
Cdd:TIGR02168 546 RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTeiqgndreILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGv 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1317 -----LQDTQELLQEETRQKLNVS---------------------------TKLRQLEEERNSLQDQLDEEMEAKQNLER 1364
Cdd:TIGR02168 626 lvvddLDNALELAKKLRPGYRIVTldgdlvrpggvitggsaktnssilerrREIEELEEKIEELEEKIAELEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1365 HISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVS 1444
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1445 NLEKKQRKF-DQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKM------LKAEMEDLV 1517
Cdd:TIGR02168 786 ELEAQIEQLkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsediesLAAEIEELE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1518 SSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQ 1597
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-QLELRLEGLEVRIDNLQER 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1598 LHE-YETELEDERKQRALAAAAKKKLEGDLKDLELQADS-------AIKGREEAIKQLRKLQAQMKDFQRELEDARASRD 1669
Cdd:TIGR02168 945 LSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
....*...
gi 13124875 1670 EIFATAKE 1677
Cdd:TIGR02168 1025 EIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1104-1913 |
1.55e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 138.65 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1104 AQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTELEDTLDSTATQQELRAKREQEvtvlkkal 1183
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLEELREELE-------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1184 deETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQE 1263
Cdd:TIGR02168 243 --ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1264 LQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEE 1343
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1344 ERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKL--QDFASTVEALEEGKKRF---QKEIENLTQQYEEKAAAYDKL 1418
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELerlEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1419 EKTKNRLQQELDDLVVDLDNQRQL---VSNLEKKQRKFDQ---LLAEEKNISSKY-----ADERDRAEAEAREKETKAL- 1486
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFsegVKALLKNQSGLSGilgVLSELISVDEGYeaaieAALGGRLQAVVVENLNAAKk 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1487 ---SLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKL 1563
Cdd:TIGR02168 561 aiaFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1564 ------------------------RLEVNMQALKGQFE-RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAA 1618
Cdd:TIGR02168 641 lrpgyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1619 KKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAA 1698
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1699 AERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERS 1778
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1779 TAQKNESARQQLERQNKELRSKLHEMEGAVKskfkstiaALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKE--ILL 1856
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRS--------ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeySLT 952
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1857 QVEDERKMAEQyKEQAEKGNARVKQLKRQLEE-------AEEESQRINANRRKLQRELDEATES 1913
Cdd:TIGR02168 953 LEEAEALENKI-EDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEA 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
971-1705 |
1.16e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 132.49 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 971 LEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSR 1050
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1051 QELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSE 1130
Cdd:TIGR02168 312 ANLERQLEELE-------AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1131 RAARNKAEKQKRDLGEELEALKTELEDTLDSTA-TQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELT 1209
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1210 EQLEQFKRAKANLDKNKQTLEKENADLAG------ELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDK-- 1281
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSlerlqeNLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAlg 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1282 -------VHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQ----- 1349
Cdd:TIGR02168 545 grlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllgg 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1350 ----DQLDEEMEAKQNLERHistLNIQLSDSKKKLQDFASTVEALEEGKKRF--QKEIENLTQQYEEKAAAYDKLEKTKN 1423
Cdd:TIGR02168 625 vlvvDDLDNALELAKKLRPG---YRIVTLDGDLVRPGGVITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALA 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1424 RLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELE 1503
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1504 RTNKMLKAEMEDLvssKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKgqferDLQAR 1583
Cdd:TIGR02168 782 AEIEELEAQIEQL---KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE-----ELSED 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1584 DEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELED 1663
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 13124875 1664 ARASRDEIFATAKEN--------EKKAKSLEADLMQLQEDLAAAERARKQ 1705
Cdd:TIGR02168 934 LEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1052-1882 |
2.92e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.87 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1052 ELEKLKRKLEGDASDfHEQIADLQAQIAELKMQLAKKE-EELQAALARLDDEIAQKNnalKKIRELEGHISDLQEDLDSE 1130
Cdd:TIGR02168 197 ELERQLKSLERQAEK-AERYKELKAELRELELALLVLRlEELREELEELQEELKEAE---EELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1131 RAARNKAEKQKRDLGEELEALKTELEDTldsTATQQELRAKREQEVTVLKKAldeetrshEAQVQEMRQKHAQAVEELTE 1210
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRL---EQQKQILRERLANLERQLEEL--------EAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1211 QLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVE 1290
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1291 SVTGMLNEAEGKAIK-LAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDE---EMEAKQNLERHI 1366
Cdd:TIGR02168 422 EIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqaRLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1367 STLN---IQLSDSKKKLQDFASTVEALEEGKKRFQKEIENL-----------TQQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:TIGR02168 502 EGFSegvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNELGRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1433 VVDLDN------------QRQLVSNLEKKQRKFDQLLAeekNISSKYADERDRAEAEAREKETKALSLA------RALEE 1494
Cdd:TIGR02168 582 KGTEIQgndreilkniegFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdLVRPG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1495 ALEAKEELERTNKML--KAEMEDLVsskddvgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL 1572
Cdd:TIGR02168 659 GVITGGSAKTNSSILerRREIEELE-------EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1573 KGQFERdLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQA 1652
Cdd:TIGR02168 732 RKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1653 QMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAeelasslSGRNALQDEKR 1732
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-------SELEALLNERA 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1733 RLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKF 1812
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1813 KSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQL 1882
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-712 |
8.32e-29 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 126.01 E-value: 8.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 105 LRERYFSGLIYTYSGLFCV-VVNPYKHL------PIYSEKIVDMYKGKKRHE--MPPHIYAIAD---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 160 ----TAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAVVASS--HKGKKDT-SITG-------------------- 212
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPalSKGSEETcKVSGstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 213 --------------------------------------------------------------ELEKQL------------ 218
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 219 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------RDERTFHI 283
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 284 FYYMIAGAK-----EKMRSDLLLEGFN--NYTFLSN------GFVPIPAA--QDDEMFQETVEAMAIMGFSEEEQLSILK 348
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDGIDcsALTYLGRsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 349 VVSSVLQLGNIVFKKERNTDQASMPDN---TAAQKVCHLMGI-NVTDFTRSILTPRIKV--GRDVVQKAQTKEQADFAVE 422
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 423 ALAKATYERLFRWILTRVNKAL----------------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLqql 486
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 487 fnhtmfileqeeYQREGiewNFIDFGLDLQPciELIERPN---------NPPGVLALLDEECWFPKAT----------DK 547
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRP--HLTARDSekdvlfiyeHPLGVFASLEELTILHQSEnmnaqqeekrNK 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 548 SFVEKLCTEQGSHPKfQKPKQLKDKTE----------FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVAD 617
Cdd:cd14894 626 LFVRNIYDRNSSRLP-EPPRVLSNAKRhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCR 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 618 LWKDVDRivgLDQMAKMTESSLPSASKTKKGMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLE 697
Cdd:cd14894 705 MLNESSQ---LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQ 780
|
810
....*....|....*
gi 13124875 698 QLRCNGVLEGIRICR 712
Cdd:cd14894 781 QCRSQRLIRQMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
998-1826 |
3.21e-28 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 124.41 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 998 SKERKLLEERISdlttNLAE-EEEKAKNLTKLK------NKHESMISELEVRLKKEEKSRQELEK----LKRKLEGDASD 1066
Cdd:TIGR02169 152 PVERRKIIDEIA----GVAEfDRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1067 FHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEdldsERAARNKAEKqkrdlgE 1146
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE----EEQLRVKEKI------G 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1147 ELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEElteqleqFKRAKANLDKNK 1226
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE-------YAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1227 QTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDkvhkLQNEVESVTGMLNEAEGKAIKL 1306
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1307 AKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAST 1386
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGT 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1387 VEALEEGKKRFQKEIE--------NLTQQYEEKAAAYDKLEKTK----------NRLQQELDDL--------------VV 1434
Cdd:TIGR02169 527 VAQLGSVGERYATAIEvaagnrlnNVVVEDDAVAKEAIELLKRRkagratflplNKMRDERRDLsilsedgvigfavdLV 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1435 DLDNQRQ-----------LVSNLEKKQRKFDQL--------LAEEKNISSKYADERDRAEAEAREKETKALSLARALEEA 1495
Cdd:TIGR02169 607 EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1496 LEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL--- 1572
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELear 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1573 KGQFERDLQA-RDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQ 1651
Cdd:TIGR02169 767 IEELEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1652 AQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQED-------LAAAERARKQADLEKEELAEELASSLSGR 1724
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKErdeleaqLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1725 NALQDEKRRLEARIAQLEEELEEEQ--GNMEAMSDRVRKATQQAEQLSNELATERSTAQKN----ESARQQLERQNKELR 1798
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRldelKEKRAKLEEERKAIL 1006
|
890 900
....*....|....*....|....*...
gi 13124875 1799 SKLHEMEGAVKSKFKSTIAALEAKIAQL 1826
Cdd:TIGR02169 1007 ERIEEYEKKKREVFMEAFEAINENFNEI 1034
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
829-1606 |
3.81e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.40 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 829 LRNWQWWRLftkvkpLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQ-AETELYAeae 907
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEeLQKELYA--- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 908 emrvrLAAKKQELEEilhemearleeeedRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEI 987
Cdd:TIGR02168 293 -----LANEISRLEQ--------------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 988 LVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDf 1067
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1068 hEQIADLQAQIAELKMQLAKKEEEL---QAALARLDDEIAQKNNALKKIRELEGHIS-------DLQEDLDSERAARNKA 1137
Cdd:TIGR02168 433 -AELKELQAELEELEEELEELQEELerlEEALEELREELEEAEQALDAAERELAQLQarldsleRLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1138 EKQKRDLG-------------EELE-ALKTELEDTLDSTATQQELRAKREQEVtvLKKAldEETRSHEAQVQEMRQKHAQ 1203
Cdd:TIGR02168 512 LKNQSGLSgilgvlselisvdEGYEaAIEAALGGRLQAVVVENLNAAKKAIAF--LKQN--ELGRVTFLPLDSIKGTEIQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1204 AVE-ELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVL--GQAKQEVEHKKKKLEAQVQ---ELQSKCSDGERARAE 1277
Cdd:TIGR02168 588 GNDrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddLDNALELAKKLRPGYRIVTldgDLVRPGGVITGGSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1278 LNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDtqelLQEETRQKLnvsTKLRQLEEERNSLQDQLDEEME 1357
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLR---KELEELSRQISALRKDLARLEA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1358 AKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLD 1437
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1438 NQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLV 1517
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1518 SSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDaKLRLEVNMQAlkgqfeRDLQARDEQNEEKRRQLQRQ 1597
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-RLSEEYSLTL------EEAEALENKIEDDEEEARRR 973
|
....*....
gi 13124875 1598 LHEYETELE 1606
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1566 |
9.17e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.78 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 930
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 931 LEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISD 1010
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 LTTNLAEEE---------EKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFH------EQIADLQ 1075
Cdd:TIGR02168 426 LLKKLEEAElkelqaeleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDslerlqENLEGFS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1076 AQIAELKM-------------QLAKKEEELQAAL-----ARLDDEI------------AQKNNALKKIRELEGHISDLQE 1125
Cdd:TIGR02168 506 EGVKALLKnqsglsgilgvlsELISVDEGYEAAIeaalgGRLQAVVvenlnaakkaiaFLKQNELGRVTFLPLDSIKGTE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1126 dLDSERAARNKAEKQKRDLGEELEALKTELEDTL----------DSTATQQELRAKREQEVTVLKKALDEETRS-----H 1190
Cdd:TIGR02168 586 -IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitgG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1191 EAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSD 1270
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1271 GERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQd 1350
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR- 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1351 qldeemEAKQNLERhistlniQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELD 1430
Cdd:TIGR02168 824 ------ERLESLER-------RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1431 DLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARaleealeakeeleRTNKMLK 1510
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS-------------LTLEEAE 957
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1511 AEMEDLVSSKDDVGKNVHELEKSKRAL-------ETQMEEMKTQLEELEDELQATEDAKLRLE 1566
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1113-1922 |
5.43e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 117.09 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1113 IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEA 1192
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1193 QVQEMRQKhaqaVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAK-QEVEHKKKKLEAQVQELQSKCSDG 1271
Cdd:TIGR02169 245 QLASLEEE----LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1272 ERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQE------ETRQKL-NVSTKLRQLEEE 1344
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaETRDELkDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1345 RNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALeegkkrfQKEIENLTQQYEEKAAAYDKLEKTKNR 1424
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-------ALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1425 LQQELDdlvvdldnqrQLVSNLEKKQRKFDQLLAeEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELER 1504
Cdd:TIGR02169 474 LKEEYD----------RVEKELSKLQRELAEAEA-QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1505 TnkMLKAEMEDLVSSKDDVGKNVHELEKSK---RALETQMEEMKTQLEELEdelQATEDAKLRLEVNMQALKGQFE---- 1577
Cdd:TIGR02169 543 V--AAGNRLNNVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1578 ---RDLQARDEQNEEKRRQLQRQLHEYETELEDE--------RKQRALAAAAKKKLE------GDLKDLELQADSAIKGR 1640
Cdd:TIGR02169 618 yvfGDTLVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsRAPRGGILFSRSEPAelqrlrERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1641 EEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELass 1720
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL--- 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1721 lsgrNALQDEKRRLEARIAQLEEELEEEQGN-MEAMSDRVRKATQQAEQLSNELATERSTAqknESARQQLERQNKELRS 1799
Cdd:TIGR02169 775 ----HKLEEALNDLEARLSHSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYL---EKEIQELQEQRIDLKE 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1800 KLHEMEGAV------KSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAE 1873
Cdd:TIGR02169 848 QIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 13124875 1874 KGNARVKQLKRQLEEAEEESQRInANRRKLQRELDEATESNEAMGrEVN 1922
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVEEEIRALE-PVN 974
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
865-1482 |
8.09e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 865 KERQQKAENELKELEQKhsqLTEEKNLLQE---QLQaetELYAEAEemrvrLAAKKQELEEILHEMEARLEEEEDRGQQL 941
Cdd:COG1196 171 KERKEEAERKLEATEEN---LERLEDILGElerQLE---PLERQAE-----KAERYRELKEELKELEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 942 QAERKKMAQQmldleeqleEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1021
Cdd:COG1196 240 ELEELEAELE---------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1022 AKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDD 1101
Cdd:COG1196 311 RREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1102 EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKreqevtvlkk 1181
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE---------- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1182 aLDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQV 1261
Cdd:COG1196 454 -LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1262 QELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLnVSTKLRQL 1341
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL-VASDLREA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1342 EEERNSLQDQLDEE-------MEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAA 1414
Cdd:COG1196 612 DARYYVLGDTLLGRtlvaarlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13124875 1415 YDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKE 1482
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1326-1922 |
2.06e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1326 EETRQKLN-VSTKLRQLEEERNSLQDQ---------LDEEMEAKQ---------NLERHISTLNIQLSDSKKKLQDFAST 1386
Cdd:COG1196 182 EATEENLErLEDILGELERQLEPLERQaekaeryreLKEELKELEaellllklrELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1387 VEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSK 1466
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1467 YADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKT 1546
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1547 QLEELEDELQATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDL 1626
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEE-EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1627 KDLELQADSA-----IKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATakENEKKAKSLEADLMQLQEDLAAAER 1701
Cdd:COG1196 501 ADYEGFLEGVkaallLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV--EDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1702 ARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQ 1781
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1782 KNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDE 1861
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1862 RKMAEQYKEqaekgnarvkqlkrqLEEAEEESQRINANRRKLQRELDEATESNEAMGReVN 1922
Cdd:COG1196 739 EELLEEEEL---------------LEEEALEELPEPPDLEELERELERLEREIEALGP-VN 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1706 |
2.20e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.08 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 844 LLQVTRQEEEMQAKEDELQKTKERQQKAENELKELE--QKHSQLTEEKNLLQEQLQAETELyaeaEEMRVRLAAKKQELE 921
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQalLKEKREYEGYELLKEKEALERQK----EAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 922 EIlhemearLEEEEDRGQQLQAERKKMAQqMLDLEEQLEEEEAARQKLQLEKVTAEakIKKLEDEILVMDDQNNKLSKER 1001
Cdd:TIGR02169 255 KL-------TEEISELEKRLEEIEQLLEE-LNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1002 KLLEERISDLttnLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLK---RKLEGDASDFHEQIADLQAQI 1078
Cdd:TIGR02169 325 AKLEAEIDKL---LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1079 AELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDt 1158
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1159 ldstaTQQELRAKREQEVTVLKKALDEETRSHE-------------------AQVQEMRQKHAQAVE------------- 1206
Cdd:TIGR02169 481 -----VEKELSKLQRELAEAEAQARASEERVRGgraveevlkasiqgvhgtvAQLGSVGERYATAIEvaagnrlnnvvve 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1207 ---ELTEQLEQFKRAKAN----LDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSK--CSDGERARAE 1277
Cdd:TIGR02169 556 ddaVAKEAIELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTlvVEDIEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1278 L-NDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEM 1356
Cdd:TIGR02169 636 MgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1357 EAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEgkkrfqkEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDL 1436
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1437 DNQRqlvsnLEKKQRKFDQLLAEEKNIsskyaderdRAEAEAREKETKALSLARALEEALEAKeelertnkmLKAEMEDL 1516
Cdd:TIGR02169 789 SHSR-----IPEIQAELSKLEEEVSRI---------EARLREIEQKLNRLTLEKEYLEKEIQE---------LQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1517 VSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQatedaklrlevnmqalkgqferDLQARDEQNEEKRRQLQR 1596
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELER 903
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1597 QLHEYETELEDERKQRALAAAAKKKLEGDLKDLElQADSAIKGREEAIKQLRKLQAQMKDFQRELED-------ARASRD 1669
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYE 982
|
890 900 910
....*....|....*....|....*....|....*..
gi 13124875 1670 EIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
807-1432 |
2.23e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 807 AKRQQQLTAMKVIQRNCAAYLKLRNWQwwrlftkvkplLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLT 886
Cdd:COG1196 212 AERYRELKEELKELEAELLLLKLRELE-----------AELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 887 EEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemearleeeedrgQQLQAERKKMAQQMLDLEEQLEEEEAAR 966
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERL--------------EELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 967 QKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKE 1046
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1047 EKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQED 1126
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1127 LDSERAARNKAEKQK----------------RDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSH 1190
Cdd:COG1196 507 LEGVKAALLLAGLRGlagavavligveaayeAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1191 EAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLgqAKQEVEHKKKKLEAQVQELQSKCSD 1270
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA--VTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1271 GERARAELNDKVHKLQNEVESvtgmlNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQD 1350
Cdd:COG1196 665 GSRRELLAALLEAEAELEELA-----ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1351 QLDEEMEAKQNLERHISTLNIQLSDSKKKLqdfastvealeegkKRFQKEIENL-------TQQYEEKAAAYDKLEKTKN 1423
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELEREL--------------ERLEREIEALgpvnllaIEEYEELEERYDFLSEQRE 805
|
....*....
gi 13124875 1424 RLQQELDDL 1432
Cdd:COG1196 806 DLEEARETL 814
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1201-1929 |
2.96e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 111.69 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1201 HAQAveELTEQLEQFKRAKANLDKNKQTLEKEnaDLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELND 1280
Cdd:TIGR02168 206 ERQA--EKAERYKELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1281 KVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEemeakq 1360
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES------ 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1361 nlerhistLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLvvdLDNQR 1440
Cdd:TIGR02168 356 --------LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL---QQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1441 QLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTnkmLKAEMEDLVSSK 1520
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA---RLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1521 DDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAklrLEVNMQAL---KGQFERDLQARDEQNEEKRRQLQRQ 1597
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRLQAVvveNLNAAKKAIAFLKQNELGRVTFLPL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1598 LHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGR----------EEAIKQLRKLQAQMKDFQRELEDARAS 1667
Cdd:TIGR02168 579 DSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1668 ------RDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEkeelaeelasslsgRNALQDEKRRLEARIAQL 1741
Cdd:TIGR02168 659 gvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE--------------LEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1742 EEELEEEQGNMEAMSDRVRKATQQAEQLSNELatERSTAQKNEsarqqLERQNKELRSKLHEMEgavkskfkSTIAALEA 1821
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKEL--TELEAEIEE-----LEERLEEAEEELAEAE--------AEIEELEA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1822 KIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRR 1901
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
730 740
....*....|....*....|....*...
gi 13124875 1902 KLQRELDEATESNEAMGREVNALKSKLR 1929
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELE 897
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
965-1612 |
1.70e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.87 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 965 ARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLK 1044
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1045 KEEKSRQELEklkrKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQ 1124
Cdd:COG1196 289 EEYELLAELA----RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1125 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEvtvlKKALDEETRSHEAQVQEMRQKHAQA 1204
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1205 VEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQskcSDGERARAELNDKVHK 1284
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA---DYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1285 LQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLER 1364
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1365 HISTLNIqlsdskkklqdfASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVS 1444
Cdd:COG1196 598 GAAVDLV------------ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1445 NLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVG 1524
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1525 KNVHELEKSKRALETQMEEMKTQLEELEDELQATEDaklrleVNMQALKgQFERdLQARDEQNEEKRRQLQRQLHEYET- 1603
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLEREIEALGP------VNLLAIE-EYEE-LEERYDFLSEQREDLEEARETLEEa 817
|
650
....*....|.
gi 13124875 1604 --ELEDERKQR 1612
Cdd:COG1196 818 ieEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1248-1913 |
3.59e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1248 QEVEHKKKKLEAQV------QELQSKcsdGERARAELN-DKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDT 1320
Cdd:COG1196 196 GELERQLEPLERQAekaeryRELKEE---LKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1321 QELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKE 1400
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1401 IENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEARE 1480
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1481 KETKALSLARALEEALEAKEELERtnkmlkaemedlvsskddvgknvhELEKSKRALETQMEEMKTQLEELEDELQATED 1560
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEE------------------------EEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1561 AKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEyetelederkqralaaaakkkLEGDLKDLELQADSAIKGR 1640
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---------------------LIGVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1641 EEAIkqLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADlekeELAEELASS 1720
Cdd:COG1196 548 LQNI--VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD----ARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1721 LSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSK 1800
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1801 LHEMEgavkskfkSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKgnaRVK 1880
Cdd:COG1196 702 EEEEE--------RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELE 770
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 13124875 1881 QLKRQLEE-------AEEESQRINANRRKLQRELDEATES 1913
Cdd:COG1196 771 RLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEA 810
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1146-1740 |
7.02e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1146 EELEALKTELEDTLDSTATQQElRAKREQEvtvLKKALDEetRSHEAQVQEMRQKHAQAvEELTEQLEQFKRAKANLDKN 1225
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAE-KAERYRE---LKEELKE--LEAELLLLKLRELEAEL-EELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1226 KQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIK 1305
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1306 LAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAS 1385
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1386 TVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNL----EKKQRKFDQLLAEEK 1461
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELleelAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1462 NISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELErtnkmLKAEMEDLVSSKDDVGKNVHELEKSK---RALE 1538
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-----LAAALQNIVVEDDEVAAAAIEYLKAAkagRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1539 TQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAA 1618
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1619 KKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAA 1698
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 13124875 1699 AERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQ 1740
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1324-1928 |
4.69e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 104.37 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1324 LQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIEN 1403
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1404 LTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKET 1483
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1484 KALSLARALEEALEAKEELERTNKMLKAEMEDLVSS-----KDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAT 1558
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleeaeLKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1559 EDAKLRLEVNMQALKGQFE--RDLQARDEQNEEKRRQL---QRQLH--------------EYETELE------------- 1606
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDslERLQENLEGFSEGVKALlknQSGLSgilgvlselisvdeGYEAAIEaalggrlqavvve 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1607 -------------DERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMK--------------DFQR 1659
Cdd:TIGR02168 554 nlnaakkaiaflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDN 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1660 ELEDARASR-DEIFATA-----------------------------KENEKKAKSLEADLMQLQEDLAAAERARKQADLE 1709
Cdd:TIGR02168 634 ALELAKKLRpGYRIVTLdgdlvrpggvitggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1710 KEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQ 1789
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1790 LERQNKELRSKLHEMEGAVKSkFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYK 1869
Cdd:TIGR02168 794 LKEELKALREALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 1870 EQAE-------KGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKL 1928
Cdd:TIGR02168 873 SELEallneraSLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
981-1695 |
5.06e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 104.38 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 981 KKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEE-------KSRQEL 1053
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1054 EKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALK-KIRELEGHISDLQEDLDSERA 1132
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1133 ARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVtvlkKALDEETRSHEAQVQEMRQKHAQAVEELT--- 1209
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY----AELKEELEDLRAELEEVDKEFAETRDELKdyr 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1210 EQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEV 1289
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1290 ESVTGMLNEAEGKAIKLAKDVASLSSQLQ----------DTQELLQEETRQKLNVSTKLRQLEEER---------NSLQD 1350
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARaseervrggrAVEEVLKASIQGVHGTVAQLGSVGERYataievaagNRLNN 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1351 -QLDEEMEAKQNlerhistlnIQLSDSKK----------KLQDFASTVEAL-EEGKKRFQKEIENLTQQYE--------- 1409
Cdd:TIGR02169 552 vVVEDDAVAKEA---------IELLKRRKagratflplnKMRDERRDLSILsEDGVIGFAVDLVEFDPKYEpafkyvfgd 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1410 -------EKAAAY-----------DKLEKT------KNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE---KN 1462
Cdd:TIGR02169 623 tlvvediEAARRLmgkyrmvtlegELFEKSgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELrriEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1463 ISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQME 1542
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1543 EMK-----TQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQ----ARDEQNE--EKRRQLQRQLHEYETELEDERKQ 1611
Cdd:TIGR02169 783 DLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeyLEKEIQElqEQRIDLKEQIKSIEKEIENLNGK 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1612 RALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQ 1691
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
....
gi 13124875 1692 LQED 1695
Cdd:TIGR02169 943 DEEI 946
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
977-1556 |
2.17e-20 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 98.55 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 977 EAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEK-------S 1049
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1050 RQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEEL---QAALARLDDEIAQKNNALKKIRELEGHISDLQED 1126
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1127 LDSERAARNKAEKQKRDLGEELEALKTELED----------TLDSTATQ-QELRAKRE----QEVTVLKKALDEETRSHE 1191
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEkqkeleqnnkKIKELEKQlNQLKSEISdlnnQKEQDWNKELKSELKNQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1192 AQVQEMRQ---KHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKC 1268
Cdd:TIGR04523 321 KKLEEIQNqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1269 SDGERARAELNDKVHKLQNEVEsvtgmlneaegkaiKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSL 1348
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKE--------------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1349 QDQLDEemeakqnLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQE 1428
Cdd:TIGR04523 467 ETQLKV-------LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1429 LDDLVVDL--DNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTN 1506
Cdd:TIGR04523 540 ISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 13124875 1507 KMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ 1556
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
851-1705 |
7.29e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 97.35 E-value: 7.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 930
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 931 LEEEEDRGQQLQAERKKMAQQMLDLEEQLeeeeaarQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISD 1010
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKL-------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLK-----------KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIA 1079
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKeleikreaeeeEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1080 ELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTL 1159
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1160 DSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGE 1239
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1240 LRVlgQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQ- 1318
Cdd:pfam02463 552 EVS--ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIl 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1319 DTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQ 1398
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1399 KEIENLTQQYEEKAAAYDKLEktKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEA 1478
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEA--QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1479 REKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAT 1558
Cdd:pfam02463 788 VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEE 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1559 EDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERK--QRALAAAAKKKLEGDLKDLELQADSA 1636
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIeeRIKEEAEILLKYEEEPEELLLEEADE 947
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1637 IKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQ 1705
Cdd:pfam02463 948 KEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1170-1924 |
4.46e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1170 AKREQEVTVLKKALDEETRSHE-AQVQEMRQKHAQAVEELTEQLEQFKRAKaNLDKNKQTLEKENADLAGELRVLGQAKQ 1248
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAfGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1249 eVEHKKKKLEAQVQELQSKCSDGERARAElndkvhKLQNEVEsvtgmlneaEGKAIKLAKDVASLSSQLQDTQELLQEET 1328
Cdd:PTZ00121 1154 -VEIARKAEDARKAEEARKAEDAKKAEAA------RKAEEVR---------KAEELRKAEDARKAEAARKAEEERKAEEA 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1329 RQklnvSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNiqlSDSKKKLQDFASTVEALEEGKKRFQKEIenltQQY 1408
Cdd:PTZ00121 1218 RK----AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEARKADEL----KKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1409 EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQllAEEKNISSKYADERDRAEAEAREKETKALSL 1488
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1489 ARALEEALEAKEELERTNKMLKAEMEdlvsskddvgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVN 1568
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEK----------KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1569 MQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLR 1648
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1649 KLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSL-EADLMQLQEDLAAAERARKQADLEkeelaeelasSLSGRNAl 1727
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDK----------NMALRKA- 1583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1728 QDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNElATERSTAQKNESARQQLERQNKELRSKlhEMEGA 1807
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA--EEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1808 VKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLE 1887
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 13124875 1888 EAE---EESQRINANRRKLQRELDEATESNEAMGREVNAL 1924
Cdd:PTZ00121 1741 EDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1600 |
1.16e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 853 EMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETelyAEAEEMRVRLAAKK--QELEEILHEMEAR 930
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTET---GKAEEARKAEEAKKkaEDARKAEEARKAE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 931 LEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDeiLVMDDQNNKLSKERKLLEERISD 1010
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 lTTNLAEEEEKAKNLTKLKnkhesmiselEVRLKKEEKSRQELEklkRKLEGDASDFHEQIADLQAQIAELKMQLAKKEE 1090
Cdd:PTZ00121 1216 -EARKAEDAKKAEAVKKAE----------EAKKDAEEAKKAEEE---RNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1091 ELQAALARLDDEIAQKNNALKKIRELEGHisdlQEDLDSERAARNKAEKQKRDlGEELEAlKTELEDTLDSTATQQELRA 1170
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKK----AEEAKKADEAKKKAEEAKKK-ADAAKK-KAEEAKKAAEAAKAEAEAA 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1171 KREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAV---EELTEQLEQFKRAKANLDKNKQTLEK--ENADLAGELRVLGQ 1245
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkaDEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1246 AKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMlNEAEGKAIKLAKDVASLSSQLQDTQELLQ 1325
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1326 EETRQKLNVSTKLRQLEEERNSLQDQLDEEM----EAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEI 1401
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1402 ENLTQQYEE----KAAAYDKLEKTKNRlQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAE 1477
Cdd:PTZ00121 1595 EEVMKLYEEekkmKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1478 AREKET--KALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELE-DE 1554
Cdd:PTZ00121 1674 KKKAEEakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDE 1753
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 13124875 1555 LQATEDAKLRLEVNMQALKGQFERDL---QARDEQNEEKRRQLQRQLHE 1600
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKD 1802
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
989-1566 |
3.52e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.25 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 989 VMDDQNNKLS--------KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKrkl 1060
Cdd:PRK02224 181 VLSDQRGSLDqlkaqieeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLE--- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1061 egdasdfhEQIADLQAQIAElkmqlAKKEEElqaalaRLDDEIAQKNNALKkirELEGHISDLQEDLDSERAARNKAEKQ 1140
Cdd:PRK02224 258 --------AEIEDLRETIAE-----TERERE------ELAEEVRDLRERLE---ELEEERDDLLAEAGLDDADAEAVEAR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1141 KrdlgEELEALKTELEDTLDSTATQQElrAKREQEVTVLKKALDEETRSHEAqvQEMRQKHAQAVEELTEQLEQFKRAKA 1220
Cdd:PRK02224 316 R----EELEDRDEELRDRLEECRVAAQ--AHNEEAESLREDADDLEERAEEL--REEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1221 NLDKNKQTLEKENADLAGELrvlgqakqevehkkKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLneAE 1300
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDL--------------GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL--EA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1301 GKAIKLAKDVAslSSQLQDTqelLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQnLERHISTLNIQLSDSKKKL 1380
Cdd:PRK02224 452 GKCPECGQPVE--GSPHVET---IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELI 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1381 QDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE 1460
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1461 KNISSKYADERDRAEAEAREKETkaLSLARALEEALEAKEELERTNKmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQ 1540
Cdd:PRK02224 606 DEIERLREKREALAELNDERRER--LAEKRERKRELEAEFDEARIEE-AREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
570 580
....*....|....*....|....*....
gi 13124875 1541 MEEMKTQLEELE---DELQATEDAKLRLE 1566
Cdd:PRK02224 683 IGAVENELEELEelrERREALENRVEALE 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1167 |
8.37e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 90.50 E-value: 8.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKAENELK-------ELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQ 918
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEqlrkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 919 ELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAA-------RQKLQLEKVTAEAKIKKLEDEILVMD 991
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltllneeAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 992 DQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQI 1071
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1072 ADLQAQIAELKMQLAKKEEELQAALARLDDEIAQK-NNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEA 1150
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDF 1004
|
330
....*....|....*..
gi 13124875 1151 LKTELEDTLDSTATQQE 1167
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1568 |
8.42e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 8.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 849 RQEEEMQAKEDelQKTKERQQKAENELKELEQKHSQltEEKNLlqEQLQAETELYAEAEEmrVRLAAKKQELEEILHEME 928
Cdd:PTZ00121 1188 RKAEELRKAED--ARKAEAARKAEEERKAEEARKAE--DAKKA--EAVKKAEEAKKDAEE--AKKAEEERNNEEIRKFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 929 ARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEA--ARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKE-RKLLE 1005
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKR--KLEGDASDFHEQIADLQAQIAELKM 1083
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1084 --QLAKKEEELQAA-LARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAA---RNKAEKQKRdlGEELEALKTELED 1157
Cdd:PTZ00121 1420 adEAKKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeaKKKAEEAKK--ADEAKKKAEEAKK 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1158 TLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTE--QLEQFKRA--KANLDKNKQTLEKEN 1233
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKKAeeKKKAEEAKKAEEDKN 1577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1234 ADL--AGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAiklakdva 1311
Cdd:PTZ00121 1578 MALrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA-------- 1649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1312 slssqlqdtQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLErhistlniqlsdSKKKLQDFASTVEALE 1391
Cdd:PTZ00121 1650 ---------EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE------------ALKKEAEEAKKAEELK 1708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1392 EGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADER 1471
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1472 DRAEAEAREKETKAL--SLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEE------ 1543
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIfdNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnkea 1868
|
730 740
....*....|....*....|....*.
gi 13124875 1544 -MKTQLEELEDELQATEDAKLRLEVN 1568
Cdd:PTZ00121 1869 dFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
852-1567 |
1.54e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 89.41 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 852 EEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETElyAEAEEMRVRLAAKKQELEEILHEMEARL 931
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEGVLQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 932 eeeedrgqqlQAERKKMAQQMLDLEEQLEEEEAARQKLQLEkvtAEAKIKKLEDEILVMDDQNNKLSKERK-----LLEE 1006
Cdd:pfam15921 198 ----------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1007 RISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKK-EEKSRQELEKLKRKLegdaSDFHEQIADLQAQIAELKMQL 1085
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1086 AKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQ 1165
Cdd:pfam15921 341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1166 QELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQ 1245
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1246 AKQEVEHKKKKLEAQVQELQSKcsdgeRARAELN-DKVHKLQNEVESVTGMLNEAEGKAIKLA---KDVASLSSQLQDTQ 1321
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKL-----RSRVDLKlQELQHLKNEGDHLRNVQTECEALKLQMAekdKVIEILRQQIENMT 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1322 ELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSD---SKKKL-----------QDFASTV 1387
Cdd:pfam15921 576 QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlelEKVKLvnagserlravKDIKQER 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1388 EALEEGKKRFQKEIENLTQQYEEKAAAY----DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQ-RKFDQLLAEEKN 1462
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDgHAMKVAMGMQKQ 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1463 ISSKyaderdRAEAEAREKETKALSLARALEEALEAKEELERTNkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQME 1542
Cdd:pfam15921 736 ITAK------RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNK--LSQELSTVATEKNKMAGELEVLRSQERRLKEKVA 807
|
730 740 750
....*....|....*....|....*....|..
gi 13124875 1543 EMKT-------QLEELEDELQATEDAKLRLEV 1567
Cdd:pfam15921 808 NMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1399 |
1.73e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.35 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKnllqEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 930
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 931 LEEEEDRGQQLQAERKKMaqqmldleeqleeeeaarQKLQlEKVTAEAKIKKLEDEILvmdDQNNKLSKERKLLEERISD 1010
Cdd:PRK03918 268 IEELKKEIEELEEKVKEL------------------KELK-EKAEEYIKLSEFYEEYL---DELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 LTTNLAEEEEKAKNLTKLKNKHESM---ISELEVRLKKEEKSRQ---ELEKLKRKLEGdasdfhEQIADLQAQIAEL--- 1081
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELekrLEELEERHELYEEAKAkkeELERLKKRLTG------LTPEKLEKELEELeka 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1082 KMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSE---------RAARNKAEKQKRDLGEELEALK 1152
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelleeyTAELKRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1153 TELEDTLDSTATQQELRakREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELT--------------EQLEQFKRA 1218
Cdd:PRK03918 480 KELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklkgeikslkkelEKLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1219 KANLDKNKQTLEKENADLAGELRVLG-QAKQEVEHKKKKLEAQVQELQSkCSDGERARAELNDKVHKLQNEVESVTGMLN 1297
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELA 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1298 EAEGKAIKLAKDVASLSSQLqdTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTlniqLSDSK 1377
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAK 710
|
570 580
....*....|....*....|..
gi 13124875 1378 KKLQDFASTVEALEEGKKRFQK 1399
Cdd:PRK03918 711 KELEKLEKALERVEELREKVKK 732
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1192-1928 |
2.81e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.59 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1192 AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEK--ENADLAGELRVLGQAKQEVE-----HKKKKLEAQVQEL 1264
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEgyellKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1265 QSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDvaslssqlqdtqellqeetrQKLNVSTKLRQLEEE 1344
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--------------------EQLRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1345 RNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNR 1424
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1425 LQQELDDLVVDLDnqrQLVSNLEKKQRKFDQLLAEEKNISSKYADerdrAEAEAREKETKALSLARALEEALEAKEELER 1504
Cdd:TIGR02169 383 TRDELKDYREKLE---KLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1505 TNKMLKAEMEDLVSSKDDvgknvheLEKSKRALETQMEEMKTQLEELEDELQATED-------AKLRLEVNMQALKGQF- 1576
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYD-------LKEEYDRVEKELSKLQRELAEAEAQARASEErvrggraVEEVLKASIQGVHGTVa 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1577 --------------------------ERDLQARDEQNEEKRRQLQRQlheyeTELEDERKQRALAAAAKKKLEG------ 1624
Cdd:TIGR02169 529 qlgsvgeryataievaagnrlnnvvvEDDAVAKEAIELLKRRKAGRA-----TFLPLNKMRDERRDLSILSEDGvigfav 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1625 DLKDLELQADSAIK------GREEAIKQLRKL--QAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDL 1696
Cdd:TIGR02169 604 DLVEFDPKYEPAFKyvfgdtLVVEDIEAARRLmgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1697 AAAERArkqadlekeelaeelasslsgRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATE 1776
Cdd:TIGR02169 684 EGLKRE---------------------LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1777 RSTAQKNESARQQLERQNKELRSKLHEMEgAVKSKFKSTIAALEAKIAQLE--------EQVEQEAREKQAATKSLKQKD 1848
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKL 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1849 KKLKEILLQVEDERKMAEQY-----------KEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAM 1917
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQridlkeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
810
....*....|.
gi 13124875 1918 GREVNALKSKL 1928
Cdd:TIGR02169 902 ERKIEELEAQI 912
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
851-1392 |
3.68e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.17 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDelQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEIlhemear 930
Cdd:PRK02224 193 KAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL------- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 931 leeeEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLqlekvTAEAKIKKLEDEILvmDDQNNKLSKERKLLEERISD 1010
Cdd:PRK02224 264 ----RETIAETEREREELAEEVRDLRERLEELEEERDDL-----LAEAGLDDADAEAV--EARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 LTTNLAEEEEKAKNLTKlknkhesMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEE 1090
Cdd:PRK02224 333 CRVAAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1091 ELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNK----------AEKQKRDLGEELEALKTELEDTLD 1160
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1161 STATQQELRAKREQEVTVLKKALDEETRSHEAQ--VQEMRQKHAQAVEELTEQLEQFKRAKANLD-------KNKQTLEK 1231
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIERLEERRedLEELIAERRETIEEKRERAEELRERAAELEaeaeekrEAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1232 ENADLAGELRVLGQAKQEVEHKKKKLEAqVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVA 1311
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1312 slSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQ---LDEEMEAKQNL-ERHistlnIQLSDSKKKLQDFASTV 1387
Cdd:PRK02224 645 --EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELrERR-----EALENRVEALEALYDEA 717
|
....*
gi 13124875 1388 EALEE 1392
Cdd:PRK02224 718 EELES 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
875-1481 |
6.79e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 875 LKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMaqqmld 954
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 955 LEEQLEEEEAARQKLQLEKVtaEAKIKKLEDEIlvmddqnnklskerKLLEERISDLTTNLAEEEEKAKNLTKLKNKHES 1034
Cdd:PRK03918 231 KELEELKEEIEELEKELESL--EGSKRKLEEKI--------------RELEERIEELKKEIEELEEKVKELKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1035 MIsELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAALARLDDEIAQKNNALKKIR 1114
Cdd:PRK03918 295 YI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1115 ELEGH--------ISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTatqQELRaKREQEVTVLKKALDEE 1186
Cdd:PRK03918 373 ELERLkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1187 TRsheaqvQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQS 1266
Cdd:PRK03918 449 HR------KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1267 KCSDGERARAELNdKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKL-NVSTKLRQLEE-- 1343
Cdd:PRK03918 523 KAEEYEKLKEKLI-KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPfy 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1344 -ERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRF-QKEIENLTQQYEEKAAAYDKLEKT 1421
Cdd:PRK03918 602 nEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAE 681
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1422 KNRLQQELDDLVVDLDNQRQLVSNLEKKQR---KFDQLLAEEKNISSKYADERDRAEAEAREK 1481
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKeleKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1185-1707 |
6.90e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1185 EETRSHEAqVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENadlagelrvlgQAKQEVEhkkkKLEAQVQEL 1264
Cdd:PRK02224 200 EEKDLHER-LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE-----------ERREELE----TLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1265 QSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEE 1344
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1345 RNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEgkkrfqkEIENLTQQYEEKAAAYDKLEKTKNR 1424
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1425 LQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIS-------SKYADERDRAEaEAREKETKALSLARALEEALE 1497
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAGKCPEcgqpvegSPHVETIEEDR-ERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1498 AKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALK---G 1574
Cdd:PRK02224 496 ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1575 QFERDLQARDEQNE--EKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDL-ELQADSAIKGREEAIKQLRKLQ 1651
Cdd:PRK02224 576 ELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrERKRELEAEFDEARIEEAREDK 655
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1652 AQMKDFQRELEDA----RASRDEIFAT--AKENE-KKAKSLEADLMQLQEDLAAAERARKQAD 1707
Cdd:PRK02224 656 ERAEEYLEQVEEKldelREERDDLQAEigAVENElEELEELRERREALENRVEALEALYDEAE 718
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1036-1611 |
7.92e-17 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 87.20 E-value: 7.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1036 ISELEVRLKKEEKSRQELEK-LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALAR----LDDEI------- 1103
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAeLNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQhgafLDADIetaaadq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1104 -------AQKNNALKKIRELEGHISDLQEDLDSERAA---RNKAE----KQKRD-LGEELEALKTELEDTLDstATQQEL 1168
Cdd:pfam12128 347 eqlpswqSELENLEERLKALTGKHQDVTAKYNRRRSKikeQNNRDiagiKDKLAkIREARDRQLAVAEDDLQ--ALESEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1169 RAKREQEVTVLKKALDE-ETRSHEAQVqemRQKHAQAVEELTEQLEQFKRAkanLDKNKQTLEKENA---DLAGELRVLG 1244
Cdd:pfam12128 425 REQLEAGKLEFNEEEYRlKSRLGELKL---RLNQATATPELLLQLENFDER---IERAREEQEAANAeveRLQSELRQAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1245 QAKQEVEHKKKKLEAQVQELQSKCsdgERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKlakdvaslSSQLQDTQ--- 1321
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSAL---DELELQLFPQAGTLLHFLRKEAPDWEQSIGKVIS--------PELLHRTDldp 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1322 ELLQEETRQKLNV-STKLR--------------QLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAST 1386
Cdd:pfam12128 568 EVWDGSVGGELNLyGVKLDlkridvpewaaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1387 VEALEEGKKRFQKEIENLTQQYEEK-AAAYDKLEKTKNRLQQELDDLVVDL-----DNQRQLVSNLEKKQRKFdQLLAEE 1460
Cdd:pfam12128 648 LKNARLDLRRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAQLKQLDKKHqawleEQKEQKREARTEKQAYW-QVVEGA 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1461 KNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELerTNKMLKAEMEDLVSSKDDVGKNVHELEK-------- 1532
Cdd:pfam12128 727 LDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD--VIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqet 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1533 ---SKRALETQMEEMKTQLEELEDELQA-TEDAKLRLEVNMQALKGQfeRDLQARDEQNEEKRRQLQRQLHEYETELEDE 1608
Cdd:pfam12128 805 wlqRRPRLATQLSNIERAISELQQQLARlIADTKLRRAKLEMERKAS--EKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
...
gi 13124875 1609 RKQ 1611
Cdd:pfam12128 883 QAQ 885
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
828-1482 |
1.56e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 828 KLRNWQWWRLFTKVKPLLQVTRQ---EEEMQAKEDELQKTKERQqKAEnELKELEQKHsQLTEEKNLLQEQLQAEtELYA 904
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKK-KAD-EAKKAEEKK-KADEAKKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 905 EAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQ-AERKKMAQQMlDLEEQLEEEEAARQKLQLEKVTAEAK---- 979
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKkkae 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 980 -IKKLEDEILVMDDQNNKLSKERKLLEE-RISDLTTNLAEEEEKAKnltKLKNKHESMISELEVRLKKEEKSRQELEKLK 1057
Cdd:PTZ00121 1402 eDKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1058 RKLEGDASDFHEQIADLQAQIAELKM--QLAKKEEELQAALARLDDEIAQKNNALKKIRELEGhisdlQEDLDSERAARN 1135
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK-----AEEKKKADELKK 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1136 KAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQA-----VEELTE 1210
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkkAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1211 QLEQFKRAKANLDKNKQTLEKENADlaGELRVLGQAKQEVEHKKKKLEAQVQElqskcsDGERARAELNDKVHKLQNEVE 1290
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEE--NKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAE 1705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1291 SVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQklnvSTKLRQLEEERNSLQdQLDEEMEAKQNLERHISTLN 1370
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIA-HLKKEEEKKAEEIRKEKEAV 1780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1371 IQLSDSKKKLQDFASTVEALEEGKKRFQKEIENltqqyEEKAAAYdkLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQ 1450
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEG-----GKEGNLV--INDSKEMEDSAIKEVADSKNMQLEEADAFEKHK 1853
|
650 660 670
....*....|....*....|....*....|..
gi 13124875 1451 RKFDQLLAEEKNISSKYADERDRAEAEAREKE 1482
Cdd:PTZ00121 1854 FNKNNENGEDGNKEADFNKEKDLKEDDEEEIE 1885
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1697 |
2.00e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 85.87 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 850 QEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQlqaetelYAEAEEMRVRLAAKKQELEEIlHEMEA 929
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-------ENELDPLKNRLKEIEHNLSKI-MKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 930 RLEEEEDRGQQLQAERKKMAQQMLDLEE-QLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERI 1008
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1009 S--DLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDA-------SDFHEQIADLQAQIA 1079
Cdd:TIGR00606 350 GrlQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktaaqlcADLQSKERLKQEQAD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1080 ELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDL---QEDLDSERAARNKAEKQK--RDLGEELEALKTE 1154
Cdd:TIGR00606 430 EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIlelDQELRKAERELSKAEKNSltETLKKEVKSLQNE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1155 LEDTLDSTATQQELRAKREQEVTVLKKALdEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKA------NLDKNKQT 1228
Cdd:TIGR00606 510 KADLDRKLRKLDQEMEQLNHHTTTRTQME-MLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQledwlhSKSKEINQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1229 LEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAElNDKVHKLQNEVESVTGMLNEAEGKAIKLAK 1308
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-ESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1309 DVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVE 1388
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1389 ALEEGKKRFQKEIENLTQQYEEKaaayDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYA 1468
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1469 DERDRAEAEarEKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHEleksKRALETQMEEMKTQL 1548
Cdd:TIGR00606 824 VQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEV 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1549 EELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQ-------------------------RQLHEYET 1603
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNdikekvknihgymkdienkiqdgkdDYLKQKET 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1604 ELEDERKQRALAAAAKKKLEGDLKDLELQADSAiKGREEAIKQ---LRKLQAQMKDFQRELEDARASRDEIFATAKENEK 1680
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ-KIQERWLQDnltLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEH 1056
|
890
....*....|....*..
gi 13124875 1681 KAKSLEADLMQLQEDLA 1697
Cdd:TIGR00606 1057 QKLEENIDLIKRNHVLA 1073
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
842-1689 |
3.78e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.02 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 842 KPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEK---------NLLQEQLQAETELYAEAEEMRVR 912
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEeyllyldylKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 913 LAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEIlvmdd 992
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL----- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 993 qnNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASdFHEQIA 1072
Cdd:pfam02463 331 --KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS-EEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1073 DLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK 1152
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1153 TELEDTLDSTATQQELRAKREQEVtvlKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKE 1232
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKV---LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1233 NADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNE--AEGKAIKLAKDV 1310
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKdtELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1311 ASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERhistLNIQLSDSKKKLQDFASTVEAL 1390
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ----LEIKKKEQREKEELKKLKLEAE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1391 EEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADE 1470
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQE 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1471 RDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEE 1550
Cdd:pfam02463 801 EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELE 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1551 LEDELQATEDAKLRLEVNMQALkgqfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLE 1630
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKEL----EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1631 LQADSAIKGrEEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADL 1689
Cdd:pfam02463 957 EEEERNKRL-LLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1050-1611 |
8.40e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.81 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1050 RQELEKLKRKLE--GDASDFHEQIADLQAQIAELKMQLA--------KKEEELQAALARLDDEIAQknnALKKIRELEGH 1119
Cdd:COG4913 241 HEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAalrlwfaqRRLELLEAELEELRAELAR---LEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1120 ISDLQEDLDSERAARNKAEkqkrdlGEELEALKTELEDTLDSTATQQELRAKREQEVtvlkKALDEETRSHEAQVQEMRQ 1199
Cdd:COG4913 318 LDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALL----AALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1200 KHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLgqakqevEHKKKKLEAQVQELQskcsdgERARAELN 1279
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-------ERRKSNIPARLLALR------DALAEALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1280 DKVHKL----------------QNEVESVTG-----MLNEAEgkaikLAKDVASLSSQLQDTQEL--------LQEETRQ 1330
Cdd:COG4913 455 LDEAELpfvgelievrpeeerwRGAIERVLGgfaltLLVPPE-----HYAAALRWVNRLHLRGRLvyervrtgLPDPERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1331 KLNVSTKLRQLEEERNSLQDQLDEEM---------EAKQNLERHistlniqlsdskkklqDFASTVEAL-EEGKKRFQKE 1400
Cdd:COG4913 530 RLDPDSLAGKLDFKPHPFRAWLEAELgrrfdyvcvDSPEELRRH----------------PRAITRAGQvKGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1401 IEN-LTQQYEEKAAAYDKLEktknRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAR 1479
Cdd:COG4913 594 DRRrIRSRYVLGFDNRAKLA----ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1480 ----EKETKALSLARALEEAleakeelertnkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDEL 1555
Cdd:COG4913 670 iaelEAELERLDASSDDLAA-------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 1556 QATEDAKLRLEVnmQALKGQFERDLQARDEQneEKRRQLQRQLHEYETELEDERKQ 1611
Cdd:COG4913 737 EAAEDLARLELR--ALLEERFAAALGDAVER--ELRENLEERIDALRARLNRAEEE 788
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
833-1432 |
9.49e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 83.48 E-value: 9.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 833 QWWRLFTKVKPLLQVTRQEEEMQAkedELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVR 912
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHT---ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 913 LAAKKQELEEILHEMEARLEEEEDRgQQLQAERKKMaQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDD 992
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLT-QKLQSLCKEL-DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 993 QNNKLSKERKLLEERISDLTTNLAEEEEKAKNltklknkhesmiseLEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIA 1072
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQT--------------KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1073 DLQAqiaelKMQLAKKEEELQAALARLDDEIAQKNNALKKIR----ELEGHISDLQEDLDSERAARNKAEKQKRDLGEEL 1148
Cdd:TIGR00618 512 HPNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1149 EALKTELEDTLDSTATQQELR-----AKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLD 1223
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEdmlacEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1224 KNKQTLEKENADLA------GELRVLGQAKQEVEHKKKKLeaqvQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLN 1297
Cdd:TIGR00618 667 IRVLPKELLASRQLalqkmqSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1298 EAEGKAIKLAKDV--ASLSSQLQDTQELLQEETRqklnvSTKLRQLEEERNSLQDQLDEEMEAKQNLERHIST-----LN 1370
Cdd:TIGR00618 743 QSLKELMHQARTVlkARTEAHFNNNEEVTAALQT-----GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeipsdED 817
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1371 IQLSDSKKKLQDFASTVEALEEgKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEE-KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
887-1455 |
1.18e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.43 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 887 EEKNLLQ--EQLQAETELYAEAEEMRVRLAAKKQELEEIlhemearleeeEDRGQQLQAERKKMAQQmlDLEEQLEEEEA 964
Cdd:COG4913 219 EEPDTFEaaDALVEHFDDLERAHEALEDAREQIELLEPI-----------RELAERYAAARERLAEL--EYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 965 ARQKLQLekvtAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEeeKAKNLTKLKNKHESMISELEVRLK 1044
Cdd:COG4913 286 AQRRLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1045 KEEKSRQELEKLKRKLEGDASDFheqiADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNAL----KKIRELEGHI 1120
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreleAEIASLERRK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1121 SDLQEDLDSERAARNKAEKQKRD----LGEELEALKTELE---------------------------DTLDSTATQQELR 1169
Cdd:COG4913 436 SNIPARLLALRDALAEALGLDEAelpfVGELIEVRPEEERwrgaiervlggfaltllvppehyaaalRWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1170 -------AKREQEVTVLKKALDE--ETRSHEAQ---VQEMRQKHAQAVEELTEQLEQFKRA--KANLDKNKQTL-EKENA 1234
Cdd:COG4913 516 yervrtgLPDPERPRLDPDSLAGklDFKPHPFRawlEAELGRRFDYVCVDSPEELRRHPRAitRAGQVKGNGTRhEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1235 DLAGELRVLGqakQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEgkaikLAKDVASLS 1314
Cdd:COG4913 596 RRIRSRYVLG---FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-----DEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1315 SQLQDtqelLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGK 1394
Cdd:COG4913 668 REIAE----LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1395 KRFQkeIENLTQQYEEkAAAYDKLEKTKNRLQQELDDLVVDLDNQRQlvsNLEKKQRKFDQ 1455
Cdd:COG4913 744 RLEL--RALLEERFAA-ALGDAVERELRENLEERIDALRARLNRAEE---ELERAMRAFNR 798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1315-1928 |
1.67e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1315 SQLQDT-QELLQ----EETRQKL-NVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHiSTLNiqlsdskkklqdfastve 1388
Cdd:PRK02224 149 SDRQDMiDDLLQlgklEEYRERAsDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLH-ERLN------------------ 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1389 ALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRL---QQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISS 1465
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHeerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1466 KYADERD--RAEAEAREKETKALSLARALEEALEAKeelertnkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEE 1543
Cdd:PRK02224 290 ELEEERDdlLAEAGLDDADAEAVEARREELEDRDEE---------LRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1544 MKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERkqralaaaakkkle 1623
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIE-ELRERFGDAPVDLGNAEDFLEELREERDELR-------------- 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1624 GDLKDLElqadSAIKGREEAIKQLRKLQAQMK--DFQRELEDArasrdEIFATAKENEKKAKSLEADLMQLQEDLAAAER 1701
Cdd:PRK02224 426 EREAELE----ATLRTARERVEEAEALLEAGKcpECGQPVEGS-----PHVETIEEDRERVEELEAELEDLEEEVEEVEE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1702 ARKQADLEKEELaeelasslSGRNALQDEKRRLEARIAQLEEEleeeqgnMEAMSDRVRKATQQAEQLSNELATERSTAQ 1781
Cdd:PRK02224 497 RLERAEDLVEAE--------DRIERLEERREDLEELIAERRET-------IEEKRERAEELRERAAELEAEAEEKREAAA 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1782 KNESARQQLERQNKELRSKLHEMEGAVKSKfkSTIAALEAKIAQLEEQVEqEAREKQAAtkslkqkdkklkeiLLQVEDE 1861
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-RLREKREA--------------LAELNDE 624
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1862 RKmaEQYKEQAEkgnaRVKQLKRQ-----LEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKL 1928
Cdd:PRK02224 625 RR--ERLAEKRE----RKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1036-1484 |
1.68e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.04 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1036 ISELEVRLKKEEKSRQELEKLK------RKLEGDASDFHEQIADLQAQIAELKMQLAKKE-EELQAALARLDDEI----A 1104
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRelaeryAAARERLAELEYLRAALRLWFAQRRLELLEAElEELRAELARLEAELerleA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1105 QKNNALKKIRELEGHISD--------LQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:COG4913 317 RLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1177 TVLKKALDEETRSHEAQVQEMRQKHaqavEELTEQLEQFKRAKANLDKN--------KQTLEKENADL--AGEL------ 1240
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARllalrdalAEALGLDEAELpfVGELievrpe 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1241 ---------RVLG--------------QAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNE--------- 1288
Cdd:COG4913 473 eerwrgaieRVLGgfaltllvppehyaAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKphpfrawle 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1289 -----------VESVTGMlnEAEGKAIKLA-----------KDVASLSSQL----QDTQELLQEETRQKLNVSTKLRQLE 1342
Cdd:COG4913 553 aelgrrfdyvcVDSPEEL--RRHPRAITRAgqvkgngtrheKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1343 EERNSLQDQLDEeMEAKQNLERHISTLN---IQLSDSKKKLQDFASTVEALEEGKKRF---QKEIENLTQQYEEKAAAYD 1416
Cdd:COG4913 631 ERLEALEAELDA-LQERREALQRLAEYSwdeIDVASAEREIAELEAELERLDASSDDLaalEEQLEELEAELEELEEELD 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1417 KLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE-----------KNISSKYADERDRAEAEAREKETK 1484
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaveRELRENLEERIDALRARLNRAEEE 788
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1054-1908 |
2.15e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 82.47 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1054 EKLKRKLEgdasDFHEQIADLQAQIAELKMQLAKKEEELQAALARLD---DEIAQKNNALKKIRELEghiSDLQEDLdse 1130
Cdd:pfam15921 74 EHIERVLE----EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQtklQEMQMERDAMADIRRRE---SQSQEDL--- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1131 raarnkaEKQKRDLGEELEALKTELEDTLDSTATQQElrakreqevtvlkkALDEETRSHEAQVQEMRQkhaqaveeLTE 1210
Cdd:pfam15921 144 -------RNQLQNTVHELEAAKCLKEDMLEDSNTQIE--------------QLRKMMLSHEGVLQEIRS--------ILV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1211 QLEQFKRAKANLDKNKQTLEKENADLAGElRVLGQAKQEVEHKKKKL---EAQVQELQSKCSDgeraRAELndkvhKLQN 1287
Cdd:pfam15921 195 DFEEASGKKIYEHDSMSTMHFRSLGSAIS-KILRELDTEISYLKGRIfpvEDQLEALKSESQN----KIEL-----LLQQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1288 EVESVTGMLNEAEGKAIKLAKDVASLSSQ---LQDTQELLQEETRQKlnVSTKLRQLEEERNSLQDQLDEEMEAKQNLER 1364
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQ--NSMYMRQLSDLESTVSQLRSELREAKRMYED 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1365 HISTLNIQLSDSKKKLqdfastVEALEEgKKRFQKEIENLTQQYEEKAAAYDKLEKTKNrLQQELDDLVVDLDNQRQLvs 1444
Cdd:pfam15921 343 KIEELEKQLVLANSEL------TEARTE-RDQFSQESGNLDDQLQKLLADLHKREKELS-LEKEQNKRLWDRDTGNSI-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1445 NLEKKQRKFDqllaeEKNIsskyadERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEdlvSSKDDVG 1524
Cdd:pfam15921 413 TIDHLRRELD-----DRNM------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE---STKEMLR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1525 KNVHELEKSKRALETQ---MEEMKTQLEELEDELQAT--EDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLH 1599
Cdd:pfam15921 479 KVVEELTAKKMTLESSertVSDLTASLQEKERAIEATnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1600 EYETELEDERKQRAlaaaakkklegDLKDLELQadsaiKGREEAIKQLRK--LQAQMKDFQRELEDARASRDEIFATAKE 1677
Cdd:pfam15921 559 EKDKVIEILRQQIE-----------NMTQLVGQ-----HGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1678 NEKKAKSLEADLMQLQEdlAAAERARKQADlekeelaeelasslsgrnaLQDEKRRLEARIAQLEEELEEEQGNMEAMSD 1757
Cdd:pfam15921 623 LEARVSDLELEKVKLVN--AGSERLRAVKD-------------------IKQERDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1758 RVRKATQQAEQLSNELATERSTAQKN-ESARQQLERQNKelrSKLHEMEGAVKSKFKST-----IAALEAKIAQLEEQVE 1831
Cdd:pfam15921 682 NFRNKSEEMETTTNKLKMQLKSAQSElEQTRNTLKSMEG---SDGHAMKVAMGMQKQITakrgqIDALQSKIQFLEEAMT 758
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1832 QEAREKQAatksLKQKDKKLKEILLQVEDER-KMA---EQYKEQAEKGNARVKQLKRQLEEAEE---------ESQRINA 1898
Cdd:pfam15921 759 NANKEKHF----LKEEKNKLSQELSTVATEKnKMAgelEVLRSQERRLKEKVANMEVALDKASLqfaecqdiiQRQEQES 834
|
890
....*....|
gi 13124875 1899 NRRKLQRELD 1908
Cdd:pfam15921 835 VRLKLQHTLD 844
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1074-1915 |
3.37e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 81.94 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1074 LQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT 1153
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1154 ELEDTLDSTATQQELRAKREQEvtvlKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKEN 1233
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDL----LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1234 ADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSkcsdgeraraelndkvhKLQNEVESVTGMLNEAEGKAIKLAKDVASL 1313
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEK-----------------ELKKEKEEIEELEKELKELEIKREAEEEEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1314 SSQLQdtqelLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEG 1393
Cdd:pfam02463 359 EELEK-----LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1394 KKrfQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDR 1473
Cdd:pfam02463 434 EE--EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1474 AEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED 1553
Cdd:pfam02463 512 LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1554 ELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQA 1633
Cdd:pfam02463 592 KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1634 DSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDlaAAERARKQADLEKEEL 1713
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK--INEELKLLKQKIDEEE 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1714 AEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKAtqQAEQLSNELATERSTAQKNESARQQLERQ 1793
Cdd:pfam02463 750 EEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA--QEEELRALEEELKEEAELLEEEQLLIEQE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1794 NKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQaATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAE 1873
Cdd:pfam02463 828 EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL-LLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 13124875 1874 KGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
870-1805 |
4.87e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 81.63 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 870 KAENELKELEQKHSQLTEEKnllQEQLQAETELYAEAEEMRVRLAAKKQELEeilhEMEARLEEEEDRGQQLQAERKKMA 949
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEH---QMELKYLKQYKEKACEIRDQITSKEAQLE----SSREIVKSYENELDPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 950 QQMldleeqleeeeaarqklqlekvtaeAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEeekaknLTKLK 1029
Cdd:TIGR00606 259 HNL-------------------------SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLY 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1030 NKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARL---------D 1100
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1101 DEIAQKNNALKKIRELEGH-------ISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDtldstaTQQELRAKRE 1173
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEaktaaqlCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK------KQEELKFVIK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1174 QEVTVLKKA-----LDEETRSHEAQVQEMRQKhaQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQ 1248
Cdd:TIGR00606 462 ELQQLEGSSdrileLDQELRKAERELSKAEKN--SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1249 EVEHKKKKLEaQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEET 1328
Cdd:TIGR00606 540 LTKDKMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1329 RQKLNVSTKL------RQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIE 1402
Cdd:TIGR00606 619 EQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1403 NLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRqlvSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKE 1482
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ---SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1483 T--KALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKD--DVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAT 1558
Cdd:TIGR00606 776 TimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1559 EDAKLRLEVNMQALKGQferdlQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIK 1638
Cdd:TIGR00606 856 QEQIQHLKSKTNELKSE-----KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1639 GREEAIKqlrKLQAQMKDFQRELEDARASRDEIFATAKEN-EKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEEL 1717
Cdd:TIGR00606 931 SKETSNK---KAQDKVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI 1007
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1718 ASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKEL 1797
Cdd:TIGR00606 1008 DTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHF 1087
|
....*...
gi 13124875 1798 RSKLHEME 1805
Cdd:TIGR00606 1088 KKELREPQ 1095
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1028-1681 |
8.03e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.45 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1028 LKNKHESMISELEVRLKK-------EEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAK---KEEELQAALA 1097
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTiknelknKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1098 RLDDEI----AQKNNALKKIRELE--------------GHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTL 1159
Cdd:TIGR04523 107 KINSEIkndkEQKNKLEVELNKLEkqkkenkknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1160 DSTATQQELRAKREQEVTVLKKaldeetrsheaqvqeMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGE 1239
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSNLKK---------------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1240 LRVLGQAKQEVEHKKKKLEAQVQELQS---KCSDGERARAELNDKVHKLQNEVESvtGMLNEAEGKAIKLAKDVASLSSQ 1316
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1317 LQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKR 1396
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1397 FQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEA 1476
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1477 EAREKETKALSLARAleealeakeelertNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ 1556
Cdd:TIGR04523 490 ELKSKEKELKKLNEE--------------KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1557 ATEDAKLRLEVNMQALKgqferdLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQ---A 1633
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEE------LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEnekL 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 13124875 1634 DSAIKGREEAIKQLRKLQAQMKDfqrELEDARASRDEIFATAKENEKK 1681
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQEVKQIKE---TIKEIRNKWPEIIKKIKESKTK 674
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1085-1671 |
1.10e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1085 LAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLdseraarNKAEKQKRDLGEELEALKTELEDtLDSTAT 1164
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-------NEISSELPELREELEKLEKEVKE-LEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1165 QQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKhaqaVEELTEQLEQFKRAKAnldknkqtLEKENADLAGELRVLG 1244
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKE--------KAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1245 QAKQEVEHKKKKLEAQVQELQSKCSDGEraraELNDKVHKLQNEVESVTGMLNEAEGKAiKLAKDVASLSSQLQDTQELL 1324
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1325 QEETRQKLNvsTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKK-----LQDFASTVEALEEGKKRFQK 1399
Cdd:PRK03918 382 TGLTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1400 EIENLTqqyEEKAAAYDKLEKTKNRLqqelddlvVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAR 1479
Cdd:PRK03918 460 ELKRIE---KELKEIEEKERKLRKEL--------RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1480 EKETKALSLaraleealeaKEELERTNKMLKaEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMK-TQLEELEDELQAT 1558
Cdd:PRK03918 529 KLKEKLIKL----------KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKEL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1559 E----------DAKLRLEVNMQALKGQFERDLQARDEQNEEKRR--QLQRQLHEYETELEDERKQRALAAAAKKKLEgdL 1626
Cdd:PRK03918 598 EpfyneylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRleELRKELEELEKKYSEEEYEELREEYLELSRE--L 675
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 13124875 1627 KDLELQADSAIKGREEAIKQLRKLQAQ---MKDFQRELEDARASRDEI 1671
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEEleeREKAKKELEKLEKALERV 723
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1135-1876 |
1.54e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 79.63 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1135 NKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKRE---QEVTVLKKALDEETRSHEA--QVQEMRQKHAQAVEELT 1209
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAElltLRSQLLTLCTPCMPDTYHErkQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1210 EQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELqsKCSDGERARAELNDKVHKLQNEV 1289
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1290 ESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRqklnvstkLRQLEEERNSLQDQLDEEMEakqnLERHISTL 1369
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQQHT----LTQHIHTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1370 NIQLSDSKKKLQDFASTVEAL--EEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQelddlvVDLDNQRQLVSNLE 1447
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCA------AAITCTAQCEKLEK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1448 KKQRKFDQLLAEEKNisskyaDERDRAEAEAREKETKALSLARALEEALEAKEELERTNKmLKAEMEDLVSSKDDVGK-- 1525
Cdd:TIGR00618 459 IHLQESAQSLKEREQ------QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-PNPARQDIDNPGPLTRRmq 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1526 ----NVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKgqferdlqardEQNEEKRRQLQRQLHEY 1601
Cdd:TIGR00618 532 rgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK-----------EDIPNLQNITVRLQDLT 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1602 ETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMK-DFQRELEDARASRDEIFATAKENEK 1680
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQL 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1681 KAKSLEADLMQLQEDLAAAErarkQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVR 1760
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLA----QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1761 KATQQAEQLSNELAT-ERSTAQKNESARQQLERQNKELRSKLHEM---EGAVKSKFKSTIAALEA---KIAQLEEQVEQE 1833
Cdd:TIGR00618 757 KARTEAHFNNNEEVTaALQTGAELSHLAAEIQFFNRLREEDTHLLktlEAEIGQEIPSDEDILNLqceTLVQEEEQFLSR 836
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 13124875 1834 AREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGN 1876
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1277-1927 |
3.69e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.14 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1277 ELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEM 1356
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1357 EAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDL 1436
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1437 DNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDL 1516
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1517 VSSK---DDVGKNVHELEKSKRALETQ-----MEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQ---FERDLQARDE 1585
Cdd:TIGR04523 277 EQNNkkiKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisqLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1586 QNEEKRRQLQrqlhEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDAR 1665
Cdd:TIGR04523 357 ENSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1666 ASRDEIFATAKENEKKAKSLEADLMQLQedlaaaerarkqadlekeelaeelasslSGRNALQDEKRRLEARIAQLEEEL 1745
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLD----------------------------NTRESLETQLKVLSRSINKIKQNL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1746 EEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKS-KFKSTIAALEAKIA 1824
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEID 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1825 QLEEQVEQEAREKqaatKSLKQKDKKLKEILLQVEDERKmaEQYKEQAEKGnARVKQLKRQLEEAEEESQRINANRRKLQ 1904
Cdd:TIGR04523 565 EKNKEIEELKQTQ----KSLKKKQEEKQELIDQKEKEKK--DLIKEIEEKE-KKISSLEKELEKAKKENEKLSSIIKNIK 637
|
650 660
....*....|....*....|...
gi 13124875 1905 RELDEATESNEAMGREVNALKSK 1927
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNK 660
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
3.70e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 68.23 E-value: 3.70e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 13124875 31 AAKRLVWVPSEKQGFEAASIKEEKGDEVVVELvENGKKVTVGKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1640-1929 |
1.08e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1640 REEAIKQLRK--------------LQAQMKDFQRELEDARasrdeifaTAKENEKKAKSLEADLMQLQEDLAAAERARKQ 1705
Cdd:COG1196 174 KEEAERKLEAteenlerledilgeLERQLEPLERQAEKAE--------RYRELKEELKELEAELLLLKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1706 ADLEKEELAeelasslsgRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELateRSTAQKNES 1785
Cdd:COG1196 246 AELEELEAE---------LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI---ARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1786 ARQQLERQNKELRSKLHEMEGAvkskfKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMA 1865
Cdd:COG1196 314 LEERLEELEEELAELEEELEEL-----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1866 EQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLR 1929
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
920-1664 |
1.19e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.70 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 920 LEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLeeeeaarQKLQLEKvTAEAKIKKLEDEilVMDDQNNKLSK 999
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRRESQ--SQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1000 ERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISEL-EVRLKKEEKSRQEL------------------EKLKRKL 1060
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIrSILVDFEEASGKKIyehdsmstmhfrslgsaiSKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1061 EGDASDFHEQIADLQAQIAELKmqlAKKEEELQAALARLDDEIAQknnalkKIRELEGHISDLQEDLDSERAARNKAEKQ 1140
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALK---SESQNKIELLLQQHQDRIEQ------LISEHEVEITGLTEKASSARSQANSIQSQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1141 krdlgeeLEALKtelEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTE---QLEQFKR 1217
Cdd:pfam15921 301 -------LEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEartERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1218 AKANLDKNkqtLEKENADLAGELRVLGQAKQE--------------VEHKKKKLEAQVQELQskcsdgeRARAELNDKVH 1283
Cdd:pfam15921 371 ESGNLDDQ---LQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitIDHLRRELDDRNMEVQ-------RLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1284 KLQNEVESVTGMLneaEGKAIKLAKdVASLSSQLQDTQELL----QEETRQKLNVSTKLRQLEEERNSLQDQldeemeak 1359
Cdd:pfam15921 441 ECQGQMERQMAAI---QGKNESLEK-VSSLTAQLESTKEMLrkvvEELTAKKMTLESSERTVSDLTASLQEK-------- 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1360 qnlERHISTLNIQLSDSKK----KLQDFAStVEALEEGKKRFQKEIENLTQQYEEKaaaydklEKTKNRLQQELDDLVVD 1435
Cdd:pfam15921 509 ---ERAIEATNAEITKLRSrvdlKLQELQH-LKNEGDHLRNVQTECEALKLQMAEK-------DKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1436 LDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMED 1515
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1516 LV----SSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAtedAKLRLEVNMQALKGQFERDLQA------RDE 1585
Cdd:pfam15921 658 LLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS---AQSELEQTRNTLKSMEGSDGHAmkvamgMQK 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1586 QNEEKRRQ---LQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELE 1662
Cdd:pfam15921 735 QITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALD 814
|
..
gi 13124875 1663 DA 1664
Cdd:pfam15921 815 KA 816
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1122-1929 |
1.84e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1122 DLQEDLDSERAARNKAEKQKRDLGEELEALKTE--LEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQ 1199
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEeaKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1200 KHAQAVEELTEQLEQFKRAK-----ANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERA 1274
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEevrkaEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1275 RAELNDKVHKLQNEVESVTGMLNEAEGKAiklakdvaslsSQLQDTQELLQEETRQKlnvSTKLRQLEEERNSlqdqldE 1354
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKA-----------EEARKADELKKAEEKKK---ADEAKKAEEKKKA------D 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1355 EMEAKQNLERHISTLNIQLSDSKKK---LQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDD 1431
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1432 LVVDLDNQRQLVSNLEKKQRKFDQLlaEEKNISSKYADE-RDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLK 1510
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADEL--KKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1511 AEMEDlvSSKDDVGKNVHELEKSKRALETQMEEMKTQleelEDELQATEDAKLRLEVNMQAlkgqferdlqardeqnEEK 1590
Cdd:PTZ00121 1464 KKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKK----ADEAKKAAEAKKKADEAKKA----------------EEA 1521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1591 RRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQmkdfqrELEDARASRDE 1670
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE------EAKKAEEARIE 1595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1671 IFATAKENEKKAKSLEADlmQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQG 1750
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAK--KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1751 NMEAmsDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKElrsklheMEGAVKSKFKSTIAALEAKIAQLEEQV 1830
Cdd:PTZ00121 1674 KKKA--EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK-------AEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1831 EQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEA 1910
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDS 1824
|
810
....*....|....*....
gi 13124875 1911 TESNEAMGREVNALKSKLR 1929
Cdd:PTZ00121 1825 KEMEDSAIKEVADSKNMQL 1843
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
846-1591 |
5.74e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 74.70 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEaeemrVRLAAKKQELEEILH 925
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERE-----LSKAEKNSLTETLKK 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 926 EMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARqklqlEKVTAEAKIKKledeilvmddqnnklskerklLE 1005
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK-----DKMDKDEQIRK---------------------IK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAElkmql 1085
Cdd:TIGR00606 556 SRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD----- 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1086 AKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAA-------RNKAEKQKRDLGEELEALKTELEDT 1158
Cdd:TIGR00606 631 VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrVFQTEAELQEFISDLQSKLRLAPDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1159 LDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELteqleqfKRAKANLDKNKQTLEKENA---- 1234
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI-------QRLKNDIEEQETLLGTIMPeees 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1235 --DLAGELRVLGQAKQEVEHKKKKLEAQVQELQSkcSDGERARAELNDKVHKLQNEVESVTgmlneaegkaiklakdvas 1312
Cdd:TIGR00606 784 akVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQHELDTVV------------------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1313 lsSQLQDTQELLQEETRQKLNVSTKLRQLEEERNslqdQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEE 1392
Cdd:TIGR00606 843 --SKIELNRKLIQDQQEQIQHLKSKTNELKSEKL----QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1393 GKKRFQKEIENLTQQYEEkaaaydklekTKNRLQQELDDLVVDLDNQRQLVSNLEKK--QRKFDQLLAEEKNISSKYADE 1470
Cdd:TIGR00606 917 FLEKDQQEKEELISSKET----------SNKKAQDKVNDIKEKVKNIHGYMKDIENKiqDGKDDYLKQKETELNTVNAQL 986
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1471 RDraEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEkskralETQMEEMKTQLEE 1550
Cdd:TIGR00606 987 EE--CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMG------QMQVLQMKQEHQK 1058
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 13124875 1551 LEDELQATEDAKLRLEVNMQALKGQ---FERDLQARDEQNEEKR 1591
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQFRDAEEK 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1203-1938 |
9.25e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1203 QAVEELTEQLEQFKRAKANLDKnkqtlEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKcsDGERARAELNDKV 1282
Cdd:COG4913 225 EAADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1283 HKLQNEVEsvtgmlneaegkaiKLAKDVASLSSQLQDTQELLQEETRQKLNVST-KLRQLEEERNSLQDQLDEEMEAKQN 1361
Cdd:COG4913 298 EELRAELA--------------RLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1362 LERHISTLNIQLSDSKkklQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldnqRQ 1441
Cdd:COG4913 364 LEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-------ER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1442 LVSNLEKKQRKFDQLLAEEKNISS------------KYADERDRAEAEA------------REKETKALSLARaleeaLE 1497
Cdd:COG4913 434 RKSNIPARLLALRDALAEALGLDEaelpfvgelievRPEEERWRGAIERvlggfaltllvpPEHYAAALRWVN-----RL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1498 AKEELERTNKmLKAEMEDLVSSKDDVGKNVHELE-KSKRALETQMEEMKTQLE----ELEDELQATEDAkLRLEVNMQAL 1572
Cdd:COG4913 509 HLRGRLVYER-VRTGLPDPERPRLDPDSLAGKLDfKPHPFRAWLEAELGRRFDyvcvDSPEELRRHPRA-ITRAGQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1573 KGQFERDLQARDEQ-------NEEKRRQLQRQLHEYETELEDERKQRalaaaakkklegdlkdlelqadSAIKGREEAIK 1645
Cdd:COG4913 587 GTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERL----------------------EALEAELDALQ 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1646 QLRKLQAQMKDFQRELEDARASRDEIfaTAKENEKKAksLEA---DLMQLQEDLAAAERARKQADLEkeelaeelassls 1722
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVASAEREI--AELEAELER--LDAssdDLAALEEQLEELEAELEELEEE------------- 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1723 gRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKA-TQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKL 1801
Cdd:COG4913 708 -LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1802 HEMEGAV---KSKFKS-------TIAALEAKIAQLEEQVEQEAREKQAATKSLKQK--DKKLKEILLQVEDERKMAEQyk 1869
Cdd:COG4913 787 EELERAMrafNREWPAetadldaDLESLPEYLALLDRLEEDGLPEYEERFKELLNEnsIEFVADLLSKLRRAIREIKE-- 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1870 eqaekgnaRVKQLKRQLEEAE---------EESQRINANRRKLQRELDEATESNEAMGRE--------VNALKSKLRGPP 1932
Cdd:COG4913 865 --------RIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEE 936
|
....*.
gi 13124875 1933 PQETSQ 1938
Cdd:COG4913 937 EESDRR 942
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
848-1230 |
9.39e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 848 TRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhem 927
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 928 eARLEEEEDRGQQLQAERK-----------KMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDeILVMDDQNNK 996
Cdd:PRK02224 436 -RTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIER 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 997 LSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESmiselevrlKKEEKsrqeleklkrklEGDASDFHEQIADLQA 1076
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEA---------EAEEK------------REAAAEAEEEAEEARE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1077 QIAELKMQLAKKEEELQaalarlddeiaqknnALKKIRELEGHISDLQEDLDS---ERAARNKAEKQKRDLGEELEALKT 1153
Cdd:PRK02224 573 EVAELNSKLAELKERIE---------------SLERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERKR 637
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1154 ELEDTLDSTATqQELRAKREQEVTVLKKAlDEETRSHEAQVQEMrQKHAQAVEELTEQLEQFKRAKANLDKNKQTLE 1230
Cdd:PRK02224 638 ELEAEFDEARI-EEAREDKERAEEYLEQV-EEKLDELREERDDL-QAEIGAVENELEELEELRERREALENRVEALE 711
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
839-1577 |
1.24e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.47 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 839 TKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELE-QKHSQLTEEKNLLQEQLQAETEL------YAEAEEMRV 911
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEeellakKKLESERLS 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 912 RLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMD 991
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 992 DQNNKLSKERKLLEERISDLTTNLAEEEEKA-----KNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASD 1066
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERsqkesKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1067 FHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDseRAARNKAEKQKRDLGE 1146
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD--KATLEADEDDKRAKVV 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1147 ELEALKTELEDTLDSTATQQELRAKreqevtvLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNK 1226
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRK-------GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1227 QTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQN--EVESVTGMLNEAEGKAI 1304
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeeKEEEKSELSLKEKELAE 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1305 KLAKDVASLSSQLQDTQELLQEETRQKLNvstKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLqDFA 1384
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALE---EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL-AEE 854
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1385 STVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIS 1464
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1465 SKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEM 1544
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
730 740 750
....*....|....*....|....*....|...
gi 13124875 1545 KTQLEELEDELQATEDAKLRLEVNMQALKGQFE 1577
Cdd:pfam02463 1015 TCQRLKEFLELFVSINKGWNKVFFYLELGGSAE 1047
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
801-1359 |
2.82e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 72.46 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 801 LARKAFAKRQQQ---LTAMKVIQRNCaaylKLRNWQWWRLFTKVKPLLQVTRQE--EEMQAKEDELQKTKERQQKAENEL 875
Cdd:pfam15921 283 LTEKASSARSQAnsiQSQLEIIQEQA----RNQNSMYMRQLSDLESTVSQLRSElrEAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 876 KELEQKHSQLTEEKNLLQEQLQA--------ETELYAEAEEMRvRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKK 947
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQNK-RLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 948 MAQQMLDLEEQLEEEEAARQKlQLEKV---TAEAKIKKLEDEILVMDDQNNKLSKERKllEERISDLTTNLAEEEE--KA 1022
Cdd:pfam15921 438 MKSECQGQMERQMAAIQGKNE-SLEKVsslTAQLESTKEMLRKVVEELTAKKMTLESS--ERTVSDLTASLQEKERaiEA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1023 KN--LTKLKnkhesmiSELEVRLkkeeksrQELEKLKRklEGDasdfheQIADLQAQIAELKMQLAKKE---EELQAALA 1097
Cdd:pfam15921 515 TNaeITKLR-------SRVDLKL-------QELQHLKN--EGD------HLRNVQTECEALKLQMAEKDkviEILRQQIE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1098 RLDDEIAQKNNALKKIR----ELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALktELEDTLDSTATQQELRAKRE 1173
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVKLVNAGSERLRAVKD 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1174 ---------QEVTVLKKALDEETRSHEAQVQEMRQKhAQAVEELTEQLE-QFKRAKANLDKNKQTLEKENADLAGELRVL 1243
Cdd:pfam15921 651 ikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNK-SEEMETTTNKLKmQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1244 GQAKQEVEHKKkkleAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQlqdTQEL 1323
Cdd:pfam15921 730 MGMQKQITAKR----GQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ---ERRL 802
|
570 580 590
....*....|....*....|....*....|....*.
gi 13124875 1324 LQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAK 1359
Cdd:pfam15921 803 KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1290 |
2.95e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 840 KVKPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQE 919
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 920 LEEIlhemearleeeedrgqqlqAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVtaEAKIKKLEDEILVMDDQNNKLSK 999
Cdd:PRK03918 354 LEEL-------------------EERHELYEEAKAKKEELERLKKRLTGLTPEKL--EKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1000 ERKLLEERISDLTTNLaEEEEKAKNLTKLKNK------HESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIAD 1073
Cdd:PRK03918 413 RIGELKKEIKELKKAI-EELKKAKGKCPVCGRelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1074 LQAQIAELKMqlAKKEEELQAALARLDDEIAQKNNAL-----KKIRELEGHISDLQEDLDSERAARNKA---EKQKRDLG 1145
Cdd:PRK03918 492 ESELIKLKEL--AEQLKELEEKLKKYNLEELEKKAEEyeklkEKLIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1146 EELEALKTELEDTLDSTATQQELRAKR--------------EQEVTVLKKALDEETRSHEaQVQEMRQKHAQAVEELTEQ 1211
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKElepfyneylelkdaEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1212 LEQFKRA-----KANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSK---CSDGERARA---ELND 1280
Cdd:PRK03918 649 LEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAkkeLEKLEKALErveELRE 728
|
490
....*....|
gi 13124875 1281 KVHKLQNEVE 1290
Cdd:PRK03918 729 KVKKYKALLK 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
769-1354 |
5.10e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 769 FFRTGVLahleEERDL--KITDVIMAFQAMCRgylARKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQwwRLFTKVKPLLQ 846
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 847 VTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQL-----QAETELYAEAEEMRVRLAAKKQELE 921
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 922 EILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKE- 1000
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARl 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1001 ---RKLLEERISDLTTNL---------AEEEEK--------------------------AKNLTKLKNKHEsmISELEVR 1042
Cdd:COG4913 443 lalRDALAEALGLDEAELpfvgelievRPEEERwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGR--LVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1043 LKKEEKSRQELEK--LKRKLEGDASDFHEQIADL---------------------------------------------- 1074
Cdd:COG4913 521 TGLPDPERPRLDPdsLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspeelrrhpraitragqvkgngtrhekddrrrirs 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1075 --------QAQIAELKMQLAKKEEELQAALARLdDEIAQKNNALKKIRELEGHISDLQ-EDLDSERAARnkaekqkrdlg 1145
Cdd:COG4913 601 ryvlgfdnRAKLAALEAELAELEEELAEAEERL-EALEAELDALQERREALQRLAEYSwDEIDVASAER----------- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1146 eELEALKTELEDTLDSTATQQELRAKREQevtvLKKALDEetrsHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKN 1225
Cdd:COG4913 669 -EIAELEAELERLDASSDDLAALEEQLEE----LEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1226 KQTLEKE-NADLAGELRVLGQAKQEvEHKKKKLEAQVQELQSKcsdGERARAELNDKVHKLQNEVESVTGMLneaeGKAI 1304
Cdd:COG4913 740 EDLARLElRALLEERFAAALGDAVE-RELRENLEERIDALRAR---LNRAEEELERAMRAFNREWPAETADL----DADL 811
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1305 KLAKDVASLSSQLQDT---------QELLQEETRQklNVSTKLRQLEEERNSLQDQLDE 1354
Cdd:COG4913 812 ESLPEYLALLDRLEEDglpeyeerfKELLNENSIE--FVADLLSKLRRAIREIKERIDP 868
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1006-1707 |
5.70e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMIS-ELEVRLKKEEKSRQELEKLKRKLEgdasDFHEQIADLQAQIAELKMQ 1084
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLWFAQRRLE----LLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1085 LAKKEEELQAALARLDD-EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLG--------------EELE 1149
Cdd:COG4913 311 LERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalrAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1150 ALKTELEDtldstatqqelrakreqevtvLKKALDEETRSHEAQVQEMRQKHaqavEELTEQLEQFKRAKANLDKN---- 1225
Cdd:COG4913 391 ALLEALEE---------------------ELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARllal 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1226 ----KQTLEKENADL--AGEL---------------RVLG--------------QAKQEVEHKKKKLEAQVQELQSKCSD 1270
Cdd:COG4913 446 rdalAEALGLDEAELpfVGELievrpeeerwrgaieRVLGgfaltllvppehyaAALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1271 GERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKdVASLsSQLQD-----TQELL--QEETRQKLNVSTKLRQ--- 1340
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRFDYVC-VDSP-EELRRhpraiTRAGQvkGNGTRHEKDDRRRIRSryv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1341 -----------LEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEgkkrfQKEIENLTQQYE 1409
Cdd:COG4913 604 lgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1410 EKAAAYDKLEktknRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQllaeeknisskyadERDRAEAEAREKETKALSLA 1489
Cdd:COG4913 679 RLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEK--------------ELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1490 RaleeaLEAKEELERTNKMLKAEMEDLVsskddvgknvheLEKSKRALETQMEEMKTQLEELEDELQATedaklrlevnM 1569
Cdd:COG4913 741 D-----LARLELRALLEERFAAALGDAV------------ERELRENLEERIDALRARLNRAEEELERA----------M 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1570 QALKGQFE---RDLQARDEQNEEKRRQLQRQ----LHEYETELEDERKQRalaaaakkkLEGDLKDLELQADSAIKGREE 1642
Cdd:COG4913 794 RAFNREWPaetADLDADLESLPEYLALLDRLeedgLPEYEERFKELLNEN---------SIEFVADLLSKLRRAIREIKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1643 AIKQL------------RKLQ--------AQMKDFQRELEDARASRDEifATAKENEKKakslEADLMQLQEDLAAAERA 1702
Cdd:COG4913 865 RIDPLndslkripfgpgRYLRlearprpdPEVREFRQELRAVTSGASL--FDEELSEAR----FAALKRLIERLRSEEEE 938
|
....*
gi 13124875 1703 RKQAD 1707
Cdd:COG4913 939 SDRRW 943
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1075-1317 |
5.93e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.79 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1075 QAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTE 1154
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1155 LEDTLDSTATQ--QELRAKREQEVTVLKKALDeetrshEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKE 1232
Cdd:COG4942 99 LEAQKEELAELlrALYRLGRQPPLALLLSPED------FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1233 NADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGmlNEAEGKAIKLAKDVAS 1312
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA--EAAAAAERTPAAGFAA 250
|
....*
gi 13124875 1313 LSSQL 1317
Cdd:COG4942 251 LKGKL 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1084-1925 |
8.34e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 70.75 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1084 QLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTELEDTLDSTA 1163
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1164 TQQELRAKREQEVTVLKkaldEETRSHEAQVQEMRQKHA---QAVEELTEQLEQFKRAKANLDKNKQTLEkeNADLAGEl 1240
Cdd:COG3096 365 EQEEVVEEAAEQLAEAE----ARLEAAEEEVDSLKSQLAdyqQALDVQQTRAIQYQQAVQALEKARALCG--LPDLTPE- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1241 rvlgQAKQEVEHKKKKLEA---QVQELQSKCSDGERARAELnDKVHKLqneVESVTGML--NEAEGKAIKLAKDVASLSS 1315
Cdd:COG3096 438 ----NAEDYLAAFRAKEQQateEVLELEQKLSVADAARRQF-EKAYEL---VCKIAGEVerSQAWQTARELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1316 QLQDTQELLQE--ETRQKLNvstKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEG 1393
Cdd:COG3096 510 LAQRLQQLRAQlaELEQRLR---QQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1394 KKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLvVDLDNQRQLVSNLEKKQRKFDQLLAEEKnisskyaderDR 1473
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADS-QEVTAAMQQLLEREREATVERDELAARK----------QA 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1474 AEAEARE-------KETKALSLAraleealeakeelERTNKMLKAEMEDLVS---------------------------- 1518
Cdd:COG3096 656 LESQIERlsqpggaEDPRLLALA-------------ERLGGVLLSEIYDDVTledapyfsalygparhaivvpdlsavke 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1519 --------------------SKDDVGKNVHELEK------SKRAL----------------ETQMEEMKTQLEELEDELq 1556
Cdd:COG3096 723 qlagledcpedlyliegdpdSFDDSVFDAEELEDavvvklSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY- 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1557 atedAKLRLEVN-MQALKGQFERDL-----QARDEQNEEKRRQLQRQLHEYETELEDERKQralaaaakkklegdlkdlE 1630
Cdd:COG3096 802 ----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELERELAQHRAQ------------------E 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1631 LQADSAIKGREEAIKQLRKLQAQM------------KDFQRELEDARASRDEIfataKENEKKAKSLEADLMQLQEDLAA 1698
Cdd:COG3096 860 QQLRQQLDQLKEQLQLLNKLLPQAnlladetladrlEELREELDAAQEAQAFI----QQHGKALAQLEPLVAVLQSDPEQ 935
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1699 AERARKQADlekeelaeelasslsgrnALQDEKRRLEARIaqleeeleeeqgnmEAMSDRVRKATQQAEQLSNELATERS 1778
Cdd:COG3096 936 FEQLQADYL------------------QAKEQQRRLKQQI--------------FALSEVVQRRPHFSYEDAVGLLGENS 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1779 TAqkNESARQQLErQNKELRSKLHEmegavkskfkstiaALEAKIAQLEE--QVEQEAREK-QAATKSLKQKDKKLKEIL 1855
Cdd:COG3096 984 DL--NEKLRARLE-QAEEARREARE--------------QLRQAQAQYSQynQVLASLKSSrDAKQQTLQELEQELEELG 1046
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1856 LQVEDErkMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALK 1925
Cdd:COG3096 1047 VQADAE--AEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAK 1114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
992-1707 |
1.06e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.38 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 992 DQNNKLSKERKLLEERISDLTTNLaeeEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEgDASDFHEQI 1071
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCT---PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1072 ADLQAQIAELKMQLAKKEE-----ELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGE 1146
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEEtqeriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1147 ELEALKTELedtldstatQQELRAKREQEVTVLKKALDEETRSHEAQVQemrqKHAQAVEELTEQLEQFKRAKANLDKNK 1226
Cdd:TIGR00618 343 QRRLLQTLH---------SQEIHIRDAHEVATSIREISCQQHTLTQHIH----TLQQQKTTLTQKLQSLCKELDILQREQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1227 QTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVEsvtgmlneaegkaikl 1306
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ---------------- 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1307 akdvaslssQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDE-EMEAKQNLERHIST-LNIQLSDSKKKLQDFA 1384
Cdd:TIGR00618 474 ---------QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGPLTrRMQRGEQTYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1385 STVE----ALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE 1460
Cdd:TIGR00618 545 EDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1461 KNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSkddvgknvhELEKSKRALETQ 1540
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ---------KMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1541 MEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKK 1620
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSL-GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAAL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1621 KLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEK-KAKSLEADLMQLQEDLAAA 1699
Cdd:TIGR00618 775 QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsRLEEKSATLGEITHQLLKY 854
|
....*...
gi 13124875 1700 ERARKQAD 1707
Cdd:TIGR00618 855 EECSKQLA 862
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1036-1453 |
1.45e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1036 ISELEVRLKKEEKSRQELEKLKRKLEgdasDFHEQIADLQAQIAELKMQLAKKEEELQA--ALARLDDEIAQKNNALKKI 1113
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1114 RELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQ 1193
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1194 VQEMRQKH-AQAVEELTEQLEQFKRAKA-------NLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQ 1265
Cdd:COG4717 229 LEQLENELeAAALEERLKEARLLLLIAAallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1266 SKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQ---------LQDTQELLQ-------EETR 1329
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqleelEQEIAALLAeagvedeEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1330 QKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHIS--TLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLtqq 1407
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQL--- 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 13124875 1408 yeEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKF 1453
Cdd:COG4717 466 --EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1290-1889 |
1.53e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1290 ESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQeetrqklnvstKLRQLEEERNSLQDQLDEEMEAKQNLERHISTL 1369
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELE-----------KLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1370 NIQLSDSKKKLQDFASTVEALEEGKKRFqKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK 1449
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1450 QRKFDQLLAEEKNISSKYADERDRAEAEAREKEtkalslaraleealeakeelertnkmLKAEMEDLvsSKDDVGKNVHE 1529
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEAKA--------------------------KKEELERL--KKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1530 LEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLqrqLHEYETELEDER 1609
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEL---LEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1610 KQRALAAAAKKKLEGDLKDLE--LQADSAIKGREEAIKQLRKLQAQMKDFQRE-LEDARASRDEIFATAKENEKKAKSLE 1686
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1687 ADLMQLQE---DLAAAERARKQADLEkeelaeelasslsgrnaLQDEKRRLEARIAQLEEELEEEQGNMEAMSDR---VR 1760
Cdd:PRK03918 546 KELEKLEElkkKLAELEKKLDELEEE-----------------LAELLKELEELGFESVEELEERLKELEPFYNEyleLK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1761 KATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAV-----------KSKFKSTIAALEAKIAQLEEQ 1829
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyeelreeYLELSRELAGLRAELEELEKR 688
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1830 VEQEAREkqaaTKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKgnarVKQLKRQLEEA 1889
Cdd:PRK03918 689 REEIKKT----LEKLKEELEEREKAKKELEKLEKALERVEELREK----VKKYKALLKER 740
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
803-1396 |
1.91e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 803 RKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAEnelkeleqkh 882
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---------- 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 883 sqlteeknllqEQLQAEtELYAEAEEMRVRLAAKKqeleeilhemearleeeedrgqqlQAERKKMAQQMLDLEEQLEEE 962
Cdd:PTZ00121 1442 -----------EAKKAD-EAKKKAEEAKKAEEAKK------------------------KAEEAKKADEAKKKAEEAKKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 963 EAARQKLQLEKVTAEAKIKKLEDEilvmddqnnKLSKERKLLEERISDLTTNLAEEEEKAKNLTKL--KNKHESMISELE 1040
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAK---------KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAeeKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1041 VRlKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHI 1120
Cdd:PTZ00121 1557 LK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1121 SDLQEDLDSE--RAARNKAEKQKRDLGEELEALKTElEDTLDSTATQQELRAKREQEVTVLKKAldEETRSHEaQVQEMR 1198
Cdd:PTZ00121 1636 EQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKAE-ELKKKE 1711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1199 QKHAQAVEELTEQlEQFKRAKANLDKNKQTLEKENADlagELRVLGQAKQEVEHKKKKLEAQVQELQSKCS--------- 1269
Cdd:PTZ00121 1712 AEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavieeelde 1787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1270 DGERARAELNDKVHKLQNEVESV-------TGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLE 1342
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIieggkegNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKE 1867
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1343 EERNS----LQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEAL--EEGKKR 1396
Cdd:PTZ00121 1868 ADFNKekdlKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLdkDEYIKR 1927
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1103-1911 |
1.96e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.48 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1103 IAQKNNALKKIRELEGHISDLQEDLDSERA---ARNKAEKQKRDLgEELEALKTELEDTLDSTATQQELRAKREQEVTVL 1179
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHWIRDIQAIAGimkIRPEFTKLQQEF-NTLESAELRLSHLHFGYKSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1180 KKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADlagelrvlgQAKQEVEhkkkklea 1259
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIE---------TAAADQE-------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1260 QVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEaegkaiKLAKDVASLSSQLQDTQEllqEETRQKLNVSTKLR 1339
Cdd:pfam12128 348 QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIRE---ARDRQLAVAEDDLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1340 QLEEE-RNSLQDQLDEEMEAKQNLERHISTLNIQL------SDSKKKLQDFASTVEALEEGKKRFQKEIENLtqQYEEKA 1412
Cdd:pfam12128 419 ALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLnqatatPELLLQLENFDERIERAREEQEAANAEVERL--QSELRQ 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1413 A------AYDKLEKTKNRLQQ---ELDDLVVDLDNQR-QLVSNLEKKQRKFDQLLAeeKNISSKYADERDRAEAEAREKE 1482
Cdd:pfam12128 497 ArkrrdqASEALRQASRRLEErqsALDELELQLFPQAgTLLHFLRKEAPDWEQSIG--KVISPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1483 TKALSL-ARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDA 1561
Cdd:pfam12128 575 GGELNLyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLD 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1562 KLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETEL--------EDERKQRALAAAAKKKLEGDLKDLELQA 1633
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqawleeqkEQKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1634 DSAIKGREEAIKqlRKLQAQMKDFQRELedarASRDEifatakeNEKKAKSLEADLMQLQEDLAAAERARKQAdleKEEL 1713
Cdd:pfam12128 735 KAAIAARRSGAK--AELKALETWYKRDL----ASLGV-------DPDVIAKLKREIRTLERKIERIAVRRQEV---LRYF 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1714 AEELASSLSGRNALQDEKRRLEARIaqleeeleeeqgnmEAMSDRVRKATQQAEQLSNELATERstaqknESARQQLERQ 1793
Cdd:pfam12128 799 DWYQETWLQRRPRLATQLSNIERAI--------------SELQQQLARLIADTKLRRAKLEMER------KASEKQQVRL 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1794 NKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQ------VEDERKMAEQ 1867
Cdd:pfam12128 859 SENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADhsgsglAETWESLREE 938
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 1868 YKEQAEKG-----------------NARVKQLKRQLEEA---------------EEESQRINANRRKLQRELDEAT 1911
Cdd:pfam12128 939 DHYQNDKGirlldyrklvpyleqwfDVRVPQSIMVLREQvsilgvdltefydvlADFDRRIASFSRELQREVGEEA 1014
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
934-1854 |
2.08e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 69.62 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 934 EEDRGQQL------QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEER 1007
Cdd:pfam02463 159 EEEAAGSRlkrkkkEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1008 ISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAK 1087
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA-------KEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1088 KEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDldseRAARNKAEKQKRDLGEELEALKTELEDTLdSTATQQE 1167
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK----REAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1168 LRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQ-------AVEELTEQLEQFKRAKANLDKNKQTLE--KENADLAG 1238
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKeekkeelEILEEEEESIELKQGKLTEEKEELEKQelKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1239 ELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQ 1318
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1319 DTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDskkklqdfastvealeegkkrfQ 1398
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL----------------------N 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1399 KEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEA 1478
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1479 REKETKALSLARALEEALEAKEELERTNKMLKAEMEDLvsskddvgknvhELEKSKRALETQMEEMKTQLEELEDELQAT 1558
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL------------LADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1559 EDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERkqRALAAAAKKKLEGDLKDLELQADSAIK 1638
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL--RALEEELKEEAELLEEEQLLIEQEEKI 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1639 GREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADlekeelaeELA 1718
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK--------KEL 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1719 SSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERStaQKNESARQQLERQNKELR 1798
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN--KRLLLAKEELGKVNLMAI 980
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 1799 SKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEI 1854
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKV 1036
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1114-1900 |
2.15e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1114 RELEGHISDLQEDLDSERAARNKAEK--QKRDLGEELEALKTELEDTLDSTATQQELRAKREQevtvlkkaldeetrshe 1191
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRL----------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1192 aqvqemrQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKK-LEAQVQELQSKCSD 1270
Cdd:COG4913 284 -------WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1271 GERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQ-ELLQEETRQKlnvsTKLRQLEEERNSLQ 1349
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALaEAEAALRDLR----RELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1350 DQ---LDEEM-EAKQNLERHistlniqLSDSKKKLQDFASTVEaLEEGKKRFQKEIENL-----------TQQYEEKAAA 1414
Cdd:COG4913 433 RRksnIPARLlALRDALAEA-------LGLDEAELPFVGELIE-VRPEEERWRGAIERVlggfaltllvpPEHYAAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1415 YDKLeKTKNRLQ-QELDDLVVDLDNQR----QLVSNLEKKQRKFDQLLAEEknisskYADERDRA---EAEAREKETKAL 1486
Cdd:COG4913 505 VNRL-HLRGRLVyERVRTGLPDPERPRldpdSLAGKLDFKPHPFRAWLEAE------LGRRFDYVcvdSPEELRRHPRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1487 SLARaleealeakeelertnkmlkaemedLVSSKDDVG-KNVHELEKSKRAL----ETQMEEMKTQLEELEDELQATEDA 1561
Cdd:COG4913 578 TRAG-------------------------QVKGNGTRHeKDDRRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAEER 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1562 KLRLEVNMQALKGQFERDLQARDEQNEEKR-RQLQRQLHEYETELEDERKqralaaaakkkLEGDLKDLELQADSAIKGR 1640
Cdd:COG4913 633 LEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDA-----------SSDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1641 EEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLmqLQEDLAAAERARKQADLekeelaeelass 1720
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGDAVEREL------------ 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1721 lsgRNALQDEKRRLEARIAQLEEELeeeqgnMEAMSDRVRKATQQAEQLSNELATERSTAQKNES-ARQQLERQNKELRS 1799
Cdd:COG4913 768 ---RENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPEYEERFKE 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1800 KLHEMEGAVKSKFKStiaALEAKIAQLEEQVEQ------------EAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQ 1867
Cdd:COG4913 839 LLNENSIEFVADLLS---KLRRAIREIKERIDPlndslkripfgpGRYLRLEARPRPDPEVREFRQELRAVTSGASLFDE 915
|
810 820 830
....*....|....*....|....*....|...
gi 13124875 1868 ykEQAEKGNARVKQLKRQLEEAEEESQRINANR 1900
Cdd:COG4913 916 --ELSEARFAALKRLIERLRSEEEESDRRWRAR 946
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
851-1377 |
5.61e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.82 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAakkQELEEILHEMEAR 930
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 931 LEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDeilVMDDQNNKLSKErkllEERISD 1010
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLKI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEK---SRQELEKLKRKLEGDASDF-------HEQIADLQAQIAE 1080
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTA 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1081 LKMQLAKKEEELQAALARLDDE-------IAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK- 1152
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEklknielTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEe 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1153 --TELEDTLDStaTQQELRAKREQEVTVLKKAlDEETRSHEAQVQEMRQKHA---QAVEELTEQLEQFKRAKANLDKNKQ 1227
Cdd:pfam05483 542 keMNLRDELES--VREEFIQKGDEVKCKLDKS-EENARSIEYEVLKKEKQMKileNKCNNLKKQIENKNKNIEELHQENK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1228 TLEKENADLAGELRV----LGQAKQEVEHKKKKLEAQVQELQSKCSDG-----------ERARAELNDKVhKLQNEVE-- 1290
Cdd:pfam05483 619 ALKKKGSAENKQLNAyeikVNKLELELASAKQKFEEIIDNYQKEIEDKkiseeklleevEKAKAIADEAV-KLQKEIDkr 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1291 ---SVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHIS 1367
Cdd:pfam05483 698 cqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
570
....*....|
gi 13124875 1368 TLNIQLSDSK 1377
Cdd:pfam05483 778 ENTAILKDKK 787
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1405-1929 |
7.16e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 67.89 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1405 TQQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnqrqlvsNLEKKQrkfdQLLAEEKNISSkyadERDRAEAE--AREKE 1482
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELK-----------ELEKKH----QQLCEEKNALQ----EQLQAETElcAEAEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1483 TKALSLARaleealeakeelertnkmlKAEMEDLVSskdDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDA- 1561
Cdd:pfam01576 62 MRARLAAR-------------------KQELEEILH---ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAr 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1562 -KLRLE-VNMQALKGQFERDLQARDEQN---EEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSA 1636
Cdd:pfam01576 120 qKLQLEkVTTEAKIKKLEEDILLLEDQNsklSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1637 IKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFA--TAKENE-------------------KKAKSLEADLMQLQED 1695
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAqlAKKEEElqaalarleeetaqknnalKKIRELEAQISELQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1696 LAAAERARKQADLEK-------EELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEA-MSDRVRKATQQAE 1767
Cdd:pfam01576 280 LESERAARNKAEKQRrdlgeelEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAqLQEMRQKHTQALE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1768 QLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAvkskfkstiaaleakiaqleeqveqeareKQAATKSLKQK 1847
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA-----------------------------KQDSEHKRKKL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1848 DKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSK 1927
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR 490
|
..
gi 13124875 1928 LR 1929
Cdd:pfam01576 491 LR 492
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
941-1678 |
1.21e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 66.67 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 941 LQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEE---RISDLTTNLAE 1017
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcaRSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1018 EEEKAKNL-TKLKNKHESMISELEVRLKKEEKSRQELE-KLKR---KLEGDASDFHEQIADLQAQIAELKMQLAKKEEEL 1092
Cdd:pfam05483 177 EREETRQVyMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEdheKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1093 QAALARLDDEIAQKNNALKKIRELEGHISDLQEdldseraarnkaekQKRDLGEELEALKTELEDtldSTATQQELrakr 1172
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEKTKLQDENLKELIE--------------KKDHLTKELEDIKMSLQR---SMSTQKAL---- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1173 EQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEqleqfkrakanLDKNKQTLEKenadlagelrVLGQAKQEVEH 1252
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE-----------FEATTCSLEE----------LLRTEQQRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1253 KKKKLEAQVQELQSKCSdgeraraelndkvhklqnEVESVTGMLNEAEgkaiklaKDVASLSSQLQDTQELLQEEtrqkl 1332
Cdd:pfam05483 375 NEDQLKIITMELQKKSS------------------ELEEMTKFKNNKE-------VELEELKKILAEDEKLLDEK----- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1333 nvstklRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALeegkkrfQKEIENLTQQYEEKA 1412
Cdd:pfam05483 425 ------KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL-------KTELEKEKLKNIELT 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1413 AAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQ----RKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSL 1488
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1489 ARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRA---------------------LETQMEEMKTQ 1547
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsaenkqlnayeikvnkLELELASAKQK 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1548 LEELEDELQATEDAKlrlEVNMQALKGQFERDLQARDEQ---NEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEG 1624
Cdd:pfam05483 652 FEEIIDNYQKEIEDK---KISEEKLLEEVEKAKAIADEAvklQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1625 DLKDLELQADSAIKGREeaiKQLRKLQAQMKDFQRELEDARASRDEIFATAKEN 1678
Cdd:pfam05483 729 LYKNKEQEQSSAKAALE---IELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1011-1241 |
1.51e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLA---K 1087
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAeleK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1088 KEEELQAALARLDDEIAQKNNALKKIreleGHISDLQEDLDSERAARnkAEKQKRDLGEELEALKTELEDTLDSTATQQE 1167
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRL----GRQPPLALLLSPEDFLD--AVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1168 LRAKREQEVTVLKKALDEETRSHeAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELR 1241
Cdd:COG4942 165 LRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1253-1487 |
1.60e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1253 KKKKLEAQVQELQSKcsdgeraRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEetrqkl 1332
Cdd:COG4942 21 AAAEAEAELEQLQQE-------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1333 nVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHiSTLNIQLS-----DSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1407
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1408 YEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALS 1487
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1192-1414 |
1.78e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1192 AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDG 1271
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1272 ERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQklnVSTKLRQLEEERNSLQDQ 1351
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1352 LDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAA 1414
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1036-1221 |
1.91e-10 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 63.02 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1036 ISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNAlKKIRE 1115
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1116 LEghisDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTldstatqQELRAKREQEVTVLKKALDEETRSHEAQVQ 1195
Cdd:COG1579 91 YE----ALQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|....*..
gi 13124875 1196 EMRQKHAQAVEELTEQL-EQFKRAKAN 1221
Cdd:COG1579 160 ELEAEREELAAKIPPELlALYERIRKR 186
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
846-1661 |
2.93e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 65.84 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETelyAEAEEMRVRLAAKKQELEEILH 925
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARD---SLIQSLATRLELDGFERGPFSE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 926 EMEARLEEEEDRGQQLQAerkKMAQQMLDleeqleeeeaarqKLQLEKVTAEAKIKKLEDEilvMDDQNNKLSKERKLLE 1005
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEA---KTAAQLCA-------------DLQSKERLKQEQADEIRDE---KKGLGRTIELKKEILE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMI-SELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQ 1084
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILELDQELRkAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1085 LAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISD------LQEDLDSERAARNKAEKQKRDLGEELEALKTeledt 1158
Cdd:TIGR00606 531 TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQ----- 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1159 lDSTATQQELRAKREQEVTVLKKALDE-ETRSHEAQVQEMRQKhaqaVEELTEQLEQFKRAKANLDKNKQTLEKENADLA 1237
Cdd:TIGR00606 606 -NKNHINNELESKEEQLSSYEDKLFDVcGSQDEESDLERLKEE----IEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1238 GELRVLGQAKQEVEHKKKKLEA-------QVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDV 1310
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1311 ASLSSQLQDTQELLqeetrQKLNVSTKLRQLEEERNSLQDQLDEEMEakqNLERHISTLNIQLSDSkkklqDFASTVEAL 1390
Cdd:TIGR00606 761 QRLKNDIEEQETLL-----GTIMPEEESAKVCLTDVTIMERFQMELK---DVERKIAQQAAKLQGS-----DLDRTVQQV 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1391 EEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDldnQRQLVSNLEKKQRKFDQLLAEEKNISSKYADE 1470
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE---KLQIGTNLQRRQQFEEQLVELSTEVQSLIREI 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1471 RDRAEAEAREKETKALSLARALEEALEAKEelerTNKMLKAEMEDLVSSKDDVGKNVHELEKS-KRALETQMEEMKTQLE 1549
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKET----SNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDDYLKQKETELN 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1550 ELEDELQATEDAKLRLEVNMQALKGQFE-RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEgdLKD 1628
Cdd:TIGR00606 981 TVNAQLEECEKHQEKINEDMRLMRQDIDtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQE--HQK 1058
|
810 820 830
....*....|....*....|....*....|...
gi 13124875 1629 LELQADSAIKGREEAIKQLRKLQAQMKDFQREL 1661
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1671-1931 |
3.17e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1671 IFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEkeelaeelasslsgRNALQDEKRRLEARIAQLEEELEEEQG 1750
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1751 NMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNK-ELRSKLHEMEGAVKSK--FKSTIAALEAKIAQLE 1827
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLqyLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1828 EQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQREl 1907
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE- 235
|
250 260
....*....|....*....|....
gi 13124875 1908 dEATESNEAMGREVNALKSKLRGP 1931
Cdd:COG4942 236 -AAAAAERTPAAGFAALKGKLPWP 258
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1069-1863 |
3.23e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1069 EQIADLQAQIAELKMQLAKKEEelqaALARLDDEIAQKNNALKkirELEGHISDLQEDLDSERAARNKAEKQKRdLGEEL 1148
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQY----RLVEMARELAELNEAES---DLEQDYQAASDHLNLVQTALRQQEKIER-YQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1149 EALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEeTRSHEAQVQemrqkhaQAVEELTEQLEQFKRAKANLDKNKQT 1228
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDE-LKSQLADYQ-------QALDVQQTRAIQYQQAVQALERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1229 LEKENADLAGelrvLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDK---VHKLQNEVESvtgmlNEAEGKAIK 1305
Cdd:PRK04863 430 CGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAyqlVRKIAGEVSR-----SEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1306 LAKDVASLSSQLQDTQELLQE--ETRQKLNvstKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDskkkLQDF 1383
Cdd:PRK04863 501 LLRRLREQRHLAEQLQQLRMRlsELEQRLR---QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES----LSES 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1384 ASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDldnqRQLVSNLEKkqrkfdQLLAEEKNI 1463
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED----SQDVTEYMQ------QLLEREREL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1464 SSkyadERDRAEAEAREKETKALSLA-RALEEALEAKEELERTNKMLKAEMEDLVS------------------------ 1518
Cdd:PRK04863 644 TV----ERDELAARKQALDEEIERLSqPGGSEDPRLNALAERFGGVLLSEIYDDVSledapyfsalygparhaivvpdls 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1519 ------------------------SKDDVGKNVHELEKS----------------------KRALETQMEEMKTQLEELE 1552
Cdd:PRK04863 720 daaeqlagledcpedlyliegdpdSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELA 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1553 DELqatedAKLRLEVN-MQALKGQFERDLQ-----ARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDL 1626
Cdd:PRK04863 800 ERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1627 KDL-ELQADSAIKGREEAIKQLRKLQAQMKdfqrELEDARASRDEIFATAKENEKKAKSLEAD---LMQLQEDLAAAERA 1702
Cdd:PRK04863 875 SALnRLLPRLNLLADETLADRVEEIREQLD----EAEEAKRFVQQHGNALAQLEPIVSVLQSDpeqFEQLKQDYQQAQQT 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1703 RKQADLEKEelaeelasslsgrnALQD-EKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERST-A 1780
Cdd:PRK04863 951 QRDAKQQAF--------------ALTEvVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQlA 1016
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1781 QKNE------SARQQLERQNKELRSKLHEM-----EGAV------KSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKS 1843
Cdd:PRK04863 1017 QYNQvlaslkSSYDAKRQMLQELKQELQDLgvpadSGAEerararRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
|
890 900
....*....|....*....|
gi 13124875 1844 LKQKDKKLKEILLQVEDERK 1863
Cdd:PRK04863 1097 LRKLERDYHEMREQVVNAKA 1116
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
846-1211 |
5.18e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 64.75 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQK----------TKERQQKAENELK----ELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRV 911
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKvssltaqlesTKEMLRKVVEELTakkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 912 RLAAKKQELEEILHEMEARLEEEED-RGQQLQ-AERKK----MAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKI--KKL 983
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDHLRNVQTEcEALKLQmAEKDKvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIndRRL 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 984 E-DEILVMDDQNNKLSKErklLEERISDLTTN----LAEEEEKAKNLTKLKNKHESMISELevrlkkeEKSRQELEKLKR 1058
Cdd:pfam15921 605 ElQEFKILKDKKDAKIRE---LEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLNEV-------KTSRNELNSLSE 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1059 KLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNAL-------KKIRELEGHISDLQEDLDSER 1131
Cdd:pfam15921 675 DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKRGQIDALQSKIQFLE 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1132 AARNKAEKQKRDLGEElealKTELEDTLDSTATQQ-----ELRAKREQE------VTVLKKALDEETRSHeAQVQEMRQK 1200
Cdd:pfam15921 755 EAMTNANKEKHFLKEE----KNKLSQELSTVATEKnkmagELEVLRSQErrlkekVANMEVALDKASLQF-AECQDIIQR 829
|
410
....*....|.
gi 13124875 1201 HAQAVEELTEQ 1211
Cdd:pfam15921 830 QEQESVRLKLQ 840
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1282 |
5.37e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMrvrlaaKKQELEEILH 925
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN---QLKSEISDL------NNQKEQDWNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 926 EMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLE 1005
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQL 1085
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQK-------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1086 AKKEEELQA----------ALARLDDEIAQKNNALKKI----RELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEAL 1151
Cdd:TIGR04523 464 ESLETQLKVlsrsinkikqNLEQKQKELKSKEKELKKLneekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1152 KTEL---EDTLDSTATQQELRAKrEQEVTVLKKALDEETRSHEaQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQT 1228
Cdd:TIGR04523 544 EDELnkdDFELKKENLEKEIDEK-NKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1229 LEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKV 1282
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1507-1915 |
6.76e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1507 KMLKAEMEDLVSSKDDVGK-NVHELEKSKRALEtQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFER-DLQARD 1584
Cdd:COG4717 49 ERLEKEADELFKPQGRKPElNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1585 EQNEEKRRQLQRQLHEYET---ELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQlrklqaQMKDFQREL 1661
Cdd:COG4717 128 LPLYQELEALEAELAELPErleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1662 EDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQL 1741
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1742 EEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQL--ERQNKELRSKLHEMEGAVKSKFKSTIAAL 1819
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLppDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1820 EAKIAQLEEQVEQ-----------EAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGN--ARVKQLKRQL 1886
Cdd:COG4717 362 ELQLEELEQEIAAllaeagvedeeELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEEL 441
|
410 420
....*....|....*....|....*....
gi 13124875 1887 EEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGE 470
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
847-1370 |
6.81e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.47 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 847 VTRQEEEMQAKEDEL-QKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEemRVRLAAKKQELEEI-- 923
Cdd:pfam12128 317 VAKDRSELEALEDQHgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIag 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 924 LHEMEARLEEEEDRG--------QQLQAE-RKKMAQQMLD--LEEQLEEEEAARQKLQLEKVTAEakikkledEILVMDD 992
Cdd:pfam12128 395 IKDKLAKIREARDRQlavaeddlQALESElREQLEAGKLEfnEEEYRLKSRLGELKLRLNQATAT--------PELLLQL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 993 QNNKlskerKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRK-----------LE 1061
Cdd:pfam12128 467 ENFD-----ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhfLR 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1062 GDASDFHEQIADLQAQIAELKMQL------AKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARN 1135
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLHRTDLdpevwdGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1136 KAEKQKRDLGEELEALKTELEDTL----DSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQ 1211
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARtalkNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAW 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1212 LEQFKRAKANLDKNKQTLEKEnadLAGELRV-LGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVE 1290
Cdd:pfam12128 702 LEEQKEQKREARTEKQAYWQV---VEGALDAqLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIR 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1291 SVTGMLNEAEGKAIKLA---------------KDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEE 1355
Cdd:pfam12128 779 TLERKIERIAVRRQEVLryfdwyqetwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL 858
|
570
....*....|....*
gi 13124875 1356 MEAKQNLERHISTLN 1370
Cdd:pfam12128 859 SENLRGLRCEMSKLA 873
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
863-1459 |
7.61e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.97 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 863 KTKERQQKAENELKELEQKHSQLTeekNLLQEQLQAETELYAEAEEMRVRLAAKkqeleeilhemearLEEEEDRGQQLQ 942
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMDLN---NNIEKMILAFEELRVQAENARLEMHFK--------------LKEDHEKIQHLE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 943 AERKKMAQQmldleeqleeeeaARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKerklLEERISDLTTNLAEEEEKA 1022
Cdd:pfam05483 229 EEYKKEIND-------------KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ----LEEKTKLQDENLKELIEKK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1023 KNLTK-LKNKHESMISELEVRLKKEEK---SRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALAR 1098
Cdd:pfam05483 292 DHLTKeLEDIKMSLQRSMSTQKALEEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1099 LDDEIAQknnaLKKIR-ELEGHISDLQEDLDSERAARNKAEKQKRDLGEElealKTELEDTLDSTATQQELRAKrEQEVT 1177
Cdd:pfam05483 372 LEKNEDQ----LKIITmELQKKSSELEEMTKFKNNKEVELEELKKILAED----EKLLDEKKQFEKIAEELKGK-EQELI 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1178 VLKKALDEETRSHEAQVQEMR---QKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELR----VLGQAKQEV 1250
Cdd:pfam05483 443 FLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlELKKHQEDI 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1251 EHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQ 1330
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1331 KLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQkeiENLTQQYEE 1410
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE---EKLLEEVEK 679
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 13124875 1411 KAAAYDKLEKtknrLQQELDDLVvdLDNQRQLVSNLEKKQRKFDQLLAE 1459
Cdd:pfam05483 680 AKAIADEAVK----LQKEIDKRC--QHKIAEMVALMEKHKHQYDKIIEE 722
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1211-1929 |
1.24e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.91 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1211 QLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELnDKVHKLQNEVE 1290
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEL-DPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1291 svtgmlnEAEGKAIKLAKDVASLSSQlqdtqellqEETRQKLNvstklRQLEEERNSLQDQLDEEM-EAKQNLERHISTL 1369
Cdd:TIGR00606 259 -------HNLSKIMKLDNEIKALKSR---------KKQMEKDN-----SELELKMEKVFQGTDEQLnDLYHNHQRTVREK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1370 NIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYE---EKAAAYDkLEKTKNRLQQELDDLVVDLDNQRQLVSNL 1446
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhqEHIRARD-SLIQSLATRLELDGFERGPFSERQIKNFH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1447 EKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKN 1526
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1527 VHELEKS---------------------------------KRALETQMEEM------KTQLEELE----DELQATEDAKL 1563
Cdd:TIGR00606 477 DQELRKAerelskaeknsltetlkkevkslqnekadldrkLRKLDQEMEQLnhhtttRTQMEMLTkdkmDKDEQIRKIKS 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1564 RLEVNMQALKGQFERDLQARD---------EQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDL------KD 1628
Cdd:TIGR00606 557 RHSDELTSLLGYFPNKKQLEDwlhskskeiNQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQD 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1629 LELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASR-------DEIFATAKENEKKAKSLEADLMQLQEDLAAAER 1701
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1702 ARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAmSDRVRKATQQAEQLSNELATERSTAQ 1781
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIME 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1782 KNESARQQLERQNKELRSKLHEMEGAVK----SKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQ 1857
Cdd:TIGR00606 796 RFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 1858 VEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEAT----ESNEAMGREVNALKSKLR 1929
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIsskeTSNKKAQDKVNDIKEKVK 951
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1902 |
1.38e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1631 LQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQadlek 1710
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1711 eelaeelasslsgrnaLQDEKRRLEARIAQLEeeleeeqgnmEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQL 1790
Cdd:COG4942 88 ----------------LEKEIAELRAELEAQK----------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1791 ERQNKELRSKLHEMEgAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKE 1870
Cdd:COG4942 142 KYLAPARREQAEELR-ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250 260 270
....*....|....*....|....*....|..
gi 13124875 1871 QAEKGNARVKQLKRQLEEAEEESQRINANRRK 1902
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1227-1703 |
1.51e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1227 QTLEKENADLageLRVLGQAKQEVEHKKKKLEAQVQELQSKcsdgERARAELNDKVHKLQNEVESVTGMLNEAEGK--AI 1304
Cdd:COG4717 49 ERLEKEADEL---FKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREEleKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1305 KLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQlsdSKKKLQDFA 1384
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1385 STVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQE-----------LDDLVVDLDNQRQLVSNLEKKQRKF 1453
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1454 DQLLAEeknISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKS 1533
Cdd:COG4717 279 LFLVLG---LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1534 KRALETQMeemktQLEELEDELQATedaklrlevnMQALKGQFERDLQARDEQNEEkRRQLQRQLHEYETELEDERKQRA 1613
Cdd:COG4717 356 AEELEEEL-----QLEELEQEIAAL----------LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1614 LAAAAKKKL--EGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDF--QRELEDARASRDEIFATAKENEKKAKSLEADL 1689
Cdd:COG4717 420 ELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
490
....*....|....
gi 13124875 1690 MQLQEDLAAAERAR 1703
Cdd:COG4717 500 ELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
936-1165 |
1.66e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 936 DRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNL 1015
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1016 AEEEEKAKNLTKLKNKHeSMISELEVRLKKEEKSRQE--LEKLKRKLEGDASDFhEQIADLQAQIAELKMQLAKKEEELQ 1093
Cdd:COG4942 100 EAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQA-EELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1094 AALARLDDEIAQKNNALKKIRELeghISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQ 1165
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1080 |
2.36e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 850 QEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEmrvRLAAKKQELEEiLHEMEA 929
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAE-LEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 930 RLEEEEDRGQQLQAERKKMAQQMLDLEEQL------EEEEAARQKLQLEKVTAEakikkLEDEILVMDDQNNKLSKERKL 1003
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPA-----RREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1004 LEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEgdasdfhEQIADLQAQIAE 1080
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAA 238
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1044-1931 |
4.58e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.99 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1044 KKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQaalarlddeiaQKNNALKKIRELEGHISDL 1123
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELD-----------PLKNRLKEIEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1124 QEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTAT--QQELRAKREQEVTVLKK--ALDEETRSHEAQVQEMRQ 1199
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHnhQRTVREKERELVDCQREleKLNKERRLLNQEKTELLV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1200 KHAQAVEELTEQLEQFKRAKANLDKNKQTLE----KENADLAGELRVLGQAKQEVEHKKKKLEAQ-VQELQSKCSDGERA 1274
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfERGPFSERQIKNFHTLVIERQEDEAKTAAQlCADLQSKERLKQEQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1275 RAELNDKV----HKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKL-----NVSTKLRQ---LE 1342
Cdd:TIGR00606 428 ADEIRDEKkglgRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKaeknsLTETLKKEvksLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1343 EERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKlqdfASTVEALEEGKKRFQKEIENLTQQYEEKAAAYD---KLE 1419
Cdd:TIGR00606 508 NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK----MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKS 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1420 KTKNRLQQELDDLVVDLDNQRQLVSNLEKK-QRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEA 1498
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNElESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATA 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1499 KEELERTNkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEdaKLRLEVNMQALKGQFER 1578
Cdd:TIGR00606 664 VYSQFITQ--LTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE--KRRDEMLGLAPGRQSII 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1579 DLQARD-EQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELqadsaikgreeaikqLRKLQAQMKDF 1657
Cdd:TIGR00606 740 DLKEKEiPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI---------------MERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1658 QRELEDARASRDEIFATAKENEKKAKSLEADlMQLQEDLAAAERARKQADLEKEELAEELasslSGRNALQDEKRRLEAR 1737
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ-HELDTVVSKIELNRKLIQDQQEQIQHLK----SKTNELKSEKLQIGTN 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1738 IAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKF----- 1812
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkd 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1813 ----------------KSTIAALEAKIAQLE---EQVEQEAREKQAATKSLKQKDKKLKEILLQvedeRKMAEQYKEQAE 1873
Cdd:TIGR00606 960 ienkiqdgkddylkqkETELNTVNAQLEECEkhqEKINEDMRLMRQDIDTQKIQERWLQDNLTL----RKRENELKEVEE 1035
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1874 KGNARVKQLKR-QLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRGP 1931
Cdd:TIGR00606 1036 ELKQHLKEMGQmQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREP 1094
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
845-1373 |
6.64e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.34 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 845 LQVTRQEEEMQAKEDELQKTKeRQQKAenelkELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLaakkQELEEil 924
Cdd:pfam01576 639 LSLARALEEALEAKEELERTN-KQLRA-----EMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQL----EELED-- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 925 hemearleeeedrgqQLQAerkkmaqqmldleeqleeeeAARQKLQLEkVTAEAKIKKLEDEILVMDDQNNklsKERKLL 1004
Cdd:pfam01576 707 ---------------ELQA--------------------TEDAKLRLE-VNMQALKAQFERDLQARDEQGE---EKRRQL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1005 EERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKlegdasdfheqiadLQAQIAELkmq 1084
Cdd:pfam01576 748 VKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK--------------LQAQMKDL--- 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1085 lakkEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSeraarnkAEKQKRDLGEELEALKTELEDTLDSTAT 1164
Cdd:pfam01576 811 ----QRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAA-------SERARRQAQQERDELADEIASGASGKSA 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1165 QQELRAKREQEVTVLKKALDEETRSHEAQVQEMRqKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVL- 1243
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLR-KSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMe 958
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1244 GQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQEL 1323
Cdd:pfam01576 959 GTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQ 1038
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1324 LQ--EETRQKLNVStklrqleeeRNSLQDQLDEEMEAKQNLERHISTLNIQL 1373
Cdd:pfam01576 1039 LEeaEEEASRANAA---------RRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
972-1284 |
1.14e-08 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 60.07 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 972 EKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEE---EEKAKNLTKLKNKHESMISEL--EVRLKKE 1046
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDEcwkKIKRKKNSALSEALNGFKYEAnfKSRLLRE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1047 EKSRQE-------LEKLKRKLEG-----------------DASDFHEQIADLQ------AQIAELKMQLAKKE------- 1089
Cdd:pfam13166 170 IEKDNFnagvllsDEDRKAALATvfsdnkpeiapltfnviDFDALEKAEILIQkvigksSAIEELIKNPDLADwveqgle 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1090 -----------------EELQAALAR-LDDEIAQKNNALKK-IRELEGHISDLQEDLDSeRAARNKAEKQKRDLGEELEA 1150
Cdd:pfam13166 250 lhkahldtcpfcgqplpAERKAALEAhFDDEFTEFQNRLQKlIEKVESAISSLLAQLPA-VSDLASLLSAFELDVEDIES 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1151 LKTELEDTLDSTatQQELRAKREQEVTV--LKKALDEETRSHEAQVQ---------EMRQKHAQAVEELTEQLEQFKRAK 1219
Cdd:pfam13166 329 EAEVLNSQLDGL--RRALEAKRKDPFKSieLDSVDAKIESINDLVASineliakhnEITDNFEEEKNKAKKKLRLHLVEE 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13124875 1220 AnlDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHK 1284
Cdd:pfam13166 407 F--KSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1632-1925 |
1.36e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1632 QADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASR----DEIFATAKENEKKAKSLEADLMQLQEdlaaaERARKQAD 1707
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQ-----EERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1708 LEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEamsDRVRKATQQAEQLSnELATERSTAQKNESAR 1787
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1788 QQLERQNKELRSKLHEMEGAVK-SKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAE 1866
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1867 qyKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESN---EAMGREVNALK 1925
Cdd:pfam17380 520 --KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMMR 579
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1070-1307 |
1.73e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1070 QIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDserAARNKAEKQKRDLGEELE 1149
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1150 ALKTE------LEDTLDSTATQQELrakreQEVTVLKKALDeetrsheaqvqemrqKHAQAVEELTEQLEQFKRAKANLD 1223
Cdd:COG3883 94 ALYRSggsvsyLDVLLGSESFSDFL-----DRLSALSKIAD---------------ADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1224 KNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKA 1303
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....
gi 13124875 1304 IKLA 1307
Cdd:COG3883 234 AAAA 237
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1649-1930 |
1.89e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1649 KLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLE-------------ADLMQLQEDLAA-----AERARKQADLEK 1710
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLErqaekaerykelkAELRELELALLVlrleeLREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1711 EELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQL 1790
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1791 ERQNKELRSKLHEMEGAVKS-------------KFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQ 1857
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEElkeelesleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1858 VEDERKMAEQYKEQAEKGN------------ARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALK 1925
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLkkleeaelkelqAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
....*
gi 13124875 1926 SKLRG 1930
Cdd:TIGR02168 489 ARLDS 493
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1629-1903 |
1.97e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1629 LELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKenekkAKSLEADLMQLQEDLAAAERARKQAdl 1708
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE-----AKLLLQQLSELESQLAEARAELAEA-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1709 ekeelaeelasslsgrnalQDEKRRLEARIAQLEEELEEEQGNmeamsDRVRKATQQAEQLSNELATERSTAQKNESARQ 1788
Cdd:COG3206 239 -------------------EARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1789 QLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEarekQAATKSLKQKDKKLKEILLQVEDERKMAEQY 1868
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVARELYESL 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 13124875 1869 ---------KEQAEKGNARVkqlkrqLEEAEEESQRINANRRKL 1903
Cdd:COG3206 371 lqrleearlAEALTVGNVRV------IDPAVVPLKPVSPKKLLI 408
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
997-1738 |
2.52e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 997 LSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHES------MISELEVRLKKEEKSRQELEKLKRKLEGDAS---DF 1067
Cdd:PRK04863 295 LYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAasdhlnLVQTALRQQEKIERYQADLEELEERLEEQNEvveEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1068 HEQIADLQAQ-------IAELKMQLAkkeeELQAALARLDDEIAQKNNALKKIRELEG--HISDLQEDLDSERAARNKAE 1138
Cdd:PRK04863 375 DEQQEENEARaeaaeeeVDELKSQLA----DYQQALDVQQTRAIQYQQAVQALERAKQlcGLPDLTADNAEDWLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1139 KQkrDLGEELEALKTELEDTlDSTATQQELRAK----------REQEVTVLKKALD--EETRSHEAQVQEMRQKHAQAVE 1206
Cdd:PRK04863 451 EQ--EATEELLSLEQKLSVA-QAAHSQFEQAYQlvrkiagevsRSEAWDVARELLRrlREQRHLAEQLQQLRMRLSELEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1207 ELTEQ------LEQF-KRAKANLDKN------KQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKcsdgER 1273
Cdd:PRK04863 528 RLRQQqraerlLAEFcKRLGKNLDDEdeleqlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR----AP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1274 ARAELNDKVHKLQnevesvtgmlnEAEGKAIKlakDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQD--- 1350
Cdd:PRK04863 604 AWLAAQDALARLR-----------EQSGEEFE---DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQpgg 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1351 -------QLDE--------------------EMEAKQNLERHISTLNiQLSDSKKKL-----------------QDFAST 1386
Cdd:PRK04863 670 sedprlnALAErfggvllseiyddvsledapYFSALYGPARHAIVVP-DLSDAAEQLagledcpedlyliegdpDSFDDS 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1387 VEALEEGKKrfqkeieNLTQQYEEKAAAYDKL-----------EKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQ 1455
Cdd:PRK04863 749 VFSVEELEK-------AVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSR 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1456 LLAEEKNISSKYADERDRAEAEAREKE-TKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDvgknvheleksk 1534
Cdd:PRK04863 822 FIGSHLAVAFEADPEAELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD------------ 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1535 ralETQMEEmktqLEELEDELQATEDAKL----------RLEVNMQALK---GQFERdLQARDEQNEEKRRQLQRQLHEY 1601
Cdd:PRK04863 890 ---ETLADR----VEEIREQLDEAEEAKRfvqqhgnalaQLEPIVSVLQsdpEQFEQ-LKQDYQQAQQTQRDAKQQAFAL 961
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1602 eTEL---------EDERKQRALAAAAKKKLEGDLKDLELQadsaikgREEAIKQLRKLQAQMKDFQRELEDARASRDeif 1672
Cdd:PRK04863 962 -TEVvqrrahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQE-------RTRAREQLRQAQAQLAQYNQVLASLKSSYD--- 1030
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 1673 atAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEelaeELASSLSGRNALQDEKRRLEARI 1738
Cdd:PRK04863 1031 --AKRQMLQELKQELQDLGVPADSGAEERARARRDELHA----RLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1050-1832 |
2.63e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.58 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1050 RQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKK---EEELQAALARLDDEIAQKNNALK---KIRELEGHISDL 1123
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsarESDLEQDYQAASDHLNLVQTALRqqeKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1124 QEDLDSERAARNKAEKQKRDLGEELEA-------LKTELED---TLDSTAT-----QQELRAKRE-QEVTVLKKALDEET 1187
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVQQTraiqyQQAVQALEKaRALCGLPDLTPENA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1188 RSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKenadLAGEL---RVLGQAKQEVEH--KKKKLEAQVQ 1262
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCK----IAGEVersQAWQTARELLRRyrSQQALAQRLQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1263 ELQSKCSDGERARAElndkvhklQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLE 1342
Cdd:COG3096 516 QLRAQLAELEQRLRQ--------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1343 EERNSLQDQLDEE----MEAKQNLERHISTLNIQLSDSKKKLQDFASTVEA----------LEEGKKRFQKEIENLTQqy 1408
Cdd:COG3096 588 EQLRARIKELAARapawLAAQDALERLREQSGEALADSQEVTAAMQQLLERereatverdeLAARKQALESQIERLSQ-- 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1409 eeKAAAYD-KLEKTKNRLQQEL-----DDLVVD--------LDNQRQ--LVSNLEKKQRKFDQLlaeEKNISSKYADERD 1472
Cdd:COG3096 666 --PGGAEDpRLLALAERLGGVLlseiyDDVTLEdapyfsalYGPARHaiVVPDLSAVKEQLAGL---EDCPEDLYLIEGD 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1473 RAEAEAREKETKALSLARALEEALEAKE-----------ELERTNKM--LKAEMEDLVSSKDDVGKNVHELEKSKRAL-- 1537
Cdd:COG3096 741 PDSFDDSVFDAEELEDAVVVKLSDRQWRysrfpevplfgRAAREKRLeeLRAERDELAEQYAKASFDVQKLQRLHQAFsq 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1538 --------------ETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFE--RDLQAR-----DEQNEEKRRQLQR 1596
Cdd:COG3096 821 fvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPQanllaDETLADRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1597 QLHEYEtELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKdfqrELEDARASRdEIFATAK 1676
Cdd:COG3096 901 ELDAAQ-EAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF----ALSEVVQRR-PHFSYED 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1677 ENEKKAKS------LEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLeeeleeeqg 1750
Cdd:COG3096 975 AVGLLGENsdlnekLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL--------- 1045
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1751 NMEAMSDRVRKATQQAEQLSNELATERstaqkneSARQQLERQNKELRSklhEMEGAVKskfksTIAALEAKIAQLEEQV 1830
Cdd:COG3096 1046 GVQADAEAEERARIRRDELHEELSQNR-------SRRSQLEKQLTRCEA---EMDSLQK-----RLRKAERDYKQEREQV 1110
|
..
gi 13124875 1831 EQ 1832
Cdd:COG3096 1111 VQ 1112
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1210-1894 |
2.76e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.96 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1210 EQLEQFKRAKANLDKNKQTLEKENADLAGELRvlgQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEV 1289
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELK---QKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1290 ESvtgmlNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQ-----------KLNVSTKLR-QLEEERNSLQDQLDEEME 1357
Cdd:pfam05483 148 KE-----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnniekMILAFEELRvQAENARLEMHFKLKEDHE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1358 AKQNLERhistlniqlsDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKtKNRLQQEldDLVVDLD 1437
Cdd:pfam05483 223 KIQHLEE----------EYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE-KTKLQDE--NLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1438 NQRQLVSNLEkkqrkfDQLLAEEKNISSKYADERDRAEAearekeTKAL-SLARALEEALEAKEELERTNKMLKAEMEDL 1516
Cdd:pfam05483 290 KKDHLTKELE------DIKMSLQRSMSTQKALEEDLQIA------TKTIcQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1517 VSSKDDVGKNVHE-LEKSKRALETQMEEMKTQLEELEDELQATEDAklrlEVNMQALKGQFERDLQARDEQNEEKRrqLQ 1595
Cdd:pfam05483 358 TCSLEELLRTEQQrLEKNEDQLKIITMELQKKSSELEEMTKFKNNK----EVELEELKKILAEDEKLLDEKKQFEK--IA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1596 RQLHEYETELEDERKQRalaaaakkklEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATA 1675
Cdd:pfam05483 432 EELKGKEQELIFLLQAR----------EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1676 KENEKKAKSLEADLMQLQEDLaaaERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAM 1755
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDI---INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSI 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1756 SDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKlhemeGAVKSKfksTIAALEAKIAQLEEQVEQEAR 1835
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK-----GSAENK---QLNAYEIKVNKLELELASAKQ 650
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1836 EKQAATKSLKQkdkklkeillQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQ 1894
Cdd:pfam05483 651 KFEEIIDNYQK----------EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ 699
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
853-1290 |
3.04e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.08 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 853 EMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETE-----LYAEA---EEMRVRLAAKKQELEEIL 924
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGtllhfLRKEApdwEQSIGKVISPELLHRTDL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 925 HEMEARLEEEEDR---GQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQlekvTAEAKIKKLEDEilvmddqnnkLSKER 1001
Cdd:pfam12128 566 DPEVWDGSVGGELnlyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQ----SAREKQAAAEEQ----------LVQAN 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1002 KLLEERISDLTTNLAEEEEKAKNLTKLKNKHESM----ISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIadlQAQ 1077
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEkdkkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQ---KEQ 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1078 IAELKMQLAKK----EEELQAALARLDDEIAQKNNALKKirelegHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT 1153
Cdd:pfam12128 709 KREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAKA------ELKALETWYKRDLASLGVDPDVIAKLKREIRTLER 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1154 ELEDTldstatqqelrAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQL----EQFKRAKANLDKNKQTL 1229
Cdd:pfam12128 783 KIERI-----------AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLarliADTKLRRAKLEMERKAS 851
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1230 EKENADLAGELRVLGQAKQEVehKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVE 1290
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKL--ATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVK 910
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
763-1437 |
3.24e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 763 IGQSKIFFRTGVLAHLEEERDL---------KITDVIMAFQAMCRGYLARKafakrqqqlTAMKVIQRNCAAYLKLRNwq 833
Cdd:PRK01156 122 LGISKDVFLNSIFVGQGEMDSLisgdpaqrkKILDEILEINSLERNYDKLK---------DVIDMLRAEISNIDYLEE-- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 834 wwRLFTKVKPLLQVTRQEEEMQAKEDELQKTKER-------QQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEA 906
Cdd:PRK01156 191 --KLKSSNLELENIKKQIADDEKSHSITLKEIERlsieynnAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 907 EEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLqlekvtaeAKIKKLEDE 986
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL--------SVLQKDYND 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 987 ILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASD 1066
Cdd:PRK01156 341 YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1067 FHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSEraaRNKAEKQKRDLGE 1146
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEK---IREIEIEVKDIDE 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1147 ELEALKtELEDTLDSTATQQELRAKReqevtvLKKALDEETRSHEAQVQEMRQKHAQAvEELTEQLEQFKRakANLDKNK 1226
Cdd:PRK01156 498 KIVDLK-KRKEYLESEEINKSINEYN------KIESARADLEDIKIKINELKDKHDKY-EEIKNRYKSLKL--EDLDSKR 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1227 QTLEKENADLAG-ELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGErarAELNDKVHKLQNEVESVTGMLNEAEGKAI- 1304
Cdd:PRK01156 568 TSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEIQENKIl 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1305 -----KLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKK 1379
Cdd:PRK01156 645 ieklrGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINET 724
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1380 LQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQ---ELDDLVVDLD 1437
Cdd:PRK01156 725 LESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKYLFEfnlDFDDIDVDQD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1264-1458 |
3.76e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1264 LQSKCSDGERARAELNDKVHKLQNEVESVtgmlnEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEE 1343
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1344 ERNSLQDQLDEEMEAK---------QNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQ-------- 1406
Cdd:COG3206 241 RLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQrilaslea 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1407 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLA 1458
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
887-1706 |
4.08e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 887 EEKNLLQEQLQAETELYaeaeEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMldleeqleeeEAAR 966
Cdd:PRK04863 280 ERRVHLEEALELRRELY----TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQ----------TALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 967 QKLQLEKVTA--EAKIKKLEDEILVMDDQNNKL--SKERK-LLEERISDLTTNLAEEE--------------------EK 1021
Cdd:PRK04863 346 QQEKIERYQAdlEELEERLEEQNEVVEEADEQQeeNEARAeAAEEEVDELKSQLADYQqaldvqqtraiqyqqavqalER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1022 AKNLTKLKNKHESMISELEVRLKKEEKSR-QELEKLKRKLE--GDASDFHEQIADLQAQIA-ELKMQLAKkeEELQAALA 1097
Cdd:PRK04863 426 AKQLCGLPDLTADNAEDWLEEFQAKEQEAtEELLSLEQKLSvaQAAHSQFEQAYQLVRKIAgEVSRSEAW--DVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1098 RLDDEIAQKNNAlkkiRELEGHISDLQEDLDSERAAR------NKAEKQKRDLGEELEALKTELEDTLDS-TATQQELRA 1170
Cdd:PRK04863 504 RLREQRHLAEQL----QQLRMRLSELEQRLRQQQRAErllaefCKRLGKNLDDEDELEQLQEELEARLESlSESVSEARE 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1171 KREQEVTVLKKaLDEETRSHEAQVQEMRQKHAqAVEELTEQL-EQFKRAKANLDKNKQTLEKEnadlagelRVLGQAKQE 1249
Cdd:PRK04863 580 RRMALRQQLEQ-LQARIQRLAARAPAWLAAQD-ALARLREQSgEEFEDSQDVTEYMQQLLERE--------RELTVERDE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1250 VEHKKKKLEAQVQEL-QSKCSDGERAR-----------AELNDKVhKLQN--EVESVTGML------NEAEGKAIKLAK- 1308
Cdd:PRK04863 650 LAARKQALDEEIERLsQPGGSEDPRLNalaerfggvllSEIYDDV-SLEDapYFSALYGPArhaivvPDLSDAAEQLAGl 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1309 ------------DVASLSSQLQDTQEL-----LQEETRQkLNVS--------------TKLRQLEEERNSLQDQLDEEME 1357
Cdd:PRK04863 729 edcpedlyliegDPDSFDDSVFSVEELekavvVKIADRQ-WRYSrfpevplfgraareKRIEQLRAEREELAERYATLSF 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1358 AKQNLER---HIS---TLNIQLSdskkklqdFASTVEALEEGKKRFQKEIEN-LTQQYEEKAAAYDKLEKTKNRLQQeLD 1430
Cdd:PRK04863 808 DVQKLQRlhqAFSrfiGSHLAVA--------FEADPEAELRQLNRRRVELERaLADHESQEQQQRSQLEQAKEGLSA-LN 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1431 DLVVDLDnqrqlvsnlekkqrkfdqLLAEEKNIsskyaderDRAEaEAREKETKALSLARaleealeakeeLERTNKMLK 1510
Cdd:PRK04863 879 RLLPRLN------------------LLADETLA--------DRVE-EIREQLDEAEEAKR-----------FVQQHGNAL 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1511 AEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAKLRLEVNMQ---ALKGQFERDLQA 1582
Cdd:PRK04863 921 AQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfSYEDAAEMLAKNSDlneKLRQRLEQAEQE 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1583 RDEQNEEkRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSaikGREEaikqlrKLQAQMKDFQRELE 1662
Cdd:PRK04863 1001 RTRAREQ-LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS---GAEE------RARARRDELHARLS 1070
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 13124875 1663 DARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1504-1912 |
4.72e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1504 RTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvnmqALKGQFE------ 1577
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEelekel 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1578 RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQaDSAIKGREEAIKQLRKLQAQMKDF 1657
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY-EEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1658 QRELEDARASRDEIfataKENEKKAKSLEADLMQLQEDLAAAERARkqadlekeelaeelasslsgrnALQDEKRRLEAR 1737
Cdd:PRK03918 327 EERIKELEEKEERL----EELKKKLKELEKRLEELEERHELYEEAK----------------------AKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1738 IAQLEEeleeeqGNMEAMSDRVRKATQQAEQLSNELATERStaqknesarqQLERQNKELRSKLHEMEGA---------- 1807
Cdd:PRK03918 381 LTGLTP------EKLEKELEELEKAKEEIEEEISKITARIG----------ELKKEIKELKKAIEELKKAkgkcpvcgre 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1808 --------VKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDK--KLKEILLQVEDERKM--------AEQYK 1869
Cdd:PRK03918 445 lteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKlkkynleeLEKKA 524
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 13124875 1870 EQAEKGNARVKQLKRQLEEAEEESQRINA---NRRKLQRELDEATE 1912
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEE 570
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1391-1928 |
4.80e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1391 EEGKKRFQKEIENLtQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKqrkFDQLLAEEKNISSKyaDE 1470
Cdd:PRK03918 144 DESREKVVRQILGL-DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE---LEEVLREINEISSE--LP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1471 RDRAEAEAREKETKALslaraleealeakeelertnKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEE 1550
Cdd:PRK03918 218 ELREELEKLEKEVKEL--------------------EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1551 LED------ELQATEDAKLRLEVNMQALKgQFERDLQARDEQNEEKRRQLQRQLHEYEtelEDERKQRALAAAAkkklEG 1624
Cdd:PRK03918 278 LEEkvkelkELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEERIKELE---EKEERLEELKKKL----KE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1625 DLKDLElqadsAIKGREEAIKQLRKLQAQMKDFQRELEDAraSRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARK 1704
Cdd:PRK03918 350 LEKRLE-----ELEERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1705 Q-ADLEKEELAEELASSLSGRNALQDEKRRLearIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKN 1783
Cdd:PRK03918 423 ElKKAIEELKKAKGKCPVCGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1784 ESARQQLERQNKELRSKLHEMEGAVK--SKFKSTIAALEAKIAQLEEQVEqearEKQAATKSLKQKDKKLKEIllqvedE 1861
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDEL------E 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1862 RKMAEQYKEQAEKGNARVKQLKRQLEE-------------AEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKL 1928
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKElepfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1529-1740 |
6.05e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1529 ELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDE 1608
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1609 RKQ-RALAAAAKKKLEGDLKDLELQADSAikgrEEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEA 1687
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1688 DLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQ 1740
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1719-1912 |
7.82e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1719 SSLSGRNALQDEKRRLEARI--AQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKE 1796
Cdd:COG3206 172 EARKALEFLEEQLPELRKELeeAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1797 LRSKLHEMEGAvkskfkSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDE-RKMAEQYKEQAEKG 1875
Cdd:COG3206 252 GPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEAELEAL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13124875 1876 NARVKQLKRQLEEAEEESQRINANRRK---LQRELDEATE 1912
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARE 365
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
844-1630 |
8.52e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.67 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 844 LLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRvrlaAKKQELEEI 923
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL----QQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 924 LHEMEARLEEEEDRGQQLQAERkkmaqqmldleeqleeeeaarqklqlekvtaeAKIKKLEDEILVMDDQNNKLSKERKL 1003
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLR--------------------------------ARIEELRAQEAVLEETQERINRARKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1004 LEerisdlttnLAEEeekAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRklegdasdfheQIADLQAQIAELKM 1083
Cdd:TIGR00618 293 AP---------LAAH---IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK-----------QQSSIEEQRRLLQT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1084 QLAKKEEelqaaLARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEelEALKTELEDTLDSTA 1163
Cdd:TIGR00618 350 LHSQEIH-----IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR--EQATIDTRTSAFRDL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1164 TQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQaveelteQLEQFKRAKANLDKNKQTLEKENAdlagelrvl 1243
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-------ESAQSLKEREQQLQTKEQIHLQET--------- 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1244 gQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELND------KVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQL 1317
Cdd:TIGR00618 487 -RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1318 QDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNL----ERHISTLNIQLSDSKKKLQDfASTVEALEEG 1393
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLaceqHALLRKLQPEQDLQDVRLHL-QQCSQELALK 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1394 KKRFQKEIENLTQQYEEKAAAY----------------DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLL 1457
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSirvlpkellasrqlalQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1458 AEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSskddvgknvhELEKSKRAL 1537
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA----------EIQFFNRLR 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1538 ETQMEEMKTQLEELEDELQATEDAKLrlevnmqALKGQFERDLQARDEQNEEKRRQLQRQLHEYEtELEDERKQRALAAA 1617
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSDEDILN-------LQCETLVQEEEQFLSRLEEKSATLGEITHQLL-KYEECSKQLAQLTQ 866
|
810
....*....|...
gi 13124875 1618 AKKKLEGDLKDLE 1630
Cdd:TIGR00618 867 EQAKIIQLSDKLN 879
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1280-1489 |
9.08e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1280 DKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAK 1359
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1360 QNLERHISTLNIQLSDskKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEkaaaydkLEKTKNRLQQELDDLVVDLDNQ 1439
Cdd:COG3883 96 YRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13124875 1440 RQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLA 1489
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
995-1706 |
9.16e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.65 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 995 NKLSKERKLLEEriSDLT-TNLAEEEEKAKnlTKLKNKHESMIsELEVRLKKEEKSRQELEK---LKRKLEG--DASDFH 1068
Cdd:COG3096 420 QALEKARALCGL--PDLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKayeLVCKIAGevERSQAW 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1069 EQIADLQAQIAELKMQlAKKEEELQAALARLDDEIAQKNNAlkkIRELEGHISDLQEDLDSERaarnkaekqkrDLGEEL 1148
Cdd:COG3096 495 QTARELLRRYRSQQAL-AQRLQQLRAQLAELEQRLRQQQNA---ERLLEEFCQRIGQQLDAAE-----------ELEELL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1149 EALKTELEDTLDSTATQQELRAKREQEvtvlkkaLDEetrsHEAQVQEMRQKH------AQAVEELTEQL-EQFKRAKAN 1221
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQRSELRQQ-------LEQ----LRARIKELAARApawlaaQDALERLREQSgEALADSQEV 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1222 LDKNKQTLEKEnadlagelRVLGQAKQEVEHKKKKLEAQVQELQSKCS--DGERAR----------AELNDKVhKLQN-- 1287
Cdd:COG3096 629 TAAMQQLLERE--------REATVERDELAARKQALESQIERLSQPGGaeDPRLLAlaerlggvllSEIYDDV-TLEDap 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1288 EVESVTGMLNEA------EGKAIKLAK-------------DVASLSSQLQDTQEL-----LQEETRQkLNVST------- 1336
Cdd:COG3096 700 YFSALYGPARHAivvpdlSAVKEQLAGledcpedlyliegDPDSFDDSVFDAEELedavvVKLSDRQ-WRYSRfpevplf 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1337 -------KLRQLEEERNSLQDQLDEEMEAKQNLERhistLNIQLSD--SKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1407
Cdd:COG3096 779 graarekRLEELRAERDELAEQYAKASFDVQKLQR----LHQAFSQfvGGHLAVAFAPDPEAELAALRQRRSELERELAQ 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1408 YEEKAAaydklektknRLQQELDDLVVDLDNQRQLVSNLEkkqrkfdqLLAEEknisskyaDERDRAEaEAREKETKALS 1487
Cdd:COG3096 855 HRAQEQ----------QLRQQLDQLKEQLQLLNKLLPQAN--------LLADE--------TLADRLE-ELREELDAAQE 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1488 LARALEEALEAKeelertnkmlkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAK 1562
Cdd:COG3096 908 AQAFIQQHGKAL-----------AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAV 976
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1563 LRLEVN---MQALKGQFERDLQARDEQNEeKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKG 1639
Cdd:COG3096 977 GLLGENsdlNEKLRARLEQAEEARREARE-QLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEE 1055
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13124875 1640 ReeaikqlrklqaqmkdfqreledARASRDEIFATAKEN-------EKKAKSLEADLMQLQEDLAAAER----ARKQA 1706
Cdd:COG3096 1056 R-----------------------ARIRRDELHEELSQNrsrrsqlEKQLTRCEAEMDSLQKRLRKAERdykqEREQV 1110
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
846-1611 |
9.71e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEI-- 923
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAkq 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 924 -LHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQklQLEKvtAEAKIKKLEDEILVMDDQNNKLSKERK 1002
Cdd:PRK04863 429 lCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS--QFEQ--AYQLVRKIAGEVSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1003 LLEERI------------SDLTTNLAEEEEKAKNLTKLKNKHESMI---SELEVRLKKEEKSRQELEKLKRKLEGDASDF 1067
Cdd:PRK04863 505 LREQRHlaeqlqqlrmrlSELEQRLRQQQRAERLLAEFCKRLGKNLddeDELEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1068 HEQIADLQAQIAELKmQLAKKEEELQAALARLDDeiaQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEE 1147
Cdd:PRK04863 585 RQQLEQLQARIQRLA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1148 LEALkteledTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMR---QKHAQAVEELTeqleqfkRAKANLDK 1224
Cdd:PRK04863 661 IERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQLAG 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1225 NKQTLEkenaDL---AGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSD-------GERARAELndkVHKLQNEVESVTG 1294
Cdd:PRK04863 728 LEDCPE----DLyliEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpevplfGRAAREKR---IEQLRAEREELAE 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1295 MLNEAEGKAIKLAKDVASLSSQL---------QDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERH 1365
Cdd:PRK04863 801 RYATLSFDVQKLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRL 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1366 ISTLNIQLSDS-KKKLQDFASTVEALEEGK---KRFQKEIENLT----------QQYEEKAAAYDKLEKTKNRLQQELDD 1431
Cdd:PRK04863 881 LPRLNLLADETlADRVEEIREQLDEAEEAKrfvQQHGNALAQLEpivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFA 960
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1432 LvVDLdNQRQLVSNLEKKQrkfdQLLAEEKNISSKYADERDRAEAEAREketkalslaraleealeakeelertnkmLKA 1511
Cdd:PRK04863 961 L-TEV-VQRRAHFSYEDAA----EMLAKNSDLNEKLRQRLEQAEQERTR----------------------------ARE 1006
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1512 EMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELedELQATEDAKLRLEVNmqalkgqfERDLQARDEQNEEKR 1591
Cdd:PRK04863 1007 QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL--GVPADSGAEERARAR--------RDELHARLSANRSRR 1076
|
810 820
....*....|....*....|
gi 13124875 1592 RQLQRQLHEYETELEDERKQ 1611
Cdd:PRK04863 1077 NQLEKQLTFCEAEMDNLTKK 1096
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
902-1349 |
1.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 902 LYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEeeaarqkLQLEKVTAEAKIK 981
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-------LEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 982 KLEDEIlvmddQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEvrlKKEEKSRQELEKLKRKLE 1061
Cdd:COG4717 120 KLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1062 GDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDD--EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEK 1139
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1140 QKRDLG-------------EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVE 1206
Cdd:COG4717 272 ILTIAGvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1207 ELTEQLEQFKRAK--ANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKvhK 1284
Cdd:COG4717 352 LLREAEELEEELQleELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--E 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1285 LQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQD--TQELLQEETRQKLNVSTKLRQLEEERNSLQ 1349
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
846-1264 |
1.12e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELyaeaeemrvrlaakkQELEEILH 925
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY---------------QELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 926 EMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLE 1005
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHE--------SMISELEVRLKKEEKSRQELEKLKRKLEG----DASDFHEQIAD 1073
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEarlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1074 LQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQ--KRDLGEELEAL 1151
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1152 KTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQemrqkhAQAVEELTEQLEQFKRAKANLDKNKQTLEK 1231
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE------ALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430
....*....|....*....|....*....|....*
gi 13124875 1232 ENADLAGELRVL--GQAKQEVEHKKKKLEAQVQEL 1264
Cdd:COG4717 454 ELAELEAELEQLeeDGELAELLQELEELKAELREL 488
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1175-1448 |
1.17e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.56 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1175 EVTVLKKALDEETRShEAQVQEMRQKHAQAVEELTE--QLEQFKRAKANLDKnKQTLEKENADLAGELrvlgqaKQEVEh 1252
Cdd:PHA02562 167 EMDKLNKDKIRELNQ-QIQTLDMKIDHIQQQIKTYNknIEEQRKKNGENIAR-KQNKYDELVEEAKTI------KAEIE- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1253 kkkKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTgmlneaegKAIKLAKD---VASLSSQLQDTQELLQEETR 1329
Cdd:PHA02562 238 ---ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ--------KVIKMYEKggvCPTCTQQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1330 QKLNVSTKLRQLEEERNSLQDQLDEEMEA---KQNLERHISTLNIQLSDSKKKLqdfastvealeegkKRFQKEIENLTQ 1406
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLVDKA--------------KKVKAAIEELQA 372
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 13124875 1407 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDnQRQLVSNLEK 1448
Cdd:PHA02562 373 EFVDNAEELAKLQDELDKIVKTKSELVKEKY-HRGIVTDLLK 413
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1037-1345 |
1.31e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 55.70 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1037 SELEVRLK-KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKnnalkkiRE 1115
Cdd:pfam00038 28 KLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1116 LEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT-------ELEDTLDSTATQQELRAKREQEVTVLkkaldeetr 1188
Cdd:pfam00038 101 AENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnheeevrELQAQVSDTQVNVEMDAARKLDLTSA--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1189 sheaqVQEMRQKHAQAVEELTEQLEQFKRAKanLDKNKQTLEKENADlagelrvLGQAKQEV---EHKKKKLEAQVQELQ 1265
Cdd:pfam00038 172 -----LAEIRAQYEEIAAKNREEAEEWYQSK--LEELQQAAARNGDA-------LRSAKEEItelRRTIQSLEIELQSLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1266 SKCSDGERARAELNDkvhKLQNEVESVTGMLNEAEGkaiKLAKDVASLSSQLQDTQELLQEETRQKLNVST--KLRQLEE 1343
Cdd:pfam00038 238 KQKASLERQLAETEE---RYELQLADYQELISELEA---ELQETRQEMARQLREYQELLNVKLALDIEIATyrKLLEGEE 311
|
..
gi 13124875 1344 ER 1345
Cdd:pfam00038 312 CR 313
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1528-1914 |
1.41e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1528 HELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFE-RDLQARDEQNEEKRRQLQRQLHEYEtELE 1606
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEELE-ELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1607 DERKQRALAAAAKKKLEGDLKDLELQadSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLE 1686
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQ--DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1687 ADLMQLQED----------------------------LAAAERARKQADLEKEELAEELASSLSGRNALQDEK-RRLEAR 1737
Cdd:COG4717 248 ARLLLLIAAallallglggsllsliltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEElEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1738 IAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNE--------------------SARQQLERQNKEL 1797
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraaleqaEEYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1798 RSKLHEMEGAVKSKFKS-TIAALEAKIAQLEEQVEQEAREKQAatksLKQKDKKLKEILLQVEDERKMAEQYKEQAEkgn 1876
Cdd:COG4717 408 EEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEE----LREELAELEAELEQLEEDGELAELLQELEE--- 480
|
410 420 430
....*....|....*....|....*....|....*...
gi 13124875 1877 arvkqLKRQLEEAEEESQRINANRRKLQRELDEATESN 1914
Cdd:COG4717 481 -----LKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1153-1481 |
1.59e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 56.40 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1153 TELEDTLDSTatqqelrakrEQEVTVLKKALDEETRSHE---AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTL 1229
Cdd:pfam06160 89 DEIEELLDDI----------EEDIKQILEELDELLESEEknrEEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1230 EK---------ENADLAGELRVLGQAKQEVEHKKKKLEaQVQELQSKCSDgeraraELNDKVHKLQNEVESVtgmlnEAE 1300
Cdd:pfam06160 159 EEefsqfeeltESGDYLEAREVLEKLEEETDALEELME-DIPPLYEELKT------ELPDQLEELKEGYREM-----EEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1301 G---KAIKLAKDVASLSSQLQDTQELLqEETRQKlNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLsdsk 1377
Cdd:pfam06160 227 GyalEHLNVDKEIQQLEEQLEENLALL-ENLELD-EAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYL---- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1378 kklqdfastvEALEEGKKRFQKEIENLTQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQ----LVSNLEKKQ 1450
Cdd:pfam06160 301 ----------EHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVayseLQEELEEIL 370
|
330 340 350
....*....|....*....|....*....|.
gi 13124875 1451 RKFDQLLAEEKNISSKYADERDrAEAEAREK 1481
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRK-DELEAREK 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
967-1115 |
1.73e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 967 QKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISEleVRLKKE 1046
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN--VRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1047 EKSRQ-ELEKLKRK---LEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRE 1115
Cdd:COG1579 91 YEALQkEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
977-1915 |
1.75e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 56.98 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 977 EAKIKKLEDEILVMDDQNNKLSKERklLEERISDLTTNLAEEE-----EKAKNLTKLKNKHESMISELEVRLKKEEKSRQ 1051
Cdd:TIGR01612 702 KSKIDKEYDKIQNMETATVELHLSN--IENKKNELLDIIVEIKkhihgEINKDLNKILEDFKNKEKELSNKINDYAKEKD 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1052 ELEKLKRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAALARLDDEIAQKNNALKKIREleGHISDLQEDLDSER 1131
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAK-QNYDKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFEN 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1132 AARNKAEKQKRDLGEELEALKTELEDtldstatqqELRAKREQEVTVLKKALDEETRSHEAQVQEMR-----QKHAQAVE 1206
Cdd:TIGR01612 857 NCKEKIDSEHEQFAELTNKIKAEISD---------DKLNDYEKKFNDSKSLINEINKSIEEEYQNINtlkkvDEYIKICE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1207 ELTEQLEQFK----RAKANLDKNKQTLEKENADlagELRVLGQAKQEVEHKKKKLEAQVQELQskCSDGERARAEL---- 1278
Cdd:TIGR01612 928 NTKESIEKFHnkqnILKEILNKNIDTIKESNLI---EKSYKDKFDNTLIDKINELDKAFKDAS--LNDYEAKNNELikyf 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1279 ND--------KVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKL--NVSTKLRQLEEERNSL 1348
Cdd:TIGR01612 1003 NDlkanlgknKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIgkNIELLNKEILEEAEIN 1082
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1349 QDQLDEEMEAKQ--NLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQY-EEKAAAYDKLEKTKNR- 1424
Cdd:TIGR01612 1083 ITNFNEIKEKLKhyNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYiDEIKAQINDLEDVADKa 1162
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1425 --------LQQELDDLVVDLDNQRQLVSNLEK------KQRKFDQLLAEEKNISSKYA------------DERDRAE--A 1476
Cdd:TIGR01612 1163 isnddpeeIEKKIENIVTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVKGINLSYGknlgklflekidEEKKKSEhmI 1242
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1477 EAREKETKALSLARALEEALEAKEELERTnkmLKAEMEDLVSSKDDVgKNVHELEKSKRALETQMEEMKTQLEELEDELQ 1556
Cdd:TIGR01612 1243 KAMEAYIEDLDEIKEKSPEIENEMGIEMD---IKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEES 1318
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1557 ATEDAKLRLEVNM-QALKGQFERDLQARDEQN------EEKRRQLQRQLHEYETELEDERKQ------RALAAAAKKKLE 1623
Cdd:TIGR01612 1319 DINDIKKELQKNLlDAQKHNSDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDD 1398
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1624 GDLKDLELQADSAIKGRE--EAIKQLRKLQAQMKDfqreledARASRDEIFATAKENEKK----------AKSLEADLMQ 1691
Cdd:TIGR01612 1399 INLEECKSKIESTLDDKDidECIKKIKELKNHILS-------EESNIDTYFKNADENNENvlllfkniemADNKSQHILK 1471
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1692 LQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSN 1771
Cdd:TIGR01612 1472 IKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIK 1551
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1772 EL--ATERSTAQKNESARQQLERQNKELRSklhEMEGAVKSKFKSTIAALEAKIAQLEEQV---------------EQEA 1834
Cdd:TIGR01612 1552 EIkdAHKKFILEAEKSEQKIKEIKKEKFRI---EDDAAKNDKSNKAAIDIQLSLENFENKFlkisdikkkindclkETES 1628
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1835 REKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQaekgnarvkqlKRQLEEAEEESQRINANRRKLQRELDEATESN 1914
Cdd:TIGR01612 1629 IEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQ-----------KKNIEDKKKELDELDSEIEKIEIDVDQHKKNY 1697
|
.
gi 13124875 1915 E 1915
Cdd:TIGR01612 1698 E 1698
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
887-1706 |
1.78e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.50 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 887 EEKNLLQEQLQAETELYAEAEEmrvrLAAKKQELEEILHEMEARLEEEEDRGQQLQAE-------RKKMAQQ-------- 951
Cdd:COG3096 279 ERRELSERALELRRELFGARRQ----LAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnlvQTALRQQekieryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 952 -MLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEI-----------LVMDDQN----------NKLSKERKLLEEriS 1009
Cdd:COG3096 355 dLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladyqQALDVQQtraiqyqqavQALEKARALCGL--P 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1010 DLT-TNLAEEEEKAKnlTKLKNKHESMIsELEVRLKKEEKSRQELEK---LKRKLEG--DASDFHEQIADLQAQIAELKM 1083
Cdd:COG3096 433 DLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKayeLVCKIAGevERSQAWQTARELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1084 QlAKKEEELQAALARLDDEIAQKNNAlkkIRELEGHISDLQEDLDSEraarnkaekqkRDLGEELEALKTELEDTLDSTA 1163
Cdd:COG3096 510 L-AQRLQQLRAQLAELEQRLRQQQNA---ERLLEEFCQRIGQQLDAA-----------EELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1164 TQQELRAKREQEvtvlkkaLDEetrsHEAQVQEMRQKH------AQAVEELTEQL-EQFKRAKANLDKNKQTLEKEnadl 1236
Cdd:COG3096 575 EAVEQRSELRQQ-------LEQ----LRARIKELAARApawlaaQDALERLREQSgEALADSQEVTAAMQQLLERE---- 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1237 agelRVLGQAKQEVEHKKKKLEAQVQELQ--SKCSDGERAR----------AELNDKVhKLQN--EVESVTGMLNEA--- 1299
Cdd:COG3096 640 ----REATVERDELAARKQALESQIERLSqpGGAEDPRLLAlaerlggvllSEIYDDV-TLEDapYFSALYGPARHAivv 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1300 ---EGKAIKLAK-------------DVASLSSQLQDTQEL-----LQEETRQkLNVST--------------KLRQLEEE 1344
Cdd:COG3096 715 pdlSAVKEQLAGledcpedlyliegDPDSFDDSVFDAEELedavvVKLSDRQ-WRYSRfpevplfgraarekRLEELRAE 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1345 RNSLQDQLDEEMEAKQNLERhistLNIQLSD--SKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAaydklektk 1422
Cdd:COG3096 794 RDELAEQYAKASFDVQKLQR----LHQAFSQfvGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQ--------- 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1423 nRLQQELDDLVVDLDNQRQLVSNLEkkqrkfdqLLAEEknisskyaDERDRAEaEAREKETKALSLARALEEALEAKeel 1502
Cdd:COG3096 861 -QLRQQLDQLKEQLQLLNKLLPQAN--------LLADE--------TLADRLE-ELREELDAAQEAQAFIQQHGKAL--- 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1503 ertnkmlkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAKLRLEVN---MQALKG 1574
Cdd:COG3096 920 --------AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLGENsdlNEKLRA 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1575 QFERDLQARDEQNeEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSaikGREEaikqlrKLQAQM 1654
Cdd:COG3096 992 RLEQAEEARREAR-EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA---EAEE------RARIRR 1061
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1655 KDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:COG3096 1062 DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1656-1929 |
1.82e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1656 DFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARkqadlekeelaeelasslsgrnALQDEKRRLE 1735
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ----------------------ALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1736 ARIaqleeeleeEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKST 1815
Cdd:TIGR02169 225 GYE---------LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1816 IAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLE----EAEE 1891
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraELEE 375
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 13124875 1892 ESQRINANRRKL---QRELDEATESNEAMGREVNALKSKLR 1929
Cdd:TIGR02169 376 VDKEFAETRDELkdyREKLEKLKREINELKRELDRLQEELQ 416
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1509-1707 |
2.71e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNE 1588
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1589 EKR----------RQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQ 1658
Cdd:COG4942 119 QPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13124875 1659 RELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQAD 1707
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
979-1160 |
2.80e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 979 KIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKr 1058
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1059 klegdasdfheQIADLQAQIAELKMQLAKKEEELQAALARLDdeiaqknNALKKIRELEGHISDLQEDLDSERAARNKAE 1138
Cdd:COG1579 90 -----------EYEALQKEIESLKRRISDLEDEILELMERIE-------ELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|..
gi 13124875 1139 KQKRDLGEELEALKTELEDTLD 1160
Cdd:COG1579 152 AELEAELEELEAEREELAAKIP 173
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1301-1913 |
3.49e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.61 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1301 GKAIKLAKDVASLSSQLQDTQEL--------LQEETRQKlNVSTKLRQLEEERNSLQDQLDEEMEAkqnlerhistLNIQ 1372
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLhfgyksdeTLIASRQE-ERQETSAELNQLLRTLDDQWKEKRDE----------LNGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1373 LSDSKKKLQDFASTVEALEEGKKRFQKeienltqqyeekaaayDKLEKTKNRLQQeLDDLVVDLDNQRQLVSNLEKKQRK 1452
Cdd:pfam12128 310 LSAADAAVAKDRSELEALEDQHGAFLD----------------ADIETAAADQEQ-LPSWQSELENLEERLKALTGKHQD 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1453 FDQLL-AEEKNISSKYADERDRAEAE-AREKETKALSLARALEEALEAKEELERTNKMLKAEMEDlvsSKDDVGKNVHEL 1530
Cdd:pfam12128 373 VTAKYnRRRSKIKEQNNRDIAGIKDKlAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNE---EEYRLKSRLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1531 eKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERK 1610
Cdd:pfam12128 450 -KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSE-LRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1611 QRALAAAAK----KKLEGDLKD-LELQADSAIKGR--------EEAIKQLRKLQAQMKDFQR-----------ELEDARA 1666
Cdd:pfam12128 528 QLFPQAGTLlhflRKEAPDWEQsIGKVISPELLHRtdldpevwDGSVGGELNLYGVKLDLKRidvpewaaseeELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1667 SRDEIFATAKENEKKAKS----LEADLMQLQEDLAAAERARKQADLEKEELAEELAS-SLSGRNALQDEKRRLEARI--- 1738
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEqlvqANGELEKASREETFARTALKNARLDLRRLFDEKQSeKDKKNKALAERKDSANERLnsl 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1739 -AQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTA-----QKNESARQQLERQNKELRSKLHEmEGAVKSKF 1812
Cdd:pfam12128 688 eAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQlallkAAIAARRSGAKAELKALETWYKR-DLASLGVD 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1813 KSTIAALEAKIAQLEEQVEQEAREKQAATkslkQKDKKLKEILLQVEDERKMAeqyKEQAEKGNARVK-QLKRQLEEAEE 1891
Cdd:pfam12128 767 PDVIAKLKREIRTLERKIERIAVRRQEVL----RYFDWYQETWLQRRPRLATQ---LSNIERAISELQqQLARLIADTKL 839
|
650 660
....*....|....*....|..
gi 13124875 1892 ESQRINANRRKLQRELDEATES 1913
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSEN 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1357-1611 |
3.74e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1357 EAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDL 1436
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1437 DNQRQLVSNLEKKQRKFDQLLAEEKNISSKyaderDRAEAEAREKETKALSLARaleealeakeelertnkmlKAEMEDL 1516
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPE-----DFLDAVRRLQYLKYLAPAR-------------------REQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1517 VSSKDdvgknvhELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDlQARDEQNEEKRRQLQR 1596
Cdd:COG4942 156 RADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL-AAELAELQQEAEELEA 227
|
250
....*....|....*
gi 13124875 1597 QLHEYETELEDERKQ 1611
Cdd:COG4942 228 LIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1754-1938 |
4.30e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1754 AMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKsKFKSTIAALEAKIAQLEEQVEQE 1833
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1834 AREKQAATKSLKQ---------KDKKLKEILLQ--VEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRK 1902
Cdd:COG4942 96 RAELEAQKEELAEllralyrlgRQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 13124875 1903 LQRELDEATESNEAMGREVNALKSKLRGPPPQETSQ 1938
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1045-1455 |
6.17e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.92 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1045 KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKK------IRELEG 1118
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlstlsLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1119 HISDLQEDLDSERAARNKAEKQkrdlgeeLEALKTELEDTLDSTATQQelraKREQEVTVLKKALDEETRSHEAQVQEMR 1198
Cdd:PRK11281 129 RLAQTLDQLQNAQNDLAEYNSQ-------LVSLQTQPERAQAALYANS----QRLQQIRNLLKGGKVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1199 QKHAQAVEelteqleqfkrakANLDKNKQTLEKENadlagELRVLGQAKQ-EVEHKKKKLEAQVQELQSKCSDGERARAE 1277
Cdd:PRK11281 198 QAEQALLN-------------AQNDLQRKSLEGNT-----QLQDLLQKQRdYLTARIQRLEHQLQLLQEAINSKRLTLSE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1278 lnDKVHKLQNEVESvtgmlNEAEGKAIkLAKDVAS---LSSQLQDTQELLQEETRQKLNVSTKL-------RQLEEERNS 1347
Cdd:PRK11281 260 --KTVQEAQSQDEA-----ARIQANPL-VAQELEInlqLSQRLLKATEKLNTLTQQNLRVKNWLdrltqseRNIKEQISV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1348 LQ------------------DQLDEEMeAKQ--NLERHISTLNIQlsdsKKKLQDFASTVEALEEG-KKRFQKEIEN-LT 1405
Cdd:PRK11281 332 LKgslllsrilyqqqqalpsADLIEGL-ADRiaDLRLEQFEINQQ----RDALFQPDAYIDKLEAGhKSEVTDEVRDaLL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 13124875 1406 QQYEEKAAAYDKLEKTKNRLQQELDDLVVdldNQRQLVSNLEKKQRKFDQ 1455
Cdd:PRK11281 407 QLLDERRELLDQLNKQLNNQLNLAINLQL---NQQQLLSVSDSLQSTLTQ 453
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1193-1706 |
6.59e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1193 QVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGE 1272
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1273 RARAELNDKVHKLQ------NEVESVTGMLNEAEGKA-----------IKLAKDVASLSSQLQDTQELLQ--EETRQKLN 1333
Cdd:PRK01156 253 RYESEIKTAESDLSmeleknNYYKELEERHMKIINDPvyknrnyindyFKYKNDIENKKQILSNIDAEINkyHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1334 VSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEAL----EEGKKRFQKEIENLTQQYE 1409
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiSEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1410 EKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQR--KFDQLLAEEK--NISSKYADERDRAEAEAREKETKA 1485
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpVCGTTLGEEKsnHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1486 LSLaraleeALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETqMEEMKTQLEELEDELQAT--EDAKL 1563
Cdd:PRK01156 493 KDI------DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINE-LKDKHDKYEEIKNRYKSLklEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1564 RLEVNMQALKGQFERDLQARDEQNEEKRRQL---QRQLHEYETELEDERKqralaaaakkKLEGDLKDLELQADSAikgr 1640
Cdd:PRK01156 566 KRTSWLNALAVISLIDIETNRSRSNEIKKQLndlESRLQEIEIGFPDDKS----------YIDKSIREIENEANNL---- 631
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1641 EEAIKQLRKLQAQMKDFQRELEDAR---ASRDEIFATAKENEKKAKSLEADLMQL--QEDLAAAERARKQA 1706
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNLKKSrkALDDAKANRARLES 702
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1589-1840 |
6.72e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1589 EKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADsaikgreEAIKQLRKLQAQMKDFQRELedarasr 1668
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAEL------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1669 deifataKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEelassLSGRNALQDEKRR--LEARIAQLEEELE 1746
Cdd:COG4942 86 -------AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLqyLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1747 EEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKfKSTIAALEAKIAQL 1826
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEELEALIARL 232
|
250
....*....|....
gi 13124875 1827 EEQVEQEAREKQAA 1840
Cdd:COG4942 233 EAEAAAAAERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1033-1230 |
7.52e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1033 ESMISELEVRLkkeEKSRQELEKLKRK-----LEGDASDFHEQIADLQAQIAELKMQLAkkeeELQAALARLDDEIAQKN 1107
Cdd:COG3206 181 EEQLPELRKEL---EEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELA----EAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1108 NALKKIRELEGhISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELedtldstatqQELRAKREQEVTVLKKALDEET 1187
Cdd:COG3206 254 DALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI----------AALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13124875 1188 RSHEAQVQEMRQKHAQA---VEELTEQLEQFKRAKANLDKNKQTLE 1230
Cdd:COG3206 323 EALQAREASLQAQLAQLearLAELPELEAELRRLEREVEVARELYE 368
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
999-1410 |
7.85e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 999 KERKLLEERISDLTTNL----AEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADL 1074
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1075 QAQIAELKMQLAKKE--EELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQkrdlgEELEALK 1152
Cdd:TIGR00606 768 EEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ-----HELDTVV 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1153 TELEDTldstatqQELRAKREQEVTVLKKALDeETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQtlekE 1232
Cdd:TIGR00606 843 SKIELN-------RKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKE----Q 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1233 NADLAGELRVLGQAKQEVEHKK----KKLEAQVQELQSKCSDGERARAELNDKVH--------KLQNEVESVTGMLNEAE 1300
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKetsnKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgkddylkQKETELNTVNAQLEECE 990
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1301 GKAIKLAKDVASLSSQL--QDTQELLQEETRQKLNVSTKLRQLEEERNSL-----QDQLDEEMEAKQNLERHISTLNIQL 1373
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVLQMKQEHQKLEENIDLIKRNH 1070
|
410 420 430
....*....|....*....|....*....|....*..
gi 13124875 1374 SDSKKKLQDFASTVEALEegKKRFQKEIENLTQQYEE 1410
Cdd:TIGR00606 1071 VLALGRQKGYEKEIKHFK--KELREPQFRDAEEKYRE 1105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
836-1235 |
8.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 836 RLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAE------NELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEM 909
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 910 RVRLAAKKQELEEILHEMEARLEEE-----------EDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEA 978
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 979 KIK-KLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKaknLTKLKNKHESMISELEVRLKKEEKSRQELEKLK 1057
Cdd:COG4717 249 RLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL---LAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1058 RKLEGDASDFHEQIADLQAQIAELKMQLAKKEEE----------------LQAALARLDDEIAQKNNALKKIRELEGHIS 1121
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqleeleqeiaalLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1122 DLQEDLDSERAARNK--AEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKaldeetrshEAQVQEMRQ 1199
Cdd:COG4717 406 ELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE---------DGELAELLQ 476
|
410 420 430
....*....|....*....|....*....|....*....
gi 13124875 1200 KHAQAVEELTEQLEQFKR---AKANLDKNKQTLEKENAD 1235
Cdd:COG4717 477 ELEELKAELRELAEEWAAlklALELLEEAREEYREERLP 515
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
884-1216 |
9.43e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 884 QLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMldleeqLEEEE 963
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK------NKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 964 AARQKLQLEKVTAEAKIKKLEDEILVMDDQnnklsKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRL 1043
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEE-----QKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1044 KKEEKSRqeleklKRKLEGDASDfHEQIADLQAQIAELKMQLAKKEEELQAALA-----------RLDDEIAQKNNALKK 1112
Cdd:pfam12128 750 KALETWY------KRDLASLGVD-PDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERA 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1113 IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQElRAKREQevtvlkkaLDEETRSHEA 1192
Cdd:pfam12128 823 ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE-DANSEQ--------AQGSIGERLA 893
|
330 340
....*....|....*....|....
gi 13124875 1193 QVQEMRQKHAQAVEELTEQLEQFK 1216
Cdd:pfam12128 894 QLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
846-1262 |
9.53e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKaENELKELEQKHsQLTEEKNLLQEQLQAETELYAEAEEM---------RVRLAAK 916
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEK-EEKAREVERRR-KLEEAEKARQAEMDRQAAIYAEQERMamerereleRIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 917 KQELEEIlhemearleeeedRGQQLQAERKKMAQQmldleeqleeeeaarQKLQLEKVTAEAKIKkledeilvmddQNNK 996
Cdd:pfam17380 359 KRELERI-------------RQEEIAMEISRMREL---------------ERLQMERQQKNERVR-----------QELE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 997 LSKERKLLEErisdlttnlaEEEEKAKnltklknkhESMISELEVRLKKEEKSRQELEKLkrklegdasdfheqiadlqa 1076
Cdd:pfam17380 400 AARKVKILEE----------ERQRKIQ---------QQKVEMEQIRAEQEEARQREVRRL-------------------- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1077 qiaelkmqlakkEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLgeeleaLKTELE 1156
Cdd:pfam17380 441 ------------EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI------LEKELE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1157 DTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDknkqTLEKEnadl 1236
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE----AMERE---- 574
|
410 420
....*....|....*....|....*.
gi 13124875 1237 agelRVLGQAKQEVEHKKKKLEAQVQ 1262
Cdd:pfam17380 575 ----REMMRQIVESEKARAEYEATTP 596
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1548-1927 |
1.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1548 LEELEdELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYeTELEDERKQRALAAAAKKKLEGDLK 1627
Cdd:PTZ00121 1029 IEELT-EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDF-DAKEDNRADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1628 DL-----ELQADSAIKGREEA--IKQLRKLQ-------------AQMKDFQRELEDARasRDEIFATAKENEKKAKSLEA 1687
Cdd:PTZ00121 1107 ETgkaeeARKAEEAKKKAEDArkAEEARKAEdarkaeearkaedAKRVEIARKAEDAR--KAEEARKAEDAKKAEAARKA 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1688 DLMQLQEDLAAAERARKQADLEKEelaeelasslsgrnalQDEKRRLEARIAQLeeeleeeqgnmEAMSDRVRKAtqqae 1767
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKA----------------EEERKAEEARKAED-----------AKKAEAVKKA----- 1232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1768 qlsnelatERSTAQKNESARQQLERQNKELRsklhEMEGAVKSKFKSTIAALEAKIAQLEEQVeQEAREKQAATKSLKQK 1847
Cdd:PTZ00121 1233 --------EEAKKDAEEAKKAEEERNNEEIR----KFEEARMAHFARRQAAIKAEEARKADEL-KKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1848 DKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSK 1927
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
850-1476 |
1.07e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 850 QEEEMQAKEDELQKTKERQQKAENELKELEQKHSQlteeknllqeQLQAETELYAEAEEMRVRLAAKKQELEEIlhemEA 929
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGK----------NLDDEDELEQLQEELEARLESLSESVSEA----RE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 930 RLEEEEDRGQQLQAERKKMAQQmldleeqLEEEEAARQKL-QLEKVTAEAkikkLEDEILVMDDQNNKLSKERKLLEERI 1008
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAAR-------APAWLAAQDALaRLREQSGEE----FEDSQDVTEYMQQLLERERELTVERD 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1009 sDLTTNLAEEEEKAKNL--------TKLKNKHE----SMISELEVRLKKEE---------KSRQ-----ELEKLKRKLEG 1062
Cdd:PRK04863 649 -ELAARKQALDEEIERLsqpggsedPRLNALAErfggVLLSEIYDDVSLEDapyfsalygPARHaivvpDLSDAAEQLAG 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1063 dASDFHEQIADLQAQIAELKMQLAKKEEELQAALarldDEIAQKNNALKKIREL--------EGHISDLQEDLD--SERA 1132
Cdd:PRK04863 728 -LEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVV----VKIADRQWRYSRFPEVplfgraarEKRIEQLRAEREelAERY 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1133 ARNKAEKQKrdLGEELEALKTELEDTL------DSTATQQELRAKREQEVTVLKkALDEETRSHEAQVQEMRQK------ 1200
Cdd:PRK04863 803 ATLSFDVQK--LQRLHQAFSRFIGSHLavafeaDPEAELRQLNRRRVELERALA-DHESQEQQQRSQLEQAKEGlsalnr 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1201 ------------HAQAVEELTEQLEQFKRAKANLDKNKQTLEKenadLAGELRVLGQAKQEVEHKKKKLEaQVQELQSKC 1268
Cdd:PRK04863 880 llprlnlladetLADRVEEIREQLDEAEEAKRFVQQHGNALAQ----LEPIVSVLQSDPEQFEQLKQDYQ-QAQQTQRDA 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1269 SDGERARAELNDKVHKLQNEvESVtGMLNEAegkaiklakdvASLSSQLQdtqellqeetrqklnvsTKLRQLEEERnsl 1348
Cdd:PRK04863 955 KQQAFALTEVVQRRAHFSYE-DAA-EMLAKN-----------SDLNEKLR-----------------QRLEQAEQER--- 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1349 qDQLDEEMEAKQNlerhistlniQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAydklektknRLQQE 1428
Cdd:PRK04863 1002 -TRAREQLRQAQA----------QLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEE---------RARAR 1061
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1429 LDDLVVDLDNQRQLVSNLEKKQRKF----DQLLAEEKNISSKYADERDRAEA 1476
Cdd:PRK04863 1062 RDELHARLSANRSRRNQLEKQLTFCeaemDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
982-1288 |
1.13e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.15 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 982 KLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLE 1061
Cdd:pfam19220 66 KLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1062 GDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEG-------HISDLQEDLDSERAAR 1134
Cdd:pfam19220 146 EEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETqldatraRLRALEGQLAAEQAER 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1135 NKAEKQkrdLGEELEALKTEL-----------------EDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEM 1197
Cdd:pfam19220 226 ERAEAQ---LEEAVEAHRAERaslrmklealtaraaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1198 RQKHAQaveeLTEQLEQFKRAKANLDKNKQTLEKEnadLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAE 1277
Cdd:pfam19220 303 EADLER----RTQQFQEMQRARAELEERAEMLTKA---LAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRR 375
|
330
....*....|.
gi 13124875 1278 LNDkvhKLQNE 1288
Cdd:pfam19220 376 LKE---ELQRE 383
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1191-1427 |
1.30e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1191 EAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKEN--ADLAGELRVLGQAKQEvehkkkkLEAQVQELQSKc 1268
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSE-------LESQLAEARAE- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1269 sdgeraRAELNDKVHKLQNEVESVTGMLNEAEGKAIklakdVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSL 1348
Cdd:COG3206 235 ------LAEAEARLAALRAQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1349 QDQLDEEmeakqnLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRF---QKEIENLTQQYEEKAAAYDKLEktkNRL 1425
Cdd:COG3206 304 RAQLQQE------AQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLL---QRL 374
|
..
gi 13124875 1426 QQ 1427
Cdd:COG3206 375 EE 376
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
851-1031 |
1.58e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAE----TELYAEAEEMRVRLAAKKQELEE---- 922
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAEllra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 923 -------------------------------ILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQL 971
Cdd:COG4942 113 lyrlgrqpplalllspedfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 972 EKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNK 1031
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1345-1803 |
1.81e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1345 RNSLQDQLDEEMEAKQNLERHISTLNI-QLSDSKKKLQDFASTVEALEEgkkrFQKEIENLTQQYEEKAAAYDKLEKTKN 1423
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1424 RLQQELDdLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKyADERDRAEAEAREKETKALSLARaleealeakeele 1503
Cdd:COG4717 120 KLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELREL-EEELEELEAELAELQEELEELLE------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1504 RTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAK---------------LRLEVN 1568
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaalLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1569 MQALKGQFER----------------DLQARDEQNEEKRRQLQRQLHEYE----TELEDERKQRALAAAAKKKLEGDLKD 1628
Cdd:COG4717 265 GGSLLSLILTiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1629 LELQADSAIKGREEAIKQLRkLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQAdl 1708
Cdd:COG4717 345 RIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL-- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1709 ekeelaeelasslsgrnALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERstaqknesARQ 1788
Cdd:COG4717 422 -----------------LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE--------LLQ 476
|
490
....*....|....*
gi 13124875 1789 QLERQNKELRSKLHE 1803
Cdd:COG4717 477 ELEELKAELRELAEE 491
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1780 |
2.09e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1538 ETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAA 1617
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1618 AKKKLEGDLKDLE--LQADSAikgrEEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQED 1695
Cdd:COG3883 94 ALYRSGGSVSYLDvlLGSESF----SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1696 LAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELAT 1775
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
....*
gi 13124875 1776 ERSTA 1780
Cdd:COG3883 250 GAAGA 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
965-1177 |
2.27e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 965 ARQKLQlekvTAEAKIK--KLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISEL--E 1040
Cdd:COG3206 187 LRKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1041 VRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAkkeEELQAALARLDDEIAQknnALKKIRELEGHI 1120
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1121 SDLQEDLDSEraarNKAEKQKRDLGEELEALKTELEDTLdstATQQELRAKREQEVT 1177
Cdd:COG3206 337 AQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1004-1923 |
2.45e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.91 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1004 LEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQElEKLKRKLEGD-------ASDFHEQIADLQA 1076
Cdd:PTZ00440 510 IKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKD-EKLKRSMKNDiknkikyIEENVDHIKDIIS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1077 QIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIREL--EGHISDLQEDLDS-------------ERAARNKAEKQK 1141
Cdd:PTZ00440 589 LNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYIlnKFYKGDLQELLDElshflddhkylyhEAKSKEDLQTLL 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1142 RDLGEELEALKTELEDTLDSTAtqQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKAN 1221
Cdd:PTZ00440 669 NTSKNEYEKLEFMKSDNIDNII--KNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEK 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1222 LDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKcsdgeraRAELNDKVHKLQNEVESVTGMLNEAEG 1301
Cdd:PTZ00440 747 LEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNK-------ENKISNDINILKENKKNNQDLLNSYNI 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1302 KAIKLAKDVASLSSQLQDTQELLQEEtrqklNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIqLSDSKKKLQ 1381
Cdd:PTZ00440 820 LIQKLEAHTEKNDEELKQLLQKFPTE-----DENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKT-LNIAINRSN 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1382 DFASTVEALEEGKKRFQKEIENLTQQYE--------EKAAAYDKLEKTKNRLQQELDDLVVDldnqrQLVSNLEKKQRKF 1453
Cdd:PTZ00440 894 SNKQLVEHLLNNKIDLKNKLEQHMKIINtdniiqknEKLNLLNNLNKEKEKIEKQLSDTKIN-----NLKMQIEKTLEYY 968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1454 DQLlaeEKNISSKyaDERDRAEAEAREKETKALSlARALEEALEAKEELERTNKMLKAEMEDLV--SSKDDVGKNvHELE 1531
Cdd:PTZ00440 969 DKS---KENINGN--DGTHLEKLDKEKDEWEHFK-SEIDKLNVNYNILNKKIDDLIKKQHDDIIelIDKLIKEKG-KEIE 1041
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1532 KSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERKQ 1611
Cdd:PTZ00440 1042 EKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVE-ALLKKIDENKNKLIEIKNKSHEHVVNADKEKNK 1120
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1612 ralAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMkdfQRELEDARASRDEIFATAKENEKKAKSLEADLMQ 1691
Cdd:PTZ00440 1121 ---QTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVN---EIEIEYERILIDHIVEQINNEAKKSKTIMEEIES 1194
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1692 LQEDLaaaerarKQADLEKEELAEELASSLSgRNALQDEKRRLEARIAQLEEELEEEQGNMEAmSDRVRKATQQAEQLSN 1771
Cdd:PTZ00440 1195 YKKDI-------DQVKKNMSKERNDHLTTFE-YNAYYDKATASYENIEELTTEAKGLKGEANR-STNVDELKEIKLQVFS 1265
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1772 ELATERSTAQKNESARQQLERQNKELRS---------------KLHEMEGAVKSKFKST---IAALEAKIAQLEE----- 1828
Cdd:PTZ00440 1266 YLQQVIKENNKMENALHEIKNMYEFLISidsekilkeilnstkKAEEFSNDAKKELEKTdnlIKQVEAKIEQAKEhknki 1345
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1829 -------QVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQleEAEEESQRINANRR 1901
Cdd:PTZ00440 1346 ygsledkQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKIDFLNKH--EAIEPSNSKEVNII 1423
|
970 980
....*....|....*....|...
gi 13124875 1902 KLQRELDEATE-SNEAMGREVNA 1923
Cdd:PTZ00440 1424 KITDNINKCKQySNEAMETENKA 1446
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1212 |
2.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAetelyAEAEEmrvRLAAKKQELEEILh 925
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-----ASAER---EIAELEAELERLD- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 926 emearleEEEDRGQQLQAERKKmaqqmldleeqleeEEAARQKLQLEKVTAEAKIKKLEDEIlvmDDQNNKLSKERKLLE 1005
Cdd:COG4913 682 -------ASSDDLAALEEQLEE--------------LEAELEELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLE 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELE-KLKRKLEGDASDFHEQIADLQAQIAELkmq 1084
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEeELERAMRAFNREWPAETADLDADLESL--- 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1085 lakkeEELQAALARLDDE--IAQKNNALKKIRELEGH-ISDLQEDLDSERAArnkAEKQKRDLGEELEALKTELEDTLds 1161
Cdd:COG4913 815 -----PEYLALLDRLEEDglPEYEERFKELLNENSIEfVADLLSKLRRAIRE---IKERIDPLNDSLKRIPFGPGRYL-- 884
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1162 tatQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQL 1212
Cdd:COG4913 885 ---RLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1101-1466 |
2.55e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1101 DEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKrdlgEELEALKTELEDtldstATQQELRAKReqEVTVLK 1180
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQ-----APAKLRQAQA--ELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1181 KALDEETRSH---------EAQVQEMRQKHAQAVEELTE-------QLEQFKRAKANLDKNKQTLEKENADLAG------ 1238
Cdd:PRK11281 108 DDNDEETRETlstlslrqlESRLAQTLDQLQNAQNDLAEynsqlvsLQTQPERAQAALYANSQRLQQIRNLLKGgkvggk 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1239 ----ELRVLGQAKQ-----EVEHKKKKLEA--QVQELqskcsdGERARAELNDKVHKLQNEVESVTGMLNEaegKAIKLA 1307
Cdd:PRK11281 188 alrpSQRVLLQAEQallnaQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQLQLLQEAINS---KRLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1308 KDVASLSSQLQDTQE-----LLQEETRQKLNVSTKLRQLEEERNSL-QD------QLDEEMEAKQNLERHISTLNIQLSD 1375
Cdd:PRK11281 259 EKTVQEAQSQDEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLtQQnlrvknWLDRLTQSERNIKEQISVLKGSLLL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1376 SK------------KKLQDFAST-----VEALEEGKKR---FQKE--IENLTQQYEEKA-----AAYDKLEKTKNRLqqe 1428
Cdd:PRK11281 339 SRilyqqqqalpsaDLIEGLADRiadlrLEQFEINQQRdalFQPDayIDKLEAGHKSEVtdevrDALLQLLDERREL--- 415
|
410 420 430
....*....|....*....|....*....|....*...
gi 13124875 1429 LDDLVVDLDNQRQLVSNLEKKQRkfdQLLAEEKNISSK 1466
Cdd:PRK11281 416 LDQLNKQLNNQLNLAINLQLNQQ---QLLSVSDSLQST 450
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1310-1536 |
2.76e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1310 VASLSSQLQDTQELLQEETRQKLN-VSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVE 1388
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1389 ALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRL----QQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIS 1464
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1465 SKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRA 1536
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1173-1481 |
2.78e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.15 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1173 EQEVTVLKKALDEETRSHE---AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLE---------KENADLAGEL 1240
Cdd:PRK04778 118 EEDIEQILEELQELLESEEknrEEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEeefsqfvelTESGDYVEAR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1241 RVLGQAKQEVEHKKKKLEaQVQELQSKCSDgeraraELNDKVHKLQNEVESVTgmlneAEG---KAIKLAKDVASLSSQL 1317
Cdd:PRK04778 198 EILDQLEEELAALEQIME-EIPELLKELQT------ELPDQLQELKAGYRELV-----EEGyhlDHLDIEKEIQDLKEQI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1318 QDTQELLqEETRQKlNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLsdskkklqdfastvEALEEGKKRF 1397
Cdd:PRK04778 266 DENLALL-EELDLD-EAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFL--------------EHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1398 QKEIENLTQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQ----LVSNLEKKQRKFDQLLAEEKNISSKYADE 1470
Cdd:PRK04778 330 KEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIayseLQEELEEILKQLEEIEKEQEKLSEMLQGL 409
|
330
....*....|.
gi 13124875 1471 RDrAEAEAREK 1481
Cdd:PRK04778 410 RK-DELEAREK 419
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
1111-1481 |
2.93e-06 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 52.15 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1111 KKIRELEGHISDLQEDLDSERAarNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSH 1190
Cdd:COG4477 78 KQLPEIEELLFDAEEAADKFRF--KKAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYRELRKTL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1191 EAQvqemRQKHAQAVEELTEQLEQFKrakANLDKNKQTLEKENADLAGElrVLGQAKQEVEHKKKKLEaQVQELQSKCSD 1270
Cdd:COG4477 156 LAH----RHSFGPAAEELEKQLEELE---PEFEEFEELTESGDYLEARE--ILEQLEEELNALEELME-EIPPLLKELQT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1271 geraraELNDKVHKLQNEVESVtgmlnEAEG---KAIKLAKDVASLSSQLQDTQELLqEETRQKlNVSTKLRQLEEERNS 1347
Cdd:COG4477 226 ------ELPDQLEELKSGYREM-----KEQGyvlEHLNIEKEIEQLEEQLKEALELL-EELDLD-EAEEELEEIEEEIDE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1348 LQDQLDEEMEAKQNLERHISTLniqlsdskkklqdfASTVEALEEGKKRFQKEIENLTQQY---EEKAAAYDKLEKTKNR 1424
Cdd:COG4477 293 LYDLLEKEVEAKKYVDKNQEEL--------------EEYLEHLKEQNRELKEEIDRVQQSYrlnENELEKVRNLEKQIEE 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1425 LQQELDDLVVDLDNQR----QLVSNLEKKQRKFDQLLAEEKNISSKYADERDRaEAEAREK 1481
Cdd:COG4477 359 LEKRYDEIDERIEEEKvaysELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKD-ELEAREK 418
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1297-1896 |
3.54e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1297 NEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDS 1376
Cdd:pfam05557 16 NEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1377 KKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKaaaydklEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQrkfdql 1456
Cdd:pfam05557 96 ESQLADAREVISCLKNELSELRRQIQRAELELQST-------NSELEELQERLDLLKAKASEAEQLRQNLEKQQ------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1457 laeeknisskyadeRDRAEAEAREKEtkaLSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRA 1536
Cdd:pfam05557 163 --------------SSLAEAEQRIKE---LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1537 LETQMEEMKTQLEELE---DELQATEDAKLRLEVNMQALKGQFE---------RDLQARDEQNEEKRRQLQRQLHEYETE 1604
Cdd:pfam05557 226 LKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSWVKLAQdtglnlrspEDLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1605 LEDERKQRALAAAAKKKLEGDLKDLElqadsaiKGREEAIKQLRKLQAQMKDFQRELEDARA---SRDEIFATAKENEKK 1681
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLN-------KKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1682 AKSLE--ADLMQLQEDLAAAERARKQADLEKEELAEELASSLsgrnalqdekrrleariaqleeeleeeqgnmEAMSDRV 1759
Cdd:pfam05557 379 LERIEeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL-------------------------------ERELQAL 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1760 RKATQQAEQLS--NELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTiaaleaKIAQLEEQVEQEAREK 1837
Cdd:pfam05557 428 RQQESLADPSYskEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKT------KVLHLSMNPAAEAYQQ 501
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1838 QAA-TKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNAR-VKQLKRQLEEAEEESQRI 1896
Cdd:pfam05557 502 RKNqLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKeVLDLRKELESAELKNQRL 562
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1039-1406 |
4.06e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1039 LEVRLKKEEKSRQEL----EKLKRKLEGDASD-------FHEQIADLQAQIAELKMQLAKKEEEL------QAALARLDD 1101
Cdd:pfam07888 32 LQNRLEECLQERAELlqaqEAANRQREKEKERykrdreqWERQRRELESRVAELKEELRQSREKHeeleekYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1102 EIAQKNNAL--------KKIRELEGHISDLQE-------DLDSERAARNKAEKQKRDLGEELEALKTELEDTldstatqq 1166
Cdd:pfam07888 112 ELSEEKDALlaqraaheARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKEEEAERKQLQAKLQQT-------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1167 elrakreqevtvlkkalDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTlEKENADLAGELRVLgqa 1246
Cdd:pfam07888 184 -----------------EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK-EAENEALLEELRSL--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1247 KQEVEHKKKKLEAQVQELQSKCSDGERARAELndkvHKLQNEVESVTGMLNEAegkAIKLAKDVASLSSQLQDTQELLQE 1326
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMAAQRDRTQAEL----HQARLQAAQLTLQLADA---SLALREGRARWAQERETLQQSAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1327 ETRQKLNVSTKLRQLEEernSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQ 1406
Cdd:pfam07888 316 DKDRIEKLSAELQRLEE---RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1016-1612 |
4.48e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.75 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1016 AEEEEKAKNLTKLKNKHESMISELEVRLK----KEEKSRQELEKLKRK-----LEGDASDFHEQIADLQAQIAELKMQLA 1086
Cdd:pfam10174 123 SEHERQAKELFLLRKTLEEMELRIETQKQtlgaRDESIKKLLEMLQSKglpkkSGEEDWERTRRIAEAEMQLGHLEVLLD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1087 KKEEELQAalarLDDEIAQKNNALKKIREleghISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtLDSTATQQ 1166
Cdd:pfam10174 203 QKEKENIH----LREELHRRNQLQPDPAK----TKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGL--LHTEDREE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1167 ELRAKreqevtvlkkaldEETRSHEaqvQEMRQKHAQAVEELTEQLEQFKRAKANLDknkqTLEKENADlagelrvlgqA 1246
Cdd:pfam10174 273 EIKQM-------------EVYKSHS---KFMKNKIDQLKQELSKKESELLALQTKLE----TLTNQNSD----------C 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1247 KQEVEHKKKKLEAQVQelqskcsdgeRArAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQE 1326
Cdd:pfam10174 323 KQHIEVLKESLTAKEQ----------RA-AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1327 ETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKR----FQKEIE 1402
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRERedreRLEELE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1403 NLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQ-----------RQLVSNLEKKQRKFDQLLAEEKNISSKYADER 1471
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklKSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1472 DRAEAEAREKETKAlSLARALEEALEAKEELERTNKMLKaEMEDLVSSKDdvgKNVHELE------------KSKRALET 1539
Cdd:pfam10174 552 TNPEINDRIRLLEQ-EVARYKEESGKAQAEVERLLGILR-EVENEKNDKD---KKIAELEsltlrqmkeqnkKVANIKHG 626
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1540 QMEEMKTQLEELEDELQATEDAKLR-LEVNMQALKGQFERDLQARDEqNEEKRRQLQRQLHEYETELEDERKQR 1612
Cdd:pfam10174 627 QQEMKKKGAQLLEEARRREDNLADNsQQLQLEELMGALEKTRQELDA-TKARLSSTQQSLAEKDGHLTNLRAER 699
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
867-1363 |
4.63e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 867 RQQKAENELKELEQKHSQLTEEKNLLQEQLQA----ETELYAEAEEMRVRLAAKKQELEEIlhemeARLEEEEDRGQQLQ 942
Cdd:PRK10246 420 EQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNvtqeQTQRNAALNEMRQRYKEKTQQLADV-----KTICEQEARIKDLE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 943 AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEIlvmddqnNKLSKERKLLEERISDLTTNLAEEEEKA 1022
Cdd:PRK10246 495 AQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEV-------KKLGEEGAALRGQLDALTKQLQRDESEA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1023 KNLTK----LKNKHESMISELEVR----------LKKEEKSRQELEKLKRKLEGDAsdfheQIADLQAQIAELKMQLAKK 1088
Cdd:PRK10246 568 QSLRQeeqaLTQQWQAVCASLNITlqpqddiqpwLDAQEEHERQLRLLSQRHELQG-----QIAAHNQQIIQYQQQIEQR 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1089 EEELQAALARLDDEIAQKNNalkkireleghisdlQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQEL 1168
Cdd:PRK10246 643 QQQLLTALAGYALTLPQEDE---------------EASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1169 RAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANldknkqtleKENADLAGELRVL--GQA 1246
Cdd:PRK10246 708 PHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQA---------SVFDDQQAFLAALldEET 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1247 KQEVEHKKKKLEAQVQELQSKCSDGERARAElndkvHKLQNEvesvtgmlneaegKAIKLAKDVASLSSQLQDTQELLQE 1326
Cdd:PRK10246 779 LTQLEQLKQNLENQRQQAQTLVTQTAQALAQ-----HQQHRP-------------DGLDLTVTVEQIQQELAQLAQQLRE 840
|
490 500 510
....*....|....*....|....*....|....*..
gi 13124875 1327 ETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLE 1363
Cdd:PRK10246 841 NTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1373-1905 |
4.74e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1373 LSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRK 1452
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1453 FDQLLAEEKNISSKYADERDRA------EAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKN 1526
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNnyykelEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1527 VHELEKSKraleTQMEEMKTQLEELE---DELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQlheyET 1603
Cdd:PRK01156 331 LSVLQKDY----NDYIKKKSRYDDLNnqiLELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ----EI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1604 ELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKdfqRELEDARASRDEIFATAKENEKKAK 1683
Cdd:PRK01156 403 DPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSV---CPVCGTTLGEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1684 SLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKA- 1762
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLk 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1763 ----TQQAEQLSNELATERST-AQKNESARQQLERQNKELRSKLHEMEGA---VKSKFKSTIAALEAKIAQLEEQVeQEA 1834
Cdd:PRK01156 560 ledlDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY-NEI 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1835 REKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEA------------------EEESQRI 1896
Cdd:PRK01156 639 QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlestieilrtriNELSDRI 718
|
....*....
gi 13124875 1897 NANRRKLQR 1905
Cdd:PRK01156 719 NDINETLES 727
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
847-1298 |
4.84e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 847 VTRQEEEMQAKEDELQKTKE----RQQKAENELKELEQKHSQLTEEKNLLQEQlqaETELYAEAEEMRVRLAAKKQELEE 922
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDADDLEERAEELREE---AAELESELEEAREAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 923 IlhemearleeeedrgqqlqaerkkmaqqmldlEEQLEEEEAA--------------RQKLQLEKVTAEAKIKKLEDEIL 988
Cdd:PRK02224 389 L--------------------------------EEEIEELRERfgdapvdlgnaedfLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 989 VMDdqnNKLSKERKLLE------------------------ERISDLTTNLAEEEEKaknLTKLKNKHESM--ISELEVR 1042
Cdd:PRK02224 437 TAR---ERVEEAEALLEagkcpecgqpvegsphvetieedrERVEELEAELEDLEEE---VEEVEERLERAedLVEAEDR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1043 LKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDeiaqknnALKKIRELEGHISD 1122
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE-------AREEVAELNSKLAE 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1123 LQEDLDSERAARNKAEKQKrDLGEELEALKTELEDtldsTATQQELRAKREQEVTVLKKALDEETrsHEAQVQEMRQKHA 1202
Cdd:PRK02224 584 LKERIESLERIRTLLAAIA-DAEDEIERLREKREA----LAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKE 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1203 QAV---EELTEQLEQFKRAKANLDKNKQTLEKENAdlagELRVLGQAKQEVEHKKKKLEA---QVQELQSKCSDgerARA 1276
Cdd:PRK02224 657 RAEeylEQVEEKLDELREERDDLQAEIGAVENELE----ELEELRERREALENRVEALEAlydEAEELESMYGD---LRA 729
|
490 500
....*....|....*....|..
gi 13124875 1277 ELNdkvhklQNEVESVTGMLNE 1298
Cdd:PRK02224 730 ELR------QRNVETLERMLNE 745
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
939-1117 |
4.90e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 939 QQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEIlvmDDQNNKLSKERKLLEERISDL------- 1011
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGERARALyrsggsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1012 --------TTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKM 1083
Cdd:COG3883 103 syldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|....
gi 13124875 1084 QLAKKEEELQAALARLDDEIAQKNNALKKIRELE 1117
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1033-1249 |
5.89e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1033 ESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKK 1112
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1113 IRELEGHISDLQEDLDSE----------------RAARNKAEKQKRDLgEELEALKTELEDTLDSTATQQELRAKREQEV 1176
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1177 TVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQE 1249
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1096-1267 |
6.87e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1096 LARLDDEIAQKNnalKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTldstatqQELRAKREQE 1175
Cdd:COG1579 12 LQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-------EARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1176 VTVLKKALDEETRSHEAQVQEMRQKHAQavEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKK 1255
Cdd:COG1579 82 LGNVRNNKEYEALQKEIESLKRRISDLE--DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|..
gi 13124875 1256 KLEAQVQELQSK 1267
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1184-1414 |
7.51e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1184 DEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAgelrvlgQAKQEVEHKKKKLEAQVQE 1263
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-------KLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1264 LqskcsdGERARAelndkvhklQNEVESVTGMLNeaegkAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEE 1343
Cdd:COG3883 88 L------GERARA---------LYRSGGSVSYLD-----VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1344 ERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAA 1414
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
999-1459 |
7.82e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 999 KERKLLEERISDLTTNLAEEEEKAKNLT-------KLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQI 1071
Cdd:pfam05557 27 RARIELEKKASALKRQLDRESDRNQELQkrirlleKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1072 ADLQAQIAELKMQLAKKEEELQAALARLDD-------------EIAQKNNALK-----------KIRELEGHI------S 1121
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEElqerldllkakasEAEQLRQNLEkqqsslaeaeqRIKELEFEIqsqeqdS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1122 DLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETR-SHEAQVQEMRQK 1200
Cdd:pfam05557 187 EIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEkEKLEQELQSWVK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1201 HAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELND 1280
Cdd:pfam05557 267 LAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1281 KVHKLQNEVESVTGMLnEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQ---LDEEME 1357
Cdd:pfam05557 347 RVLLLTKERDGYRAIL-ESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQaqtLERELQ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1358 AK--QNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ---------------------YEEKAAA 1414
Cdd:pfam05557 426 ALrqQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQgdydpkktkvlhlsmnpaaeaYQQRKNQ 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 13124875 1415 YDKLEKTKNRLQQELDDLVVDLDNQRQL-VSNLEKKQRKFDQLLAE 1459
Cdd:pfam05557 506 LEKLQAEIERLKRLLKKLEDDLEQVLRLpETTSTMNFKEVLDLRKE 551
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
849-1487 |
8.63e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.91 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 849 RQEEEMQAKEDELQKTKERQQKAENELKELeQKHSQLTEEKNLLQE-QLQAETELYAEAEEMRVRLAAKKQELEEILHEM 927
Cdd:pfam07111 43 GQGPGRRGRSLELEGSQALSQQAELISRQL-QELRRLEEEVRLLREtSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 928 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKlQLEKVTAEAKikKLEDEILVMDDQNNKLSKERKLLEER 1007
Cdd:pfam07111 122 AALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE-ALSSLTSKAE--GLEKSLNSLETKRAGEAKQLAEAQKE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1008 ISDLTTNLAEEEEKAKNLTKLKNKHESMISEL---EVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQ 1084
Cdd:pfam07111 199 AELLRKQLSKTQEELEAQVTLVESLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1085 LAKKEEELQAALARLDdeiAQKNNALKKIRELeghISDLQEDLDSERAARNKAEKQKRDLGEELEalkteledtlDSTAT 1164
Cdd:pfam07111 279 LALQEEELTRKIQPSD---SLEPEFPKKCRSL---LNRWREKVFALMVQLKAQDLEHRDSVKQLR----------GQVAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1165 QQELRAKREQEVTVLKKALDEETRshEAQVQEMRQKHAQAveelteqleQFKRAKANLDKNKQTLEKENADLAGELRVLG 1244
Cdd:pfam07111 343 LQEQVTSQSQEQAILQRALQDKAA--EVEVERMSAKGLQM---------ELSRAQEARRRQQQQTASAEEQLKFVVNAMS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1245 QAKQEVEHKKKKLEAQVQELQSkcsdgeraraeLNDKVHKLQNEVESVTGMlneaegkaikLAKDVAsLSSQLQDTQELL 1324
Cdd:pfam07111 412 STQIWLETTMTRVEQAVARIPS-----------LSNRLSYAVRKVHTIKGL----------MARKVA-LAQLRQESCPPP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1325 QEETRQKLNVSTKLRQLEEERNSLQDQLD--------------EEMEA-KQNLERHISTLNIQLSDSKKKLQDFASTVEA 1389
Cdd:pfam07111 470 PPAPPVDADLSLELEQLREERNRLDAELQlsahliqqevgrarEQGEAeRQQLSEVAQQLEQELQRAQESLASVGQQLEV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1390 LEEGKKRFQKEIENLTQQYEEKAAAY-----DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIS 1464
Cdd:pfam07111 550 ARQGQQESTEEAASLRQELTQQQEIYgqalqEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERN 629
|
650 660
....*....|....*....|...
gi 13124875 1465 SkyadERDRAEAEAREKETKALS 1487
Cdd:pfam07111 630 Q----ELRRLQDEARKEEGQRLA 648
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1450-1912 |
8.91e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1450 QRKFDQLLAEEKNISskyADERDRAEAEAREKETKALSLARALEEALEAKEELERTNkmLKAEMEDLVSSKDDVGKNVHE 1529
Cdd:TIGR00606 172 KQKFDEIFSATRYIK---ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQ--ITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1530 LEKSKRALEtQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYE------- 1602
Cdd:TIGR00606 247 LDPLKNRLK-EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKErelvdcq 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1603 TELEDERKQRALAAAAKKKLEGDLKDLELQAD---SAIKGREEAIKQLrKLQAQMKDFQRELEDARASRDEIFATAKENE 1679
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADrhqEHIRARDSLIQSL-ATRLELDGFERGPFSERQIKNFHTLVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1680 KKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEelasslsgrnALQDEKRRLEARIAQLEEELEEEQgNMEAMSDRV 1759
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR----------TIELKKEILEKKQEELKFVIKELQ-QLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1760 RKATQQAEQLSNELaterSTAQKNESARQQLERQnKELRSKlhemegavKSKFKSTIAALEAKIAQLE------EQVEQE 1833
Cdd:TIGR00606 474 LELDQELRKAEREL----SKAEKNSLTETLKKEV-KSLQNE--------KADLDRKLRKLDQEMEQLNhhtttrTQMEML 540
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1834 AREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATE 1912
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1450-1867 |
1.10e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1450 QRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHE 1529
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1530 LEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQnEEKRRQLQRQLHEYETELEDER 1609
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1610 KQRALaaaakkklegdLKDLELQADSAIKGREEAIKQLRKL--QAQMKDFQRE--LEDARASRDEIFATakenEKKAKSL 1685
Cdd:pfam07888 192 KEFQE-----------LRNSLAQRDTQVLQLQDTITTLTQKltTAHRKEAENEalLEELRSLQERLNAS----ERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1686 EADL--MQLQEDLAAAE--RARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRK 1761
Cdd:pfam07888 257 GEELssMAAQRDRTQAElhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1762 ATQQAEQLSNELATERSTaqkNESARQQLERQNKELRSKLHEMEGAvKSKFKSTIAALEAKIAQLEEQVEQEAREKQAAT 1841
Cdd:pfam07888 337 ERMEREKLEVELGREKDC---NRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAKWSEA 412
|
410 420
....*....|....*....|....*.
gi 13124875 1842 KSLkqKDKKLKEILLQVEDERKMAEQ 1867
Cdd:pfam07888 413 ALT--STERPDSPLSDSEDENPEALQ 436
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
852-1055 |
1.12e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 852 EEMQAKEDELQKT-KERQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAEAE-EMRVRLAAKKQELEEILHE--M 927
Cdd:PRK00409 519 NELIASLEELERElEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEkEAQQAIKEAKKEADEIIKElrQ 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 928 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLqleKVTAEAKIKKLED--EILVMDDQNN--------KL 997
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL---KVGDEVKYLSLGQkgEVLSIPDDKEaivqagimKM 672
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13124875 998 SKERKLLEerisdLTTNLAEEEEKAKNLTKLKNKHESMisELEVRLKKEEKSRQELEK 1055
Cdd:PRK00409 673 KVPLSDLE-----KIQKPKKKKKKKPKTVKPKPRTVSL--ELDLRGMRYEEALERLDK 723
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1251-1478 |
1.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1251 EHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQ 1330
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1331 KLNVSTKLRQLEE--ERNSLQDQLDEemeakqnlerhISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQY 1408
Cdd:COG3883 95 LYRSGGSVSYLDVllGSESFSDFLDR-----------LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1409 EEKAAAYDKLEKTKNRLQQELDDLvvdldnQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEA 1478
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQL------SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1299-1482 |
1.37e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1299 AEGKAIKLAKDVASLSSQLQDTQELLQeetrqklNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKK 1378
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELD-------ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1379 KLQDFA----------STVEALEEGK--KRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNL 1446
Cdd:COG3883 87 ELGERAralyrsggsvSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 13124875 1447 EKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKE 1482
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1025-1407 |
1.43e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1025 LTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIA 1104
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1105 QKNNALKKIRELEGHISDLQEDLDSeraarnkaekqkrdLGEELEALKTELEDtldstaTQQELRAKReQEVTVLKKALD 1184
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISC--------------LKNELSELRRQIQR------AELELQSTN-SELEELQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1185 EEtrsheaqvqemrQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEH--KKKKLEAQVQ 1262
Cdd:pfam05557 143 LL------------KAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1263 ELQSKCSDGERARAELNDKVHKLQNEVESVTGMlneaEGKAIKLAKDVASLSSQLQDTQELLQE---ETRQKLNVSTKLR 1339
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEVEDLKRKLEREEKY----REEAATLELEKEKLEQELQSWVKLAQDtglNLRSPEDLSRRIE 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13124875 1340 QLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1407
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKE 354
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1105-1331 |
1.47e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1105 QKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtldstATQQELrAKREQEVTVLKKALD 1184
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID------KLQAEI-AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1185 EETRSheAQVQEMRQKHAQAV---EELTEQLEQFKRAKANLDKNKQTLEKenadlagelrvLGQAKQEVEHKKKKLEAQV 1261
Cdd:COG3883 90 ERARA--LYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLEE-----------LKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1262 QELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQK 1331
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1069-1208 |
1.56e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.19 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1069 EQIADLQAQIAELKMQLA---KKEEELQAALARLDDEIAQKnnalkkirelEGHISDLQEDLDSERAARNKAEKQKRDLG 1145
Cdd:PRK09039 53 SALDRLNSQIAELADLLSlerQGNQDLQDSVANLRASLSAA----------EAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1146 EELEALKTELEDTLDSTAT-QQELRAKREQeVTVLKKALD-EETRSHEAQVQ------EMRQKHAQAVEEL 1208
Cdd:PRK09039 123 QELDSEKQVSARALAQVELlNQQIAALRRQ-LAALEAALDaSEKRDRESQAKiadlgrRLNVALAQRVQEL 192
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
849-1273 |
1.62e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 849 RQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQL-QAETELYAEAEEMRVRLAAKKQELEeilheM 927
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQLD-----K 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 928 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEdeilvmdDQNNKLSKERKLLEER 1007
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE-------TWYKRDLASLGVDPDV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1008 ISDLTTNLAEEEEKAKNLTklKNKHESmiseLEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAK 1087
Cdd:pfam12128 770 IAKLKREIRTLERKIERIA--VRRQEV----LRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1088 KEEELQAalarLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAA-------------RNKAEKQKRDLGEELEALKTE 1154
Cdd:pfam12128 844 LEMERKA----SEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQgsigerlaqledlKLKRDYLSESVKKYVEHFKNV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1155 LEDTLDSTATQQELRAkREQEVTVLKKALDEETRSHEAQV----------------QEMRQKHAQAVEELTEQLEQFKRA 1218
Cdd:pfam12128 920 IADHSGSGLAETWESL-REEDHYQNDKGIRLLDYRKLVPYleqwfdvrvpqsimvlREQVSILGVDLTEFYDVLADFDRR 998
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1219 KANLDKNKQTLEKENADLAG--ELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGER 1273
Cdd:pfam12128 999 IASFSRELQREVGEEAFFEGvsESAVRIRSKVSELEYWPELRVFVKAFRLWKSDGFG 1055
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1378-1791 |
1.72e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1378 KKLQDFASTVEALEEGKKRFQKE--IENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnQRQLVSNLEKKQRKFDq 1455
Cdd:pfam17380 221 KEVQGMPHTLAPYEKMERRKESFnlAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIV-----QHQKAVSERQQQEKFE- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1456 llaeeknissKYADERDRAEAEAREKEtkaLSLARALEEALEAKEELERTNKMLKAEMEDLVsskddvgknvheLEKSKR 1535
Cdd:pfam17380 295 ----------KMEQERLRQEKEEKARE---VERRRKLEEAEKARQAEMDRQAAIYAEQERMA------------MERERE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1536 ALETQMEEMKTQLEELEDELQATEDAKLRlevnmqalkgQFERdLQARDEQNEEKRRQlqrqlheyetELEDERKQRALA 1615
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEISRMR----------ELER-LQMERQQKNERVRQ----------ELEAARKVKILE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1616 AAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFaTAKENEKKAKSLEADLMQLQED 1695
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRDRK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1696 LAAAER---------ARKQADLEKEELAEELASSLSGR-NALQDEKRRleaRIAQLEEELEEEQGNMEAMSDRVRKATQQ 1765
Cdd:pfam17380 488 RAEEQRrkilekeleERKQAMIEEERKRKLLEKEMEERqKAIYEEERR---REAEEERRKQQEMEERRRIQEQMRKATEE 564
|
410 420
....*....|....*....|....*....
gi 13124875 1766 AEQLsNELATERSTAQK---NESARQQLE 1791
Cdd:pfam17380 565 RSRL-EAMEREREMMRQiveSEKARAEYE 592
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1025-1159 |
2.11e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1025 LTKLKNKHESMISELEVRLKK-EEKSRQELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAKKE---EELQAALARLD 1100
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEhEERELTEEEEEIRRLE-------EQVERLEAEVEELEAELEEKDeriERLERELSEAR 454
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1101 DEIAQKNNALKKIRELEGHISDLQEDLDSEraaRNKAEKQKRDLGEELEALKTELEDTL 1159
Cdd:COG2433 455 SEERREIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1109 |
2.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMRVRLAAKKQELEeilhemear 930
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---ALQAEIDKLQAEIAEAEAEIE--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 931 leeeedrgqQLQAERKKMAQQMldleeqleeeeaARQKLQLEKVTAEAKIKKLEDEIlvmdDQNNKLSKERKLLEERISD 1010
Cdd:COG3883 83 ---------ERREELGERARAL------------YRSGGSVSYLDVLLGSESFSDFL----DRLSALSKIADADADLLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEE 1090
Cdd:COG3883 138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
250
....*....|....*....
gi 13124875 1091 ELQAALARLDDEIAQKNNA 1109
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1372-1595 |
2.33e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1372 QLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQR 1451
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1452 K-------FDQLLAeekniSSKYADERDRAEAeareketkalsLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVG 1524
Cdd:COG3883 97 RsggsvsyLDVLLG-----SESFSDFLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1525 KNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQ 1595
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
844-1443 |
2.75e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 844 LLQVTRQEE---EMQAKEDELQKTKERQQKAENELKELE--QKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQ 918
Cdd:PRK10246 246 LNWLTRLDElqqEASRRQQALQQALAAEEKAQPQLAALSlaQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 919 ELEEILHEMEARLeeeedrgQQLQAERKKMAQQMldleeqleeeeaarqklqlekvTAEAKIKKLEDEILVMDDQNNKLS 998
Cdd:PRK10246 326 LRARIRHHAAKQS-------AELQAQQQSLNTWL----------------------AEHDRFRQWNNELAGWRAQFSQQT 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 999 KERklleERISDLTTNLAEEEEKAKNLTKLKnkheSMISELEVRLKKEEKSRQeleklkRKLEGDASDFHEQIADLQAQI 1078
Cdd:PRK10246 377 SDR----EQLRQWQQQLTHAEQKLNALPAIT----LTLTADEVAAALAQHAEQ------RPLRQRLVALHGQIVPQQKRL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1079 AELKMQLAKKEEELQAALARLDD------EIAQKNNALKKIRELEGHISDLQE--------------------------- 1125
Cdd:PRK10246 443 AQLQVAIQNVTQEQTQRNAALNEmrqrykEKTQQLADVKTICEQEARIKDLEAqraqlqagqpcplcgstshpaveayqa 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1126 -DLDSERAARNKAEKQKRDLGEELEALKTELEdtldsTATQQELRAKRE-QEVTVLKKALDEETRSHEAQVQEMRQKHaq 1203
Cdd:PRK10246 523 lEPGVNQSRLDALEKEVKKLGEEGAALRGQLD-----ALTKQLQRDESEaQSLRQEEQALTQQWQAVCASLNITLQPQ-- 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1204 avEELTEQLEQFKRAKANLDKNKQTLEKEnADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDK-- 1281
Cdd:PRK10246 596 --DDIQPWLDAQEEHERQLRLLSQRHELQ-GQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRqq 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1282 -----------VHKLQNEVESVTGMLN--EAEGKAIKLAKDVA------------SLSSQLQDTQELLQEET------RQ 1330
Cdd:PRK10246 673 eaqswqqrqneLTALQNRIQQLTPLLEtlPQSDDLPHSEETVAldnwrqvheqclSLHSQLQTLQQQDVLEAqrlqkaQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1331 KLNVSTKLRQLEEERNSLQDQLDEEMEA-----KQNLERHISTLNIQLSDSKKKLQ----------DFASTVEALeegkk 1395
Cdd:PRK10246 753 QFDTALQASVFDDQQAFLAALLDEETLTqleqlKQNLENQRQQAQTLVTQTAQALAqhqqhrpdglDLTVTVEQI----- 827
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1396 rfQKEIENLTQQYEEKAAAYDKL-----EKTKNRLQQEldDLVVDLDNQRQLV 1443
Cdd:PRK10246 828 --QQELAQLAQQLRENTTRQGEIrqqlkQDADNRQQQQ--ALMQQIAQATQQV 876
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1528-1930 |
3.09e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1528 HELEKSKRAL---ETQMEEMKTQLEE-------LEDELQATEDaKLRLEVNMQALKGQFER------DLQARDEQNEEKR 1591
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD-HLNLVQTALRQQEKIERyqedleELTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1592 RQLQRQLHEYETELEderkqralaaaakkKLEGDLKDLELQ-ADsaikgREEAI--KQLRKLQAQMKdfQRELEDARA-- 1666
Cdd:COG3096 371 EEAAEQLAEAEARLE--------------AAEEEVDSLKSQlAD-----YQQALdvQQTRAIQYQQA--VQALEKARAlc 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1667 -----SRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLekeelaeelasslsgrnALQdekrrLEARIAQL 1741
Cdd:COG3096 430 glpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEK-----------------AYE-----LVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1742 EEELEEEQGNMEAMSD--RVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEgavksKFKSTIAAL 1819
Cdd:COG3096 488 VERSQAWQTARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----ELEELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1820 EAKIAQLEEQVEqEAREKQAATKS----LKQKDKKLKE-----ILLQVEDERkMAEQYKEQAEKGNARVKQLKRQLE--- 1887
Cdd:COG3096 563 EAQLEELEEQAA-EAVEQRSELRQqleqLRARIKELAArapawLAAQDALER-LREQSGEALADSQEVTAAMQQLLErer 640
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 13124875 1888 EAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRG 1930
Cdd:COG3096 641 EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1387-1929 |
3.59e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1387 VEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVS-------NLEKKQRKFDQLLAE 1459
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeqakkALEYYQLKEKLELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1460 EKNISSKY----ADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKR 1535
Cdd:pfam02463 224 EYLLYLDYlklnEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1536 ALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALA 1615
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1616 AAAKKKLEGDLKDLELQ------ADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADL 1689
Cdd:pfam02463 384 ERLSSAAKLKEEELELKseeekeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1690 MQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQL 1769
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1770 SNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAK-------IAQLEEQVEQEAREKQAATK 1842
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVleidpilNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1843 SLKQKDKKLKEILLQVEDERKMAEQYK-EQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREV 1921
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKgVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
....*...
gi 13124875 1922 NALKSKLR 1929
Cdd:pfam02463 704 KEQREKEE 711
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1071-1222 |
3.65e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 48.19 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1071 IADLQAQIAELKMQLAKkeeeLQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEA 1150
Cdd:pfam00529 53 PTDYQAALDSAEAQLAK----AQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1151 LKTELEDTL---DSTATQQELRAKREQEVTVLKKALD----EETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANL 1222
Cdd:pfam00529 129 RRVLAPIGGisrESLVTAGALVAQAQANLLATVAQLDqiyvQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDL 207
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
844-1168 |
4.08e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 844 LLQVTRQE--EEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELE 921
Cdd:pfam07888 35 RLEECLQEraELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 922 EILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKER 1001
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1002 KLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHE------------ 1069
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1070 -----QIADLQAQIAELKMQL-------AKKEEELQAA-------LARLDDEIAQKNNALKKIR-ELEGHISDLQEDLDS 1129
Cdd:pfam07888 275 hqarlQAAQLTLQLADASLALregrarwAQERETLQQSaeadkdrIEKLSAELQRLEERLQEERmEREKLEVELGREKDC 354
|
330 340 350
....*....|....*....|....*....|....*....
gi 13124875 1130 ERAARNKAEKQKRDLGEELEALKTELEDTLdstATQQEL 1168
Cdd:pfam07888 355 NRVQLSESRRELQELKASLRVAQKEKEQLQ---AEKQEL 390
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1595-1929 |
4.34e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1595 QRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFAT 1674
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1675 AKENEKKAkslEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEA 1754
Cdd:pfam07888 120 LLAQRAAH---EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1755 MSDRVRKATQQAEQLSNELAT---ERSTAQKNESARQQLERQNKELRSKLHEMEGAV---KSKFKSTIAALEAKIAQLEE 1828
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTltqKLTTAHRKEAENEALLEELRSLQERLNASERKVeglGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1829 QVEQEARekqaATKSLKQKDKKLKEILLQVEDERKMAEQykeQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELD 1908
Cdd:pfam07888 277 ARLQAAQ----LTLQLADASLALREGRARWAQERETLQQ---SAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
330 340
....*....|....*....|....*
gi 13124875 1909 EATESNEAM----GREVNALKSKLR 1929
Cdd:pfam07888 350 REKDCNRVQlsesRRELQELKASLR 374
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
858-1061 |
4.68e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 858 EDELQKTKERQQKAENELKELEQKHS--QLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEE 935
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 936 D-------RGQQLQAERkKMAQQMLDLEEQLEEEEAARQKLQlekvTAEAKIKKLEDEILVmddqnnKLSKERKLLEERI 1008
Cdd:COG3206 261 QspviqqlRAQLAELEA-ELAELSARYTPNHPDVIALRAQIA----ALRAQLQQEAQRILA------SLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1009 SDLTTNLAEEEEKAKNLTKLKNKHESMISELEVrlkkeekSRQELEKLKRKLE 1061
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEV-------ARELYESLLQRLE 375
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
985-1357 |
4.99e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 48.31 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 985 DEILVMDDQnnKLSKERKLLEERISDLTTNLAEEEEKAKNLtKLKNKHESMISELEVRLKK----------------EEK 1048
Cdd:PLN03229 383 DELGKMDTE--ELLKHRMLKFRKIGGFQEGVPVDPERKVNM-KKREAVKTPVRELEGEVEKlkeqilkakessskpsELA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1049 SRQELEKLKRKLEGDASDFHEQIAdLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLD 1128
Cdd:PLN03229 460 LNEMIEKLKKEIDLEYTEAVIAMG-LQERLENLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1129 SERAA-RNKAEKQKRDLGEELealKTELEDTLDSTATQQELRAKREqevtvlkkALDEETRSHEAQvqemrqKHAQAVEE 1207
Cdd:PLN03229 539 MLNEFsRAKALSEKKSKAEKL---KAEINKKFKEVMDRPEIKEKME--------ALKAEVASSGAS------SGDELDDD 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1208 LTEQLEqfkrakanldKNKQTLEKEnadLAGELRVLGQAKQEVEHKKKKLEAQ--VQELQSKCsdgERARAELNDKVHKL 1285
Cdd:PLN03229 602 LKEKVE----------KMKKEIELE---LAGVLKSMGLEVIGVTKKNKDTAEQtpPPNLQEKI---ESLNEEINKKIERV 665
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1286 QNevesVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEME 1357
Cdd:PLN03229 666 IR----SSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARE 733
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
873-1472 |
5.35e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 873 NELKELEQKHSQLTEEKNLLQEQLQAETELYAEAeemrvrlaakKQELEEILHEMEARleeeedrgqqlqAERKKMAQQM 952
Cdd:TIGR01612 1486 NELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY----------KKDVTELLNKYSAL------------AIKNKFAKTK 1543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 953 LDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQ---NNKLSK------------ERKLLeeRISDLTTN--- 1014
Cdd:TIGR01612 1544 KDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakNDKSNKaaidiqlslenfENKFL--KISDIKKKind 1621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1015 -LAEEEEKAKNLTKLK-NKHESMISELEVRLKKEEKSRQELEKLKRKLEgdasDFHEQIADLQAQIAELKMQLAKKEEEL 1092
Cdd:TIGR01612 1622 cLKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIE----DKKKELDELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1093 QAALARLDDEIAQKN-NALKKIRELeghisdLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELrak 1171
Cdd:TIGR01612 1698 EIGIIEKIKEIAIANkEEIESIKEL------IEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNI--- 1768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1172 reqeVTVLKKALDEETRSHEaqvqEMRQKHAQAVEELTEQLEQFKRAKANLDKnkqtLEKENADlagelRVLGQAKQEVE 1251
Cdd:TIGR01612 1769 ----IAGCLETVSKEPITYD----EIKNTRINAQNEFLKIIEIEKKSKSYLDD----IEAKEFD-----RIINHFKKKLD 1831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1252 HKKKKLEAQVQELQ------SKCSDGERARAELNDKVHKLQNEVESVTGMLN--------EAEGKAIKLAKDVASLSSQL 1317
Cdd:TIGR01612 1832 HVNDKFTKEYSKINegfddiSKSIENVKNSTDENLLFDILNKTKDAYAGIIGkkyysykdEAEKIFINISKLANSINIQI 1911
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1318 QDTQEL-------------LQEETRQKLNVSTKLRQLEEE----RNSLQDQLDEEMEAKQNLERHISTLNI-----QLSD 1375
Cdd:TIGR01612 1912 QNNSGIdlfdniniailssLDSEKEDTLKFIPSPEKEPEIytkiRDSYDTLLDIFKKSQDLHKKEQDTLNIifenqQLYE 1991
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1376 SKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEE---------------KAAAYDKLEKTKNRLQQELDDLVVDLDNQ- 1439
Cdd:TIGR01612 1992 KIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKFGIDFDVKa 2071
|
650 660 670
....*....|....*....|....*....|....
gi 13124875 1440 -RQLVSNLEKKQRKFDQLLAEEKNISSKYADERD 1472
Cdd:TIGR01612 2072 mEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1141-1316 |
6.77e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1141 KRDLGEELEALKTELEDTLDstATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKA 1220
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1221 NLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKleaQVQELQSKCS-DGERARAELNDKV-HKLQNEVES-VTGMLN 1297
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERISGlTAEEAKEILLEKVeEEARHEAAVlIKEIEE 180
|
170
....*....|....*....
gi 13124875 1298 EAEGKAIKLAKDVASLSSQ 1316
Cdd:PRK12704 181 EAKEEADKKAKEILAQAIQ 199
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
851-1678 |
7.00e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDELQKTKE--RQQKA----ENELKELEQK---HSQLTEEKNLLQEQLQAETELY-AEAEEMRVRLAAKKQEL 920
Cdd:COG3096 326 EQDYQAASDHLNLVQTalRQQEKieryQEDLEELTERleeQEEVVEEAAEQLAEAEARLEAAeEEVDSLKSQLADYQQAL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 921 --------------------EEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQklQLEKvtAEAKI 980
Cdd:COG3096 406 dvqqtraiqyqqavqalekaRALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARR--QFEK--AYELV 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 981 KKLEDEIlvmdDQNNKLSKERKLLEE---------RISDLTTNLAEEEEKAKNltklKNKHESMISELEVRLKKEEKSRQ 1051
Cdd:COG3096 482 CKIAGEV----ERSQAWQTARELLRRyrsqqalaqRLQQLRAQLAELEQRLRQ----QQNAERLLEEFCQRIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1052 ELEKLKRKLEGDASDFHEQIADLQAQIAELKMQL----AKKEE---------ELQAALARLDDEIAQknnALKKIRELEG 1118
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLeqlrARIKElaarapawlAAQDALERLREQSGE---ALADSQEVTA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1119 HisdLQEDLDSERAA---RNKAEKQKRDLGEELEALkteledTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQ 1195
Cdd:COG3096 631 A---MQQLLEREREAtveRDELAARKQALESQIERL------SQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYF 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1196 EMR---QKHAQAVEELT---EQLEQFKRAKANL-----------DKNKQTLEKENADLAG----ELRV--------LGQA 1246
Cdd:COG3096 702 SALygpARHAIVVPDLSavkEQLAGLEDCPEDLyliegdpdsfdDSVFDAEELEDAVVVKlsdrQWRYsrfpevplFGRA 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1247 KQevEHKKKKLEAQVQELqskcsdgERARAELNDKVHKLQNEVESVTGMLneAEGKAIKLAKDVAslssqlqdtqELLQE 1326
Cdd:COG3096 782 AR--EKRLEELRAERDEL-------AEQYAKASFDVQKLQRLHQAFSQFV--GGHLAVAFAPDPE----------AELAA 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1327 ETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDS-KKKLQDFASTVEALEEGK---KRFQKEIE 1402
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETlADRLEELREELDAAQEAQafiQQHGKALA 920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1403 NLT----------QQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnqrQLVSNLEKkqrkfdqlLAeeknisskYADerd 1472
Cdd:COG3096 921 QLEplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALS-------EVVQRRPH--------FS--------YED--- 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1473 raeAEAREKETKALslaraleealeakeelertNKMLKAemedlvsskddvgknvhELEKSKRALETQMEEMKTQLEELE 1552
Cdd:COG3096 975 ---AVGLLGENSDL-------------------NEKLRA-----------------RLEQAEEARREAREQLRQAQAQYS 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1553 DELQATEDAKLRLEVNMQALKgQFERDLQA----RDEQNEEKRRQLQRQLHEyetELEDERKQRALAAAAKKKLEGDLKD 1628
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQ-ELEQELEElgvqADAEAEERARIRRDELHE---ELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 13124875 1629 LElqadsaikgreeaiKQLRKLQAQMKDFQRELEDARASRDEIFATAKEN 1678
Cdd:COG3096 1092 LQ--------------KRLRKAERDYKQEREQVVQAKAGWCAVLRLARDN 1127
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
852-1080 |
7.15e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 852 EEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARL 931
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 932 EEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDqnnklsKERKLLEERISDL 1011
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLEL 671
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13124875 1012 TTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEgDASDFHEQIADLQAQIAE 1080
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALLKE 739
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
977-1553 |
7.43e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 977 EAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLtTNLAEEEEKAKNLTKLKNKHESMISELEV--------RLKKEEK 1048
Cdd:TIGR01612 578 EKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNI-SDKNEYIKKAIDLKKIIENNNAYIDELAKispyqvpeHLKNKDK 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1049 SRQELE-KLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEI----------------AQKNNALK 1111
Cdd:TIGR01612 657 IYSTIKsELSKIYEDDIDALYNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIqnmetatvelhlsnieNKKNELLD 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1112 KIRELEGHI-SDLQEDLDSERAARNKAEKQkrdLGEELEALKTELEDTLDSTATQQELRAKREQEVTVlKKALDEETRSH 1190
Cdd:TIGR01612 737 IIVEIKKHIhGEINKDLNKILEDFKNKEKE---LSNKINDYAKEKDELNKYKSKISEIKNHYNDQINI-DNIKDEDAKQN 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1191 EAQVQEMRQKHAQAVEELTEQLEQFKR------AKANLDKNKQTLEKENADLAGE--LRVLGQAKQEVEhkkkklEAQVQ 1262
Cdd:TIGR01612 813 YDKSKEYIKTISIKEDEIFKIINEMKFmkddflNKVDKFINFENNCKEKIDSEHEqfAELTNKIKAEIS------DDKLN 886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1263 ELQSKCSDGERARAELNDKVHKLQNEVESvtgmLNEAEGkAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLE 1342
Cdd:TIGR01612 887 DYEKKFNDSKSLINEINKSIEEEYQNINT----LKKVDE-YIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIE 961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1343 EernSLQDQLDEEMEAKQN-LERHISTLNIQLSDSKKKlqdfaSTVEALEEGKKRFQKEIEN-LTQQYEEKaaaydklEK 1420
Cdd:TIGR01612 962 K---SYKDKFDNTLIDKINeLDKAFKDASLNDYEAKNN-----ELIKYFNDLKANLGKNKENmLYHQFDEK-------EK 1026
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1421 TKNRLQQELDDLVVDLDNQRQLV-SNLEKKQRKFDQLLAeeKNISSKYADERDRAEAEAREKETKALSLARALEEALEAK 1499
Cdd:TIGR01612 1027 ATNDIEQKIEDANKNIPNIEIAIhTSIYNIIDEIEKEIG--KNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGKE 1104
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1500 EELERTNKMLKAEmEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED 1553
Cdd:TIGR01612 1105 ENIKYADEINKIK-DDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED 1157
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1196 |
8.40e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 967 QKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKlknkhesmisELEVRLKKE 1046
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE----------ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1047 EKSRQELEKLKRKLE-GDASDFHEQIADLQaQIAELKMQLAKKEEELQAALARLDDEI-AQKNNALKKIRELEGHISDLQ 1124
Cdd:COG3883 96 YRSGGSVSYLDVLLGsESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1125 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQE 1196
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
850-1410 |
8.57e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 850 QEEEMQAKEDELQKTKERQQKAENELKELEQKHS-QLTEEKNL--LQEQLQAETE-LYAEAEEMRVRLAAKKQELEEI-- 923
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGqQLDAAEELeeLLAELEAQLEeLEEQAAEAVEQRSELRQQLEQLra 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 924 ----LHEMEARLEEEEDRGQQLQ-------AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKL------ED- 985
Cdd:COG3096 593 rikeLAARAPAWLAAQDALERLReqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLsqpggaEDp 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 986 ---------------EI----------------------LVMDDqnnkLSKERKLLEERiSDLTTNL------------- 1015
Cdd:COG3096 673 rllalaerlggvllsEIyddvtledapyfsalygparhaIVVPD----LSAVKEQLAGL-EDCPEDLyliegdpdsfdds 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1016 ---AEEEEKA---------------------------KNLTKLKNKHEsmisELEVRLKKEEKSRQELEklkrKLEGDAS 1065
Cdd:COG3096 748 vfdAEELEDAvvvklsdrqwrysrfpevplfgraareKRLEELRAERD----ELAEQYAKASFDVQKLQ----RLHQAFS 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1066 DF---HEQIA---DLQAQIAELKMQLAkkeeELQAALARLDDEIAQKNNALKKIRE---------------LEGHISDLQ 1124
Cdd:COG3096 820 QFvggHLAVAfapDPEAELAALRQRRS----ELERELAQHRAQEQQLRQQLDQLKEqlqllnkllpqanllADETLADRL 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1125 EDLDSERAARNKAEKQKRDLGEELEALKTELeDTLDSTATQQElrakreqevtvlkkALDEETRSHEAQVQEMRQKhAQA 1204
Cdd:COG3096 896 EELREELDAAQEAQAFIQQHGKALAQLEPLV-AVLQSDPEQFE--------------QLQADYLQAKEQQRRLKQQ-IFA 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1205 VEELTEQLEQFKRAKAnldknkQTLEKENADLagelrvlgqakqevehkkkkleaqVQELQSKCSDGERARAELNDKVHK 1284
Cdd:COG3096 960 LSEVVQRRPHFSYEDA------VGLLGENSDL------------------------NEKLRARLEQAEEARREAREQLRQ 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1285 LQNEVESVTGMLneaegkaiklakdvASLSSQLQDTQELLQEetrqklnvstklrqLEEERNSLQDQLDEEMEAKQNLER 1364
Cdd:COG3096 1010 AQAQYSQYNQVL--------------ASLKSSRDAKQQTLQE--------------LEQELEELGVQADAEAEERARIRR 1061
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 13124875 1365 hiSTLNIQLSDSKKKLqdfastvEALEEGKKRFQKEIENLTQQYEE 1410
Cdd:COG3096 1062 --DELHEELSQNRSRR-------SQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
9.08e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 45.03 E-value: 9.08e-05
10 20
....*....|....*....|....*
gi 13124875 657 YKEQLGKLMTTLRNTTPNFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1025-1449 |
9.74e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1025 LTKLKNKHESMISELEVRLKKEEKSRQELEKLKrklegdasdfhEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIA 1104
Cdd:pfam06160 95 LDDIEEDIKQILEELDELLESEEKNREEVEELK-----------DKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1105 QKNN---------ALKKIRELEGHISDLQEDLDseraarnkaekqkrDLGEELEALKTELEDTLDS-TATQQELrakREQ 1174
Cdd:pfam06160 164 QFEEltesgdyleAREVLEKLEEETDALEELME--------------DIPPLYEELKTELPDQLEElKEGYREM---EEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1175 EVTVLKKALDEETRSHEAQVQEmrqkhaqaVEELTEQLEqFKRAKANLDKNKQTLEKENADLAGELrvlgQAKQEVEHKK 1254
Cdd:pfam06160 227 GYALEHLNVDKEIQQLEEQLEE--------NLALLENLE-LDEAEEALEEIEERIDQLYDLLEKEV----DAKKYVEKNL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1255 KKLEAQVQELQskcsdgeraraelnDKVHKLQNEVESVT---GMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEET--- 1328
Cdd:pfam06160 294 PEIEDYLEHAE--------------EQNKELKEELERVQqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEvay 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1329 ---RQKLNVSTK-LRQLEEERNSLQDQL----DEEMEAKQNLERhistLNIQLSDSKKKLQdfastvealeegkkrfQKE 1400
Cdd:pfam06160 360 selQEELEEILEqLEEIEEEQEEFKESLqslrKDELEAREKLDE----FKLELREIKRLVE----------------KSN 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1401 IENLTQQYEE-KAAAYDKLEKTKNRLQQ---ELDDLVVDLDNQRQLVSNLEKK 1449
Cdd:pfam06160 420 LPGLPESYLDyFFDVSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEK 472
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1146-1418 |
9.89e-05 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 47.00 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1146 EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKN 1225
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1226 KQTLEKENADLA-----GELRVLGQ--AKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNE 1298
Cdd:pfam04108 83 LDKLRNTPVEPAlppgeEKQKTLLDfiDEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSSPSES 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1299 AE------GKAIKLAKDVASLSSQL------------------QDTQELLQEETRQKLNVSTKLR----QLEEERNSLQD 1350
Cdd:pfam04108 163 ISliptllKELESLEEEMASLLESLtnhydqcvtavklteggrAEMLEVLENDARELDDVVPELQdrldEMENNYERLQK 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1351 QLDEEMEAKQNLE---RHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKL 1418
Cdd:pfam04108 243 LLEQKNSLIDELLsalQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPSAYGSL 313
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
858-1105 |
1.04e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 858 EDELQKTKE---RQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAeaeemrvrLAAKKQELEEilhemearleee 934
Cdd:COG0497 154 EELLEEYREayrAWRALKKELEELRADEAERARELDLLRFQLE---ELEA--------AALQPGEEEE------------ 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 935 edrgqqLQAERKKMAQqmldLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEE---RISDL 1011
Cdd:COG0497 211 ------LEEERRRLSN----AEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESaliELEEA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1012 TTN--------------LAEEEEKAKNLTKLKNKHESMISELevrLKKEEKSRQELEKLkrklegdaSDFHEQIADLQAQ 1077
Cdd:COG0497 281 ASElrryldslefdperLEEVEERLALLRRLARKYGVTVEEL---LAYAEELRAELAEL--------ENSDERLEELEAE 349
|
250 260 270
....*....|....*....|....*....|..
gi 13124875 1078 IAELKMQLAKKEEEL----QAALARLDDEIAQ 1105
Cdd:COG0497 350 LAEAEAELLEAAEKLsaarKKAAKKLEKAVTA 381
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
906-1264 |
1.08e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 906 AEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLED 985
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 986 EILVMDDQNNKLSKERKLLEERISDLttnlaeeEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDAS 1065
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIREL-------EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1066 DFHEQIADLQAQIAELKMQLAKKEEELQaalaRLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLG 1145
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVL----QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1146 EELEALKTELEDTL------------------DSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEE 1207
Cdd:pfam07888 258 EELSSMAAQRDRTQaelhqarlqaaqltlqlaDASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1208 LTEQleqfKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQEL 1264
Cdd:pfam07888 338 RMER----EKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1234-1612 |
1.11e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.60 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1234 ADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGkaiklakDVASL 1313
Cdd:pfam19220 16 ADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1314 SSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQ----DFASTVEA 1389
Cdd:pfam19220 89 VARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQraegELATARER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1390 ---LEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldnQRQLVSNLEKKQRKFDQLLAEEKNISSK 1466
Cdd:pfam19220 169 lalLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRAL------EGQLAAEQAERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1467 YADERDRAEA-EAREKET-KALSLARALEEAleakeeleRTNKMLKAE--MEDLVSSKDDVGKNVHELEKSKRALETQME 1542
Cdd:pfam19220 243 RASLRMKLEAlTARAAATeQLLAEARNQLRD--------RDEAIRAAErrLKEASIERDTLERRLAGLEADLERRTQQFQ 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1543 EMKTQLEELEDE-------LQATEDAKLRLEVNMQALKGQFErDLQARDEQneeKRRQLQRQLHEYETELEDERKQR 1612
Cdd:pfam19220 315 EMQRARAELEERaemltkaLAAKDAALERAEERIASLSDRIA-ELTKRFEV---ERAALEQANRRLKEELQRERAER 387
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1020-1141 |
1.16e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1020 EKAK-NLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLakkEEELQAALAR 1098
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 13124875 1099 LDDEIAQknnALKKIRELE--GHISDLQEDLDSERAARNKAEKQK 1141
Cdd:PRK00409 582 AKKEADE---IIKELRQLQkgGYASVKAHELIEARKRLNKANEKK 623
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
858-1562 |
1.17e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 858 EDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEemrvRLAAKKQELEEIlhEMEARLEEEEDR 937
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVE----RSQAWQTARELL--RRYRSQQALAQR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 938 GQQLQAE----RKKMAQQmldleeqleeEEAARQKLQLEKVTAeakiKKLEDEILVMDDQNNklskerklLEERISDLTT 1013
Cdd:COG3096 514 LQQLRAQlaelEQRLRQQ----------QNAERLLEEFCQRIG----QQLDAAEELEELLAE--------LEAQLEELEE 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1014 NLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLkRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQ 1093
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL-REQSGEALADSQEVTAAMQQLLEREREATVERDELA 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1094 AALARLDDEIAQKNNA-------LKKIRELEGH--ISDLQEDLDSERA----ARNKAEKQK---RDLGEELEALKTeLED 1157
Cdd:COG3096 651 ARKQALESQIERLSQPggaedprLLALAERLGGvlLSEIYDDVTLEDApyfsALYGPARHAivvPDLSAVKEQLAG-LED 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1158 TL--------------DSTATQQEL-------------------------RAKREQEVTVLKKALDEETRSHeAQVQEMR 1198
Cdd:COG3096 730 CPedlyliegdpdsfdDSVFDAEELedavvvklsdrqwrysrfpevplfgRAAREKRLEELRAERDELAEQY-AKASFDV 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1199 QKHaqavEELTEQLEQFKRAKANLdknkqtleKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAEL 1278
Cdd:COG3096 809 QKL----QRLHQAFSQFVGGHLAV--------AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLL 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1279 NDKVHK--------LQNEVESVTGMLNEAEGKAIKLAKDVASLsSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQD 1350
Cdd:COG3096 877 NKLLPQanlladetLADRLEELREELDAAQEAQAFIQQHGKAL-AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQ 955
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1351 QLDEEMEAKQNLErHIStlniqLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYdklektkNRLQQELD 1430
Cdd:COG3096 956 QIFALSEVVQRRP-HFS-----YEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQY-------SQYNQVLA 1022
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1431 DLVVDLDNQRQLVSNLEkkqRKFDQL-LAEEKNISSKYADERDRAEAEAREKETKALSL----ARALEEALEAKEELERT 1505
Cdd:COG3096 1023 SLKSSRDAKQQTLQELE---QELEELgVQADAEAEERARIRRDELHEELSQNRSRRSQLekqlTRCEAEMDSLQKRLRKA 1099
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1506 NKMLKAEMEDLVSSK------------DDVGKNVHELE--------------KSKRALETQMEEmktqLEELEDELQATE 1559
Cdd:COG3096 1100 ERDYKQEREQVVQAKagwcavlrlardNDVERRLHRRElaylsadelrsmsdKALGALRLAVAD----NEHLRDALRLSE 1175
|
...
gi 13124875 1560 DAK 1562
Cdd:COG3096 1176 DPR 1178
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1046-1446 |
1.20e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1046 EEKSRQELEKLKrklegDASDFHeqiadlQAQIAElkmqlakkeeELQAALARLDDeiaqKNNALKKIRELEGHISDLqe 1125
Cdd:PRK10929 25 EKQITQELEQAK-----AAKTPA------QAEIVE----------ALQSALNWLEE----RKGSLERAKQYQQVIDNF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1126 dldseraarnkaEKQKRDLGEELEALKTELEdTLDSTATQQELrakrEQEVTVLKKALDEETRSHEaQVQEMRQKHAQAV 1205
Cdd:PRK10929 78 ------------PKLSAELRQQLNNERDEPR-SVPPNMSTDAL----EQEILQVSSQLLEKSRQAQ-QEQDRAREISDSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1206 EELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAkqEVEHKKKKLE----AQV-----QELQskcsdgeRARA 1276
Cdd:PRK10929 140 SQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQA--ESAALKALVDelelAQLsannrQELA-------RLRS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1277 ELNDKVH-KLQNEVESVTGMLN-----EAEgKAIK----LAKDVASL----SSQLQDTQELLQE--ETRQKLN-VSTKLR 1339
Cdd:PRK10929 211 ELAKKRSqQLDAYLQALRNQLNsqrqrEAE-RALEstelLAEQSGDLpksiVAQFKINRELSQAlnQQAQRMDlIASQQR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1340 QLEEERNSLQDQLDEEMEAKQNLERHIS---TLNIQLSD--SKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAA 1414
Cdd:PRK10929 290 QAASQTLQVRQALNTLREQSQWLGVSNAlgeALRAQVARlpEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQAD 369
|
410 420 430
....*....|....*....|....*....|..
gi 13124875 1415 YDKLEKTKNRLqqeLDDLvvdLDNQRQLVSNL 1446
Cdd:PRK10929 370 GQPLTAEQNRI---LDAQ---LRTQRELLNSL 395
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1520-1706 |
1.33e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1520 KDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAtedakLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLH 1599
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1600 EYETELEDERKQRALAAAAKKKLEGD--LKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARAS-RDEIFATAK 1676
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILA 316
|
170 180 190
....*....|....*....|....*....|
gi 13124875 1677 ENEKKAKSLEADLMQLQEDLAAAERARKQA 1706
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1725-1875 |
1.45e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1725 NALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNEsARQQLERQNKELRSKLHEM 1804
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-EQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1805 EGAVK--SKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKG 1875
Cdd:COG1579 99 ESLKRriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
841-1407 |
1.50e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 841 VKPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLA------ 914
Cdd:pfam10174 160 IKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTviemkd 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 915 AKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQN 994
Cdd:pfam10174 240 TKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQN 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 995 NKLSKERKLLEErisdlttNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHE----- 1069
Cdd:pfam10174 320 SDCKQHIEVLKE-------SLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvk 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1070 --QIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdlgEE 1147
Cdd:pfam10174 393 erKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL---EE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1148 LEALKTELEDTLDSTATQQELRAKREQEVTVLKkaldeETRSHEAQVQEMRQKHAQAVE-ELTEQLEQFKRAKANLDKNK 1226
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTEKESSLIDLK-----EHASSLASSGLKKDSKLKSLEiAVEQKKEECSKLENQLKKAH 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1227 QTLEKEnadlagelrvlgQAKQEVEHKKKKLEaqvQELQSKCSDGERARAELN---DKVHKLQNEVESVTGMLNEAEGKA 1303
Cdd:pfam10174 545 NAEEAV------------RTNPEINDRIRLLE---QEVARYKEESGKAQAEVErllGILREVENEKNDKDKKIAELESLT 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1304 IKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKlRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDF 1383
Cdd:pfam10174 610 LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEK 688
|
570 580
....*....|....*....|....
gi 13124875 1384 ASTVEALEEGKKRFQKEIENLTQQ 1407
Cdd:pfam10174 689 DGHLTNLRAERRKQLEEILEMKQE 712
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1006-1273 |
1.51e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmql 1085
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1086 aKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSER----------AARNKAEKQKRDLGEELEALKTEL 1155
Cdd:COG1340 78 -EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspEEEKELVEKIKELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1156 EDTLDSTATQQELRAKREQ--EVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQT---LE 1230
Cdd:COG1340 157 EKNEKLKELRAELKELRKEaeEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEiieLQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 13124875 1231 KENADLAGELRVL--GQAKQEVEHKKKKLEAQVQELQSKCSDGER 1273
Cdd:COG1340 237 KELRELRKELKKLrkKQRALKREKEKEELEEKAEEIFEKLKKGEK 281
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
802-1074 |
1.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 802 ARKAFAKRQQQLTAMkviQRNCAAYLKLRNWQWwrlftkvkPLLQVTRQEEEMQAKEDELqktkERQQKAENELKELEQK 881
Cdd:COG4913 629 AEERLEALEAELDAL---QERREALQRLAEYSW--------DEIDVASAEREIAELEAEL----ERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 882 HSQLTEEKNLLQEQLQAETELYAEAEEmrvRLAAKKQELEEilhemeaRLEEEEDRGQQLQAERKKMAQQMLDLEEQLEE 961
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDE-------LQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 962 EEAARQKLQLEKVTAEAKIKKLEDEIlvmddqNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHesmISELEV 1041
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG---LPEYEE 834
|
250 260 270
....*....|....*....|....*....|....*
gi 13124875 1042 RLK--KEEKSRQELEKLKRKLEGDASDFHEQIADL 1074
Cdd:COG4913 835 RFKelLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1763-1920 |
1.78e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1763 TQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHemegavKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATK 1842
Cdd:PTZ00491 645 TRDSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLE------RQKMHDKAKAEEQRTKLLELQAESAAVESSGQSR 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1843 SlkQKDKKLKEILLQVEDERKMAEqYKEQAEK--GNARVKQLKRQLEEAEEESQRINANRRKLQRELDEaTESN------ 1914
Cdd:PTZ00491 719 A--EALAEAEARLIEAEAEVEQAE-LRAKALRieAEAELEKLRKRQELELEYEQAQNELEIAKAKELAD-IEATkferiv 794
|
....*.
gi 13124875 1915 EAMGRE 1920
Cdd:PTZ00491 795 EALGRE 800
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1635-1924 |
1.86e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1635 SAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIfataKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELA 1714
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKI----DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1715 EELASSLSgrnalqdeKRRLEARIAQLEEELEEEQGNMeamsdrvrkATQQAEQLSNELATERstAQKNESARQQlerQN 1794
Cdd:PRK11281 115 RETLSTLS--------LRQLESRLAQTLDQLQNAQNDL---------AEYNSQLVSLQTQPER--AQAALYANSQ---RL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1795 KELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATkslkqkdkklkeiLLQvederkmaEQYKEQAEK 1874
Cdd:PRK11281 173 QQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNT-------------QLQ--------DLLQKQRDY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1875 GNARVKQLKRQLEEAEEEsqrINANRRKL-QRELDEATESNEAMGREVNAL 1924
Cdd:PRK11281 232 LTARIQRLEHQLQLLQEA---INSKRLTLsEKTVQEAQSQDEAARIQANPL 279
|
|
| ASY3-like |
pfam20435 |
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific ... |
1008-1113 |
2.04e-04 |
|
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific proteins, such as AtASY3 from Arabidopsis and PAIR3 from rice. They are coiled-coil domain proteins required for normal meiosis. PAIR3 is an axial element and part of the synaptonemal complex (SC) that forms between homologous chromosomes during meiosis. Members of this family are homologs of SCYP2 from vertebrates and fungal Red1/Rec10.
Pssm-ID: 466584 [Multi-domain] Cd Length: 793 Bit Score: 46.42 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1008 ISDLTTNLAEEEEKAKNLTKLKNKHEsmiselEVRLK-KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLA 1086
Cdd:pfam20435 667 LENIKSHIITEAGKTSNLAKTKRKHA------ETRLQeQEEKMRMIHEKFKDDVSHHLEDFKSTIEELEANQSELKGSIK 740
|
90 100
....*....|....*....|....*...
gi 13124875 1087 KKEEELQAALARLDDEIAQK-NNALKKI 1113
Cdd:pfam20435 741 KQRTSHQKLIAHFEGGIETKlDDATKRI 768
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1308-1482 |
2.40e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1308 KDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLE----EERNSLQDQLD-----------------EEMEAKQNLERHI 1366
Cdd:PRK11637 82 EAISQASRKLRETQNTLNQLNKQIDELNASIAKLEqqqaAQERLLAAQLDaafrqgehtglqlilsgEESQRGERILAYF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1367 STLNIQLSDSKKKLQDFASTV---EALEEGKKRFQKEIenLTQQYEEKAaaydKLEKTKNRLQQELDdlvvdldnqrQLV 1443
Cdd:PRK11637 162 GYLNQARQETIAELKQTREELaaqKAELEEKQSQQKTL--LYEQQAQQQ----KLEQARNERKKTLT----------GLE 225
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13124875 1444 SNLEKKQRKFDQLLAEEKNISSKYAD-ERD---RAEAEAREKE 1482
Cdd:PRK11637 226 SSLQKDQQQLSELRANESRLRDSIARaEREakaRAEREAREAA 268
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1821-1929 |
2.50e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1821 AKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVE---DERKMAEQYKE-QAEKGNARVKQLKRQLEEAEEESQRI 1896
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLErlrREREKAERYQAlLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110
....*....|....*....|....*....|...
gi 13124875 1897 NANRRKLQRELDEATESNEAMGREVNALKSKLR 1929
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLE 275
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
851-1142 |
2.53e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 851 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRvrlaakKQELEEIlhemear 930
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKR------DELNEKV------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 931 leeeedrgQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLeERISD 1010
Cdd:COG1340 74 --------KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELV-EKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1011 LTTNLaeeeEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKlegdASDFHEQIADLQAQIAELKMQLAKKEE 1090
Cdd:COG1340 145 LEKEL----EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEE----AQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1091 ELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKR 1142
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
855-1218 |
2.70e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.90 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 855 QAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQlqAETELYAEAEEMrvrlaaKKQELEEILHEMEARLEEE 934
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPK--SEQEKEKALEEV------LKEAISKAESATAVAKEAK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 935 EDRGQQLQAERKKMAQQMLDLEEQLEEeeAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTN 1014
Cdd:pfam09731 153 DDAIQAVKAHTDSLKEASDTAEISREK--ATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1015 LAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSR--------QELEKL-KRKLEGDASDFHEQIADLQAQIAELKMQL 1085
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIfpdiipvlKEDNLLsNDDLNSLIAHAHREIDQLSKKLAELKKRE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1086 AKK-EEELQAALARLDDEIAQKNNALKKIRELEghISDLQEDLDSERAARNKAEKQKrdLGEELEALKTELEDTLDSTAT 1164
Cdd:pfam09731 311 EKHiERALEKQKEELDKLAEELSARLEEVRAAD--EAQLRLEFEREREEIRESYEEK--LRTELERQAEAHEEHLKDVLV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1165 QQELRAKREQEvtvlkkaldeetRSHEAQVQEMRQKHAQAVEELTEQLEQFKRA 1218
Cdd:pfam09731 387 EQEIELQREFL------------QDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1071-1292 |
2.73e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1071 IADLQAQIAELKMQlAKKEEELQAALArlDDEIAQKNNAL---KKIRELEgHISDLQEDLDS--ERAARNKAEKQKRDLG 1145
Cdd:NF012221 1537 TSESSQQADAVSKH-AKQDDAAQNALA--DKERAEADRQRleqEKQQQLA-AISGSQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1146 EELEALKTELE------DTLDSTATQQELRAKREQE------VTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLE 1213
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDQWRNpfagglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1214 QFKRAKANLDKNKQTLEKENADLA--GELR---VLGQaKQEVEHKKKKLEAQVQELQSKcsdGERARAELNDKVHKLQNE 1288
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDIDDAKadAEKRkddALAK-QNEAQQAESDANAAANDAQSR---GEQDASAAENKANQAQAD 1768
|
....
gi 13124875 1289 VESV 1292
Cdd:NF012221 1769 AKGA 1772
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1642-1928 |
2.81e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1642 EAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEAdlmqlQEDLAAAERAR-----KQADLEKEELAEE 1716
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER-----RRKLEEAEKARqaemdRQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1717 LASSLSGRNALQDEKRRLEARIAQLEEELEEEQgnMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKE 1796
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEISR--MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1797 LRSKLHEMEGAVKSKFKstiaALEAKIAQLEEQVEQEAREKQAATKSLKQKD---KKLKEILLQVEDERKMAEQY----- 1868
Cdd:pfam17380 422 MEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEeerKRKKLELEKEKRDRKRAEEQrrkil 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1869 -KEQAEKGNARV------KQLKRQLEE-----AEEESQRINANRRKLQRELDEATESNEAMgREVNALKSKL 1928
Cdd:pfam17380 498 eKELEERKQAMIeeerkrKLLEKEMEErqkaiYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1757-1936 |
2.99e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1757 DRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKskfkstIAALEAKIAQLEEQVEQEARE 1836
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ------LLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1837 KQAatksLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKR-QLEEAEEESQRINANRRKLQRELDEATESNE 1915
Cdd:COG4717 148 LEE----LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180
....*....|....*....|.
gi 13124875 1916 AMGREVNALKSKLRGPPPQET 1936
Cdd:COG4717 224 ELEEELEQLENELEAAALEER 244
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1081-1251 |
3.03e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1081 LKMQLAKKEEelqaALARLDDEIAQKNNALKkireLE-GHISDLQEDLDSERAARNKAEkqkrdlgeeleALKTELEDTL 1159
Cdd:PRK09039 44 LSREISGKDS----ALDRLNSQIAELADLLS----LErQGNQDLQDSVANLRASLSAAE-----------AERSRLQALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1160 DSTATQQELRAKREQEvtvLKKALDEE-TRSHEAQVQemrqkhaqaVEELTEQLEQFKRAKANLDKNKQTLEKEN----- 1233
Cdd:PRK09039 105 AELAGAGAAAEGRAGE---LAQELDSEkQVSARALAQ---------VELLNQQIAALRRQLAALEAALDASEKRDresqa 172
|
170 180
....*....|....*....|.
gi 13124875 1234 --ADLAGELRV-LGQAKQEVE 1251
Cdd:PRK09039 173 kiADLGRRLNVaLAQRVQELN 193
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1278-1530 |
3.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1278 LNDKVHKLQNEVESVTGMLNEAEGKaIKLAKDvaslssqLQDTQELLQEETRQKL-NVSTKLRQLEEERNSLQDQLDEEM 1356
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQ-IKTYNK-------NIEEQRKKNGENIARKqNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1357 EA----KQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKkrfqkEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDL 1432
Cdd:PHA02562 244 LNlvmdIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGG-----VCPTCTQQISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1433 VVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIssKYADERDRAEAEAREKETKALSLARALEEALEakeelertnKMLKAE 1512
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKISTN--KQSLITLVDKAKKVKAAIEELQAEFVDNAEEL---------AKLQDE 387
|
250
....*....|....*...
gi 13124875 1513 MEDLVSSKDDVGKNVHEL 1530
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHR 405
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
846-1136 |
3.93e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILH 925
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 926 EMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLE 1005
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1006 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQL 1085
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1086 AKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNK 1136
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1235-1441 |
4.44e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1235 DLAGELRVLGQAKQEVEHKKKKLEAQVQELQS-KCSDGEraRAELNDKVHKLQN------EVESVTGMLNEAE------- 1300
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAaALQPGE--EEELEEERRRLSNaeklreALQEALEALSGGEggaldll 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1301 GKAIKLAKDVASLSSQLQDTQELLQEetrqklnVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNiQLsdsKKKl 1380
Cdd:COG0497 247 GQALRALERLAEYDPSLAELAERLES-------ALIELEEAASELRRYLDSLEFDPERLEEVEERLALLR-RL---ARK- 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1381 qdFASTVEALEEGKKRFQKEIENLTQQYEEKAAaydkLEKTKNRLQQELDDLVVDLDNQRQ 1441
Cdd:COG0497 315 --YGVTVEELLAYAEELRAELAELENSDERLEE----LEAELAEAEAELLEAAEKLSAARK 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1336-1484 |
5.91e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1336 TKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQ---------KEIENLTQ 1406
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13124875 1407 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDnqrQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETK 1484
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELA---ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1144-1427 |
6.28e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1144 LGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALD---EETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKA 1220
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1221 NLDKNKQTLEKENAD-------LAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVT 1293
Cdd:pfam07888 112 ELSEEKDALLAQRAAhearireLEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1294 GMLNEAEGkaiKLAKDVASLsSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQL 1373
Cdd:pfam07888 192 KEFQELRN---SLAQRDTQV-LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13124875 1374 SDSKKKLQ-----------DFASTVEALEEGKKRFQKEIENLTQQYEekaAAYDKLEKTKNRLQQ 1427
Cdd:pfam07888 268 DRTQAELHqarlqaaqltlQLADASLALREGRARWAQERETLQQSAE---ADKDRIEKLSAELQR 329
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1231-1595 |
6.74e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1231 KENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCsDGERARAELNDKVHKL-------------QNEVESVTGMLN 1297
Cdd:pfam17380 259 RYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM-EQERLRQEKEEKAREVerrrkleeaekarQAEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1298 EAEGKAIKLAKDVA--SLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLErhistlnIQLSD 1375
Cdd:pfam17380 338 EQERMAMERERELEriRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVK-------ILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1376 SKKKLQDFASTVEAL-EEGKKRFQKEIENLTqqyEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRkfD 1454
Cdd:pfam17380 411 RQRKIQQQKVEMEQIrAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR--D 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1455 QLLAEEKNisskyadeRDRAEAEAREKETKALslaraleealeakeELERTNKMLKAEMEDLvsskddvGKNVHELEKSK 1534
Cdd:pfam17380 486 RKRAEEQR--------RKILEKELEERKQAMI--------------EEERKRKLLEKEMEER-------QKAIYEEERRR 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1535 RAletqmEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQ 1595
Cdd:pfam17380 537 EA-----EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
960-1466 |
7.28e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 960 EEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLS---KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMI 1036
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKII 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1037 SElevrlkKEEKSRQELEKLkRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAALARLDDEIAQKNNALKKIREL 1116
Cdd:PRK01156 287 ND------PVYKNRNYINDY-FKYKNDIENKKQILSNIDAEINKYH-AIIKKLSVLQKDYNDYIKKKSRYDDLNNQILEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1117 EGHISDLQEDLDS----ERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQ---EVTVLKKALDeETRS 1189
Cdd:PRK01156 359 EGYEMDYNSYLKSieslKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIR-ALRE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1190 HEAQVQE-MRQKHAQAV----------EELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKK-KKL 1257
Cdd:PRK01156 438 NLDELSRnMEMLNGQSVcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEiNKS 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1258 EAQVQELQSKCSDGERARAELN------DKVHKLQNEVESVTgmLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQK 1331
Cdd:PRK01156 518 INEYNKIESARADLEDIKIKINelkdkhDKYEEIKNRYKSLK--LEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1332 LN-VSTKLRQLE---EERNSLQDQLDEEMEAKQNLerhistlniqLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1407
Cdd:PRK01156 596 LNdLESRLQEIEigfPDDKSYIDKSIREIENEANN----------LNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1408 YEEKAAAYDKLEKTKNRLQQ---ELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAE-EKNISSK 1466
Cdd:PRK01156 666 IPDLKEITSRINDIEDNLKKsrkALDDAKANRARLESTIEILRTRINELSDRINDiNETLESM 728
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
940-1110 |
7.35e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 940 QLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQ--NNKLSKERKLLEERISDLTTNLAE 1017
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1018 EEEKAKNLTKLKNKHESMISELEVRLKKEEKsrqELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAKKEEELQAALA 1097
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELD-------EELAELEAELEELEAEREELAAKIPPELL 177
|
170
....*....|...
gi 13124875 1098 RLDDEIAQKNNAL 1110
Cdd:COG1579 178 ALYERIRKRKNGL 190
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1221-1412 |
7.88e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1221 NLDKNKQTLEKENADlagelRVLGQAKQEVEHKKKKLEAQVQElqskcsdgeraraelndKVHKLQNEVEsvtgmlneae 1300
Cdd:PRK12704 27 KIAEAKIKEAEEEAK-----RILEEAKKEAEAIKKEALLEAKE-----------------EIHKLRNEFE---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1301 gkaiklaKDVASLSSQLQDTQELLQeetRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKL 1380
Cdd:PRK12704 75 -------KELRERRNELQKLEKRLL---QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 13124875 1381 QDFA--STVEA----LEEGKKRFQKEIENLTQQYEEKA 1412
Cdd:PRK12704 145 ERISglTAEEAkeilLEKVEEEARHEAAVLIKEIEEEA 182
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1684-1832 |
7.95e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.95 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1684 SLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQG--NMEAMSDRVRK 1761
Cdd:pfam00529 62 SAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrrVLAPIGGISRE 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1762 ATQQAEQLSNEL-ATERSTAQKNESARQQLERQNKELRSKLhemegavkskfKSTIAALEAKIAQLEEQVEQ 1832
Cdd:pfam00529 142 SLVTAGALVAQAqANLLATVAQLDQIYVQITQSAAENQAEV-----------RSELSGAQLQIAEAEAELKL 202
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
876-1126 |
8.02e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 876 KELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEilhemearleeeedrgqQLQAERKKMAQQMLDL 955
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYD-----------------ELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 956 EEQLEEEEaarqkLQLEKVTAEakIKKLEDEILVMDDQNNKLSKERKLLEE---------RISDLTTNLAEEEEKAKNLT 1026
Cdd:PHA02562 240 TDELLNLV-----MDIEDPSAA--LNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1027 KLKNKHESMISELEVRLKKEEKSRQELEKLKRKLE---GDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEI 1103
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIStnkQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|...
gi 13124875 1104 AQKNNALKKIRELeGHISDLQED 1126
Cdd:PHA02562 393 KTKSELVKEKYHR-GIVTDLLKD 414
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
978-1185 |
8.02e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 978 AKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTT----NLAEEEEKAKNLTKLKNKHESMISELEVRLKkeeksrqEL 1053
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDELL-------NL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1054 EKLKRKLEGDASDFHEQIADLQAQIAELK--MQLAKKEEELQAALARLDDE------IAQKNNAL-KKIRELEGHISDLQ 1124
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQkvIKMYEKGGVCPTCTQQISEGpdritkIKDKLKELqHSLEKLDTAIDELE 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1125 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKR---EQEVTVLKKALDE 1185
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQDELDK 390
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
995-1129 |
8.08e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.51 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 995 NKLSKERKLLEERISDLTTNLAE-EEEKAKNLTKLKNKHESMISELEvrLKKEEKSRQELEKLKRKLEGD----ASDFHE 1069
Cdd:cd22656 124 DDLLKEAKKYQDKAAKVVDKLTDfENQTEKDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLneeyAAKLKA 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1070 QIADLQAQIAELKMQLAKKE---EELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDS 1129
Cdd:cd22656 202 KIDELKALIADDEAKLAAALrliADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDS 264
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
872-1356 |
8.20e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 872 ENELKELeQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEeilhemearleeeedrgqqlQAERKkmaqq 951
Cdd:PRK11281 42 QAQLDAL-NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLA--------------------QAPAK----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 952 mldleeqleeeeaarqklqLEKVTAE-AKIKKLEDEilVMDDQNNKLSKER--KLLEERISDLTT---NLAEEEEKAKNL 1025
Cdd:PRK11281 96 -------------------LRQAQAElEALKDDNDE--ETRETLSTLSLRQleSRLAQTLDQLQNaqnDLAEYNSQLVSL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1026 TKLKNKHESMISELEVRLkkeeksrQELEK-LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIA 1104
Cdd:PRK11281 155 QTQPERAQAALYANSQRL-------QQIRNlLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1105 QKNNALKKIRELEGHISDLQEDLDSERaarnkaekqkrdlgeelealKTELEDTLDSTATQQElrAKREQEVTVLKKALD 1184
Cdd:PRK11281 228 QRDYLTARIQRLEHQLQLLQEAINSKR--------------------LTLSEKTVQEAQSQDE--AARIQANPLVAQELE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1185 EETrsheaqvqEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQT---LEKENADLAGEL---RVLGQAKQEVEHKK--KK 1256
Cdd:PRK11281 286 INL--------QLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSernIKEQISVLKGSLllsRILYQQQQALPSADliEG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1257 LEAQVQELQSKCSDGERARAEL---NDKVHKL-QNEVESVTGMLNEAegkaiklakdvasLSSQLQDTQELLQEETRQ-- 1330
Cdd:PRK11281 358 LADRIADLRLEQFEINQQRDALfqpDAYIDKLeAGHKSEVTDEVRDA-------------LLQLLDERRELLDQLNKQln 424
|
490 500 510
....*....|....*....|....*....|.
gi 13124875 1331 -KLNVSTKL----RQLEEERNSLQDQLDEEM 1356
Cdd:PRK11281 425 nQLNLAINLqlnqQQLLSVSDSLQSTLTQQI 455
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
867-1065 |
8.72e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 867 RQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAE--------AEEMRVRlaakKQELEEilhEMEARLEEEEDRG 938
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREEleleqqrrFEEIRLR----KQRLEE---ERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 939 QQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEilvmddqnnKLSKERKLLEErisdlttnLAEE 1018
Cdd:pfam15709 412 LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEM---------QLAEEQKRLME--------MAEE 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13124875 1019 EEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDAS 1065
Cdd:pfam15709 475 ERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1048-1265 |
9.25e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1048 KSRQELEKLKRKLEGDASDFHEQIADLQAQIAEL-KMQLAKKE-EELQAALARLD--DEIAQK-NNALKKIRELEGHISD 1122
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEERRRLSnaEKLREAlQEALEALSGGEGGALD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1123 LQEDLDSERAARNKAEKQKRDLGEELEALKTELED---TLDSTATQQELRAKREQEVtvlkkaldeETRSheAQVQEMRQ 1199
Cdd:COG0497 245 LLGQALRALERLAEYDPSLAELAERLESALIELEEaasELRRYLDSLEFDPERLEEV---------EERL--ALLRRLAR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1200 KHAQAVEELTEQLEQFKRAKANL---DKNKQTLEKENADLAGELRVLGQAKQEVEHKK-KKLEAQV-QELQ 1265
Cdd:COG0497 314 KYGVTVEELLAYAEELRAELAELensDERLEELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVtAELA 384
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1642-1842 |
9.49e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1642 EAIKQLRKLQAQMKDFQRELEDARASRDEIFATA-KENEkkakslEADLMQLQEDLAAAERARKQADLEKEELAEELASS 1720
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAAlQPGE------EEELEEERRRLSNAEKLREALQEALEALSGGEGGA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1721 LSgrnALQDEKRRLEaRIAQleeeleeEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLE-RQN----- 1794
Cdd:COG0497 243 LD---LLGQALRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEeRLAllrrl 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13124875 1795 ---------------KELRSKLHEMEGAvkskfKSTIAALEAKIAQLEEQVEQEARE-----KQAATK 1842
Cdd:COG0497 312 arkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaarKKAAKK 374
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1443-1888 |
9.94e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1443 VSNLEKKQRKFDQLLAEEKNISS---KYADERDRAEAEAREKETKAlslARALEEALEAKEELERTNKMLKAemedlVSS 1519
Cdd:COG3096 274 MRHANERRELSERALELRRELFGarrQLAEEQYRLVEMARELEELS---ARESDLEQDYQAASDHLNLVQTA-----LRQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1520 KDDVGKNVHELEKSKRALETQMEemktQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQneeKRRQLQRQlh 1599
Cdd:COG3096 346 QEKIERYQEDLEELTERLEEQEE----VVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQ---QTRAIQYQ-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1600 EYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARA-----SRDEIFAT 1674
Cdd:COG3096 417 QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1675 AKENEKKAKSLEA---DLMQLQEDLAAAERA---RKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQleeeleee 1748
Cdd:COG3096 497 ARELLRRYRSQQAlaqRLQQLRAQLAELEQRlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE-------- 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1749 qgnmeaMSDRVRKATQQAEQLSNELaterstaqknesarQQLERQNKELRSKLHEMegavkskfkstiAALEAKIAQLEE 1828
Cdd:COG3096 569 ------LEEQAAEAVEQRSELRQQL--------------EQLRARIKELAARAPAW------------LAAQDALERLRE 616
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1829 QVEQEAREKQAATKSLKQkdkklkeillQVEDERKmAEQYKEQAEkgnARVKQLKRQLEE 1888
Cdd:COG3096 617 QSGEALADSQEVTAAMQQ----------LLERERE-ATVERDELA---ARKQALESQIER 662
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
869-1055 |
1.03e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 869 QKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemearleeeedrgQQLQAERKKM 948
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI--------------EEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 949 AQQMLDLEEQLEEeeaarQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEeekaknltkl 1028
Cdd:COG1579 79 EEQLGNVRNNKEY-----EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---------- 143
|
170 180
....*....|....*....|....*..
gi 13124875 1029 KNKHESMISELEVRLKKEEKSRQELEK 1055
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAA 170
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
982-1333 |
1.04e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 43.69 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 982 KLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEkakNLTKLKNKHESMIS--ELEVRLKKEEKSrqeLEKLKRK 1059
Cdd:pfam03148 61 ELEKELEELDEEIELLLEEKRRLEKALEALEEPLHIAQE---CLTLREKRQGIDLVhdEVEKELLKEVEL---IEGIQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1060 LEGDASDFHEQIADLQAQIAELKMQLAKKEE-----ELQAALARLDDEIAQKNNALKkireLEGHISDLQEDLDSERAAR 1134
Cdd:pfam03148 135 LQRTLEQAWEQLRLLRAARHKLEKDLSDKKEaleidEKCLSLNNTSPNISYKPGPTR----IPPNSSTPEEWEKFTQDNI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1135 NKAEKQKRDLgeelEALKTELEDTLdstatqqelrakreqevtvlkkaldeetrsheAQVQEMRQKHAQAVEE-LTEQLE 1213
Cdd:pfam03148 211 ERAEKERAAS----AQLRELIDSIL--------------------------------EQTANDLRAQADAVNFaLRKRIE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1214 QFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKK----KLEAQVQ----ELqskCSDgeRARAELNDKVHKL 1285
Cdd:pfam03148 255 ETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKlaqtRLENRTYrpnvEL---CRD--EAQYGLVDEVKEL 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 13124875 1286 QNEVESVTGMLNEAEgkaiklakdvASLsSQLQDTQELLQEETRQKLN 1333
Cdd:pfam03148 330 EETIEALKQKLAEAE----------ASL-QALERTRLRLEEDIAVKAN 366
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1143-1275 |
1.06e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1143 DLGEELEALKTELEDTLdstatqQELRAKReQEVTVLKKALDEETRS----HEAQVQEMRQKHAQAVEELTEQLEQFKRA 1218
Cdd:PRK00409 520 ELIASLEELERELEQKA------EEAEALL-KEAEKLKEELEEKKEKlqeeEDKLLEEAEKEAQQAIKEAKKEADEIIKE 592
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1219 KANLDKNKQTLEKENaDLAGELRVLGQAKQEVEHKKKKLEAQVQELQSkcsdGERAR 1275
Cdd:PRK00409 593 LRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQEELKV----GDEVK 644
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1059-1213 |
1.06e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.87 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1059 KLEGDASDFHEQIADLQAQIAELKMQLAKK-EEELQAALARLDDEIAQKNNALKKIRE-----LEGHISDLQEDLDSE-R 1131
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRlEKETEALRERLQKDLEEVRAKLEPYLEelqakLGQNVEELRQRLEPYtE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1132 AARNKAEKQKRDLGEELEALKTELEDTLDSTATQ---------QELRAKREQEVTVLKKALDEETRSHEAQ----VQEMR 1198
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDAlrarlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQELR 160
|
170
....*....|....*
gi 13124875 1199 QKHAQAVEELTEQLE 1213
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
964-1105 |
1.07e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 964 AARQKLQLEKVTAEakIKKLEDEILVMDDQNNKLSKERKLL-EERISDLTTNLAEEEEKaknltklknkhesmISELEVR 1042
Cdd:COG0542 399 AARVRMEIDSKPEE--LDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEE--------------LEALKAR 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124875 1043 LKKEEKSRQELEKLKRKLEGDasdfHEQIADLQAQIAELKMQLAKKEEELQAALArlDDEIAQ 1105
Cdd:COG0542 463 WEAEKELIEEIQELKEELEQR----YGKIPELEKELAELEEELAELAPLLREEVT--EEDIAE 519
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1063-1208 |
1.17e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1063 DASDFHEQIADLQAQIAELKMQLAKKE---------EELQAALARLDDEIAQKNNALKKIREL--EGHISdlQEDLDSER 1131
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALykKGAVS--QQELDEAR 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1132 AARNKAEKQkrdlgeeLEALKTELEDTLDSTATQQELRAKreqevtvlkkaldeetrshEAQVQEMRQKHAQAVEEL 1208
Cdd:COG1566 155 AALDAAQAQ-------LEAAQAQLAQAQAGLREEEELAAA-------------------QAQVAQAEAALAQAELNL 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1811-1929 |
1.20e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1811 KFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKG-NAR--------VKQ 1881
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKeyealqkeIES 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 13124875 1882 LKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLR 1929
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1578-1912 |
1.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1578 RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDF 1657
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1658 QRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEAR 1737
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1738 IAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIA 1817
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1818 ALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRIN 1897
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
330
....*....|....*
gi 13124875 1898 ANRRKLQRELDEATE 1912
Cdd:COG4372 354 DVLELLSKGAEAGVA 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1781-1935 |
1.35e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1781 QKNESARQQLERQNKELRSKLHEMEGAVK------SKFKSTIAALEAKIAQLEEQVEQ-EAREKQAATKSLKQKD-KKLK 1852
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAalearlEAAKTELEDLEKEIKRLELEIEEvEARIKKYEEQLGNVRNnKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1853 EILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRGPP 1932
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
...
gi 13124875 1933 PQE 1935
Cdd:COG1579 173 PPE 175
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1119-1901 |
1.38e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1119 HISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTAT-------------QQELRAKREQeVTVLKKALDE 1185
Cdd:NF041483 16 HLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASrpaydgadigyqaEQLLRNAQIQ-ADQLRADAER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1186 ETRSHEAQVQEMRQKHAQAVEEL-----TEQLEQFKRAKANLDKNKQTLE---KENADLAGEL---------RVLGQAKQ 1248
Cdd:NF041483 95 ELRDARAQTQRILQEHAEHQARLqaelhTEAVQRRQQLDQELAERRQTVEshvNENVAWAEQLrartesqarRLLDESRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1249 EVEHKKKKLEAQVQEL-----QSKCSDGERARAELNDKVHKLQNEVESvtgMLNEAEGKaiklAKDVASLSSQLQDTQEL 1323
Cdd:NF041483 175 EAEQALAAARAEAERLaeearQRLGSEAESARAEAEAILRRARKDAER---LLNAASTQ----AQEATDHAEQLRSSTAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1324 LQEETRQKlnvSTKLRQLEEERnsLQDQLDEEMEAKQNLERhistlniQLSDSKKKLQDFASTVEALEEGKKRFQK-EIE 1402
Cdd:NF041483 248 ESDQARRQ---AAELSRAAEQR--MQEAEEALREARAEAEK-------VVAEAKEAAAKQLASAESANEQRTRTAKeEIA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1403 NLTQQYEEKAaaydklEKTKNRLQQELDDLVVDLDnqrQLVSNLEKKQRkfdQLLAEEKnisskyADERDRAEAEAREKE 1482
Cdd:NF041483 316 RLVGEATKEA------EALKAEAEQALADARAEAE---KLVAEAAEKAR---TVAAEDT------AAQLAKAARTAEEVL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1483 TKALSLARALEEALEAKEELERTNKmlKAEMEDLVSSKDDVGknvhelEKSKRALETQMEEMKTQLEELEDELQatedaK 1562
Cdd:NF041483 378 TKASEDAKATTRAAAEEAERIRREA--EAEADRLRGEAADQA------EQLKGAAKDDTKEYRAKTVELQEEAR-----R 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1563 LRLEVNmqalkgQFERDLQARDEQ-NEEKRRQLQRQLHEYETELEDerkqralaaaAKKKLEGDLKDLELQADS-AIKGR 1640
Cdd:NF041483 445 LRGEAE------QLRAEAVAEGERiRGEARREAVQQIEEAARTAEE----------LLTKAKADADELRSTATAeSERVR 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1641 EEAIKQLRKLQAQMKDfqrELEDARASRDEIFATAKENEKKAKS-LEADLMQLQEDLAAAERARK-QADLEKEELAEELA 1718
Cdd:NF041483 509 TEAIERATTLRRQAEE---TLERTRAEAERLRAEAEEQAEEVRAaAERAARELREETERAIAARQaEAAEELTRLHTEAE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1719 SSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAmsDRVRKATQQAEQLSNELATErsTAQKNESARQQLERQNKELR 1798
Cdd:NF041483 586 ERLTAAEEALADARAEAERIRREAAEETERLRTEAA--ERIRTLQAQAEQEAERLRTE--AAADASAARAEGENVAVRLR 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1799 SKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLqvEDERKMAEQYKEQA-EKGNA 1877
Cdd:NF041483 662 SEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETL--GSARAEADQERERArEQSEE 739
|
810 820
....*....|....*....|....*.
gi 13124875 1878 RVKQLKRQLEEAEEESQRI--NANRR 1901
Cdd:NF041483 740 LLASARKRVEEAQAEAQRLveEADRR 765
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1413-1640 |
1.42e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1413 AAYDKLEKTKNR-LQQELDDLVVDLDN-------QRQLVSNLEK--------KQRKFDQLLAEEKNISSKYADERDRAEA 1476
Cdd:PHA02562 166 SEMDKLNKDKIReLNQQIQTLDMKIDHiqqqiktYNKNIEEQRKkngeniarKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1477 EAREKETKALSLARALEEALEAKEELERTNKMLK---------AEMEDLVSSKDDVGK---NVHELEKSKRALETQMEEm 1544
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKikdKLKELQHSLEKLDTAIDE- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1545 ktqLEELEDELQATEDAKLRLEVNMQALKGQFER-DLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLE 1623
Cdd:PHA02562 325 ---LEEIMDEFNEQSKKLLELKNKISTNKQSLITlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
250
....*....|....*....
gi 13124875 1624 GDLKDL--ELQADSAIKGR 1640
Cdd:PHA02562 402 KYHRGIvtDLLKDSGIKAS 420
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1529-1928 |
1.50e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1529 ELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErdlQARDEQNEEKRRQLQRQLHEYETELEDE 1608
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAH---IKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1609 RKQRALaaaakkklegdlkdleLQADSAikGREEAIKQLRKLQAQMKDFQRELEDARASRDEIfatakeneKKAKSLEAD 1688
Cdd:TIGR00618 327 LMKRAA----------------HVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS--------CQQHTLTQH 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1689 LMQLQEDLAAAE---RARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQ 1765
Cdd:TIGR00618 381 IHTLQQQKTTLTqklQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1766 AEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQeaREKQAATKSLK 1845
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT--RRMQRGEQTYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1846 QKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALK 1925
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
...
gi 13124875 1926 SKL 1928
Cdd:TIGR00618 619 RKL 621
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1816-1921 |
1.56e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1816 IAALEAKIAQLEEQVEQEAREKQAATKSLKQKDK-KLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQ 1894
Cdd:COG0542 406 IDSKPEELDELERRLEQLEIEKEALKKEQDEASFeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|....*..
gi 13124875 1895 RINANRRKLQrELDEATESNEAMGREV 1921
Cdd:COG0542 486 KIPELEKELA-ELEEELAELAPLLREE 511
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1215-1685 |
1.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1215 FKRAKANLDKNKQTLEkenadlagELRVLGQAKQEVEHkkkKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTG 1294
Cdd:PRK04863 232 FQDMEAALRENRMTLE--------AIRVTQSDRDLFKH---LITESTNYVAADYMRHANERRVHLEEALELRRELYTSRR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1295 MLNEAEGKAIKLAKDVASLSSQLQDTQELLQeETRQKLN-VSTKLRQLEEErnslqDQLDEEMEAkqnlerhistLNIQL 1373
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDYQ-AASDHLNlVQTALRQQEKI-----ERYQADLEE----------LEERL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1374 SDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQElddlVVDLDNQRQLVSNLEKKQRKF 1453
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQA----VQALERAKQLCGLPDLTADNA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1454 DQLLAEEKNISSKYADERDRAE------AEAREKETKALSLARAleealeakeelertnkmLKAEMEDlvSSKDDVGKNV 1527
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEqklsvaQAAHSQFEQAYQLVRK-----------------IAGEVSR--SEAWDVAREL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1528 HELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLevnmQALKGQFERDLQARDEQnEEKRRQLQRQLHEYETELED 1607
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLL----AEFCKRLGKNLDDEDEL-EQLQEELEARLESLSESVSE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1608 ERKQRALAAAAKKKLEGDLKDLELQA-------DSAIKGRE---EAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKE 1677
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARApawlaaqDALARLREqsgEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
....*...
gi 13124875 1678 NEKKAKSL 1685
Cdd:PRK04863 657 LDEEIERL 664
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1816-1922 |
1.79e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1816 IAALEAKIAQLEEQVEQEAREKQAATKslkqkdKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQR 1895
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASF------ERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK 486
|
90 100
....*....|....*....|....*..
gi 13124875 1896 INAnrrkLQRELDEATESNEAMGREVN 1922
Cdd:COG0542 487 IPE----LEKELAELEEELAELAPLLR 509
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
846-1291 |
1.86e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQKTKERqqkaeneLKELEQKHSQLTEeknlLQEQLQAETELYAEAEEmrvrlaaKKQELEEILH 925
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEAEQ----LRQNLEKQQSSLAEAEQ-------RIKELEFEIQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 926 EMEARLEEEEDRGQQLQ--AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLE---DEILVMDDQNNKLSKE 1000
Cdd:pfam05557 181 SQEQDSEIVKNSKSELAriPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1001 RKLLEERISDLTTNLAEEEEKAKNLTKLKNK---HESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQ 1077
Cdd:pfam05557 261 LQSWVKLAQDTGLNLRSPEDLSRRIEQLQQReivLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1078 IAELKMQLA---KKEEELQAALARLDDEIAQKNNALKK---IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEAL 1151
Cdd:pfam05557 341 VRRLQRRVLlltKERDGYRAILESYDKELTMSNYSPQLlerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1152 KTELedTLDSTATQQELRAKREQEVTVLKKALDEetrsHEAQVQEMRQKhaqaVEELTEQLEQFK-RAKANLDKNKQTLE 1230
Cdd:pfam05557 421 EREL--QALRQQESLADPSYSKEEVDSLRRKLET----LELERQRLREQ----KNELEMELERRClQGDYDPKKTKVLHL 490
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1231 KENADLAGELR---VLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVES 1291
Cdd:pfam05557 491 SMNPAAEAYQQrknQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELES 554
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1766-1905 |
1.89e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1766 AEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSkFKSTIAALEAKIAQLEEQVEQEAREKqaatkslK 1845
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE-LEAELEEKDERIERLERELSEARSEE-------R 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1846 QKDKKLKEIllqvederkmaeqykeqaEKGNARVKQLKRQLEEAEEesqRINANRRKLQR 1905
Cdd:COG2433 459 REIRKDREI------------------SRLDREIERLERELEEERE---RIEELKRKLER 497
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1632-1922 |
2.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1632 QADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKE 1711
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1712 ELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELAterstAQKNESARQQLE 1791
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ-----ALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1792 RQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQ 1871
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1872 AEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVN 1922
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
978-1161 |
2.21e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.43 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 978 AKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKlknkhesmiselevRLKKEEKSRQELEKLK 1057
Cdd:pfam13851 26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRK--------------QLENYEKDKQSLKNLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1058 RKLEgdasDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDD---EIAQKnnALKKIRELEGHISDLQEDLDSERAAR 1134
Cdd:pfam13851 92 ARLK----VLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAaiqDVQQK--TGLKNLLLEKKLQALGETLEKKEAQL 165
|
170 180
....*....|....*....|....*..
gi 13124875 1135 NKAEKQKRDLGEELEALKTELEDTLDS 1161
Cdd:pfam13851 166 NEVLAAANLDPDALQAVTEKLEDVLES 192
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1555-1898 |
2.22e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 42.70 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1555 LQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQAD 1634
Cdd:COG0840 6 LLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1635 SAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELA 1714
Cdd:COG0840 86 LALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1715 EELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSN-ELATERSTAQKNESArqQLERQ 1793
Cdd:COG0840 166 LLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEgDLTVRIDVDSKDEIG--QLADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1794 NKELRSKLHEMEGAVKS---KFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKE 1870
Cdd:COG0840 244 FNRMIENLRELVGQVREsaeQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASE 323
|
330 340
....*....|....*....|....*...
gi 13124875 1871 QAEKGNARVKQLKRQLEEAEEESQRINA 1898
Cdd:COG0840 324 LAEEGGEVVEEAVEGIEEIRESVEETAE 351
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1383-1707 |
2.28e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.75 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1383 FASTVEALEEGKKR---FQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLdnqRQLVSNLEKKQRKFDQLLAE 1459
Cdd:pfam19220 36 IEAILRELPQAKSRlleLEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARL---AKLEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1460 EKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLvsskddvgknvHELEKSKRALET 1539
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERL-----------ALLEQENRRLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1540 QMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARdeqneekrrqlQRQLHEYETELEDERKQRALAAAAk 1619
Cdd:pfam19220 182 LSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAER-----------ERAEAQLEEAVEAHRAERASLRMK- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1620 kklegdLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIfatakenEKKAKSLEADLMQLQEDLAAA 1699
Cdd:pfam19220 250 ------LEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTL-------ERRLAGLEADLERRTQQFQEM 316
|
....*...
gi 13124875 1700 ERARKQAD 1707
Cdd:pfam19220 317 QRARAELE 324
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1256-1437 |
2.36e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.65 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1256 KLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVS 1335
Cdd:pfam17078 21 QLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1336 TKLRQLEEERNSLQDQ----LDEEMEAKQNLERHISTLNIQLSDSKKKLQDFastVEALEEGKKRFQKEIENLTQQYEEK 1411
Cdd:pfam17078 101 ASETTLEAELERLQIQydalVDSQNEYKDHYQQEINTLQESLEDLKLENEKQ---LENYQQRISSNDKDIDTKLDSYNNK 177
|
170 180
....*....|....*....|....*..
gi 13124875 1412 AAAYDKLEKTKN-RLQQELDDLVVDLD 1437
Cdd:pfam17078 178 FKNLDNIYVNKNnKLLTKLDSLAQLLD 204
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1545-1841 |
2.37e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1545 KTQLEELEDELQATEDAKLRLEVNMQALkgqfERDLQARdeqnEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEG 1624
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFEARQARL----EREKAAR----EARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1625 DLKDLELQADSAIKGREEAikqlRKLQAQmkdfqreledARASRDEifATAKENEKKAKsleadlmqlqedlAAAERARK 1704
Cdd:PRK05035 507 VIKAGARPDNSAVIAAREA----RKAQAR----------ARQAEKQ--AAAAADPKKAA-------------VAAAIARA 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1705 QADlekeeLAEELASSLSGRNALQDEKRRLEARIAQLEEeleeeqgnmeamsdrvRKATQQAEQLSNELATERSTAQKNE 1784
Cdd:PRK05035 558 KAK-----KAAQQAANAEAEEEVDPKKAAVAAAIARAKA----------------KKAAQQAASAEPEEQVAEVDPKKAA 616
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1785 ----SARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQL---EEQVEQEAREKQAAT 1841
Cdd:PRK05035 617 vaaaIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQqqaNAEPEEAEDPKKAAV 680
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1761-1928 |
2.53e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.97 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1761 KATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEgavKSKFKSTIAALEAKIAQLEEQVEQEAREKQAA 1840
Cdd:pfam15964 353 KALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKE---REELGATMLALSQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1841 TKSLKQKDKKLKEillQVEDERKMAEQYKEQaekgnarVKQLKRQLEEAEEESQRInanRRKLQRELDEATESNEAMGRE 1920
Cdd:pfam15964 430 VSQLEEAQKQLAS---QEMDVTKVCGEMRYQ-------LNQTKMKKDEAEKEHREY---RTKTGRQLEIKDQEIEKLGLE 496
|
....*...
gi 13124875 1921 VNALKSKL 1928
Cdd:pfam15964 497 LSESKQRL 504
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1806-1926 |
2.58e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.92 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1806 GAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQ 1885
Cdd:COG5283 6 GAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 13124875 1886 LEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKS 1926
Cdd:COG5283 86 QRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQR 126
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
965-1214 |
2.87e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 965 ARQKLQLEKVTAE-AKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTT-NLAEEEEKAknltkLKNKHEsmiselevR 1042
Cdd:COG0497 151 AGLEELLEEYREAyRAWRALKKELEELRADEAERARELDLLRFQLEELEAaALQPGEEEE-----LEEERR--------R 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1043 LKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELkmqlAKKEEELQAALARLDDEIAQKNNAlkkIRELEGHISD 1122
Cdd:COG0497 218 LSNAEKLREALQEALEALSGGEGGALDLLGQALRALERL----AEYDPSLAELAERLESALIELEEA---ASELRRYLDS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1123 LqeDLDSERAA-----RNKAEKQKRDLG---EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETrsheAQV 1194
Cdd:COG0497 291 L--EFDPERLEeveerLALLRRLARKYGvtvEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA----EKL 364
|
250 260
....*....|....*....|.
gi 13124875 1195 QEMRQKHAQAVEE-LTEQLEQ 1214
Cdd:COG0497 365 SAARKKAAKKLEKaVTAELAD 385
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1509-1656 |
2.95e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRL---EVNMQALKGQFE---RDLQA 1582
Cdd:pfam05667 340 LQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVE 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1583 RDEQNEEKRRQL---QRQLHEYETELEDERKQRALAAAAkkklegdLKDLELQADSAIKGREEAIKQlrkLQAQMKD 1656
Cdd:pfam05667 420 LAGQWEKHRVPLieeYRALKEAKSNKEDESQRKLEEIKE-------LREKIKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
977-1066 |
3.05e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 977 EAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKL 1056
Cdd:COG2433 419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
90
....*....|
gi 13124875 1057 KRKLEGDASD 1066
Cdd:COG2433 499 KELWKLEHSG 508
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1089-1857 |
3.50e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.43 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1089 EEELQAALARLDDEIAQKnnaLKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQEL 1168
Cdd:pfam07111 54 ELEGSQALSQQAELISRQ---LQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1169 RAKREQEVtvlKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKqtlekenadlAGELRVLGQAKQ 1248
Cdd:pfam07111 131 RKNLEEGS---QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKR----------AGEAKQLAEAQK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1249 EVEHKKKKLEAQVQELQSKCSDGERARAELNDKVhklQNEVESVTGMLNEAEgkAIKLAKDVASLSSQLQDTQELLQEET 1328
Cdd:pfam07111 198 EAELLRKQLSKTQEELEAQVTLVESLRKYVGEQV---PPEVHSQTWELERQE--LLDTMQHLQEDRADLQATVELLQVRV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1329 rQKLNVSTKLRQLEEERN-SLQDQLDEEMEAK-----QNLERHISTLNIQL-------SDSKKKLQDfasTVEALEEGKK 1395
Cdd:pfam07111 273 -QSLTHMLALQEEELTRKiQPSDSLEPEFPKKcrsllNRWREKVFALMVQLkaqdlehRDSVKQLRG---QVAELQEQVT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1396 RFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKkQRKFdqllaeeknISSKYADERDRAE 1475
Cdd:pfam07111 349 SQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEE-QLKF---------VVNAMSSTQIWLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1476 AeareketkalSLARALEEALEAKEELERTNKMLKA--EMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED 1553
Cdd:pfam07111 419 T----------TMTRVEQAVARIPSLSNRLSYAVRKvhTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1554 ElqatedaKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQralaaaakkklegdLKDLELQA 1633
Cdd:pfam07111 489 E-------RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQES--------------LASVGQQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1634 DSAIKGREEAIKQLRKLQAQMKDFQreledarasrdEIFATAkenekkaksleadlmqLQEDLAAAE-RARKQadlekee 1712
Cdd:pfam07111 548 EVARQGQQESTEEAASLRQELTQQQ-----------EIYGQA----------------LQEKVAEVEtRLREQ------- 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1713 laeelasslsgrnaLQDEKRRL-EARIAQLEEELEEEQGNmeamsdrvRKATQQAEQlSNELATERSTAQKNESAR---- 1787
Cdd:pfam07111 594 --------------LSDTKRRLnEARREQAKAVVSLRQIQ--------HRATQEKER-NQELRRLQDEARKEEGQRlarr 650
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13124875 1788 -QQLERQNKELRSKLHEMEGAVKSKFKSTIAAL----EAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQ 1857
Cdd:pfam07111 651 vQELERDKNLMLATLQQEGLLSRYKQQRLLAVLpsglDKKSVVSSPRPECSASAPIPAAVPTRESIKGSLTVLLD 725
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
865-1138 |
3.52e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 865 KERQQKAENELKELEQKHSQ---LTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQL 941
Cdd:pfam19220 114 RDKTAQAEALERQLAAETEQnraLEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAEL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 942 QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIkkledeilvmDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1021
Cdd:pfam19220 194 TRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQL----------EEAVEAHRAERASLRMKLEALTARAAATEQL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1022 AKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQ---LAKKEEELQAALAR 1098
Cdd:pfam19220 264 LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERaemLTKALAAKDAALER 343
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 13124875 1099 LDDEIA---QKNNALKKIRE-----LEGHISDLQEDLDSERAARNKAE 1138
Cdd:pfam19220 344 AEERIAslsDRIAELTKRFEveraaLEQANRRLKEELQRERAERALAQ 391
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1277-1484 |
3.63e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1277 ELNDKVHKLQNE-VESVTGMLNEAEGKAIKLAKDVASLSS--------QLQDTQELLQEETRQKLNVSTKLRQLEEERNS 1347
Cdd:PRK05771 32 HIEDLKEELSNErLRKLRSLLTKLSEALDKLRSYLPKLNPlreekkkvSVKSLEELIKDVEEELEKIEKEIKELEEEISE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1348 LQDQLDEemeakqnLERHISTL----NIQLSDSkkKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEK--- 1420
Cdd:PRK05771 112 LENEIKE-------LEQEIERLepwgNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1421 --TKNRLQQELDDLVVDLDNQR----------QLVSNLEKK----QRKFDQLLAEEKNISSKYAD-----------ERDR 1473
Cdd:PRK05771 183 vvVLKELSDEVEEELKKLGFERleleeegtpsELIREIKEEleeiEKERESLLEELKELAKKYLEellalyeyleiELER 262
|
250
....*....|.
gi 13124875 1474 AEAEAREKETK 1484
Cdd:PRK05771 263 AEALSKFLKTD 273
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
976-1259 |
3.63e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 976 AEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKaknLTKLKNKHEsmisELEVRLKKEEKSRQELEK 1055
Cdd:PTZ00440 1054 MKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNK---LIEIKNKSH----EHVVNADKEKNKQTEHYN 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1056 LKRKlegDASDFHEQIADLQAQIAELKMQLAKKEE----ELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSer 1131
Cdd:PTZ00440 1127 KKKK---SLEKIYKQMEKTLKELENMNLEDITLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQ-- 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1132 aARNKAEKQKRDLGEELE---------ALKTELEDTLDSTATQQEL--RAKREQEVTVLKKALDEETRSHEAQVQEMRQK 1200
Cdd:PTZ00440 1202 -VKKNMSKERNDHLTTFEynayydkatASYENIEELTTEAKGLKGEanRSTNVDELKEIKLQVFSYLQQVIKENNKMENA 1280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124875 1201 HAQaVEELTEQLEQFK--RAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEA 1259
Cdd:PTZ00440 1281 LHE-IKNMYEFLISIDseKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKE 1340
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1215-1687 |
3.64e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1215 FKRAKANLDKNKQTLEkenadlagELRVlgqaKQEVEHKKKKLEAQVQELQSkcSDGERARAELNDKVhklqnevesvtg 1294
Cdd:COG3096 231 FQDMEAALRENRMTLE--------AIRV----TQSDRDLFKHLITEATNYVA--ADYMRHANERRELS------------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1295 mlneaeGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLErhistlniqls 1374
Cdd:COG3096 285 ------ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE----------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1375 dskkKLQDFASTVEALEEgKKRFQKEI-ENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQ-------RQLVSNL 1446
Cdd:COG3096 348 ----KIERYQEDLEELTE-RLEEQEEVvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyQQAVQAL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1447 EKKQRkfdqlLAEEKNISSKYADERdRAEAEAREKE--TKALSLARALEEALEAKEELERTNKMLKAeMEDLVSSKD--D 1522
Cdd:COG3096 423 EKARA-----LCGLPDLTPENAEDY-LAAFRAKEQQatEEVLELEQKLSVADAARRQFEKAYELVCK-IAGEVERSQawQ 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1523 VGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvnmqALKGQFERDLQARDEQnEEKRRQLQRQLHEYE 1602
Cdd:COG3096 496 TARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEEL-EELLAELEAQLEELE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1603 TELEDERKQRALAAAAKKKLEGDLKDLELQA-------DSAIKGREEAIKQLRKLQAQMKDFQRELEDARA---SRDEIF 1672
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqDALERLREQSGEALADSQEVTAAMQQLLEREREatvERDELA 650
|
490
....*....|....*
gi 13124875 1673 ATAKENEKKAKSLEA 1687
Cdd:COG3096 651 ARKQALESQIERLSQ 665
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1318-1785 |
3.65e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.34 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1318 QDTQELLQEETRQKLNVSTKLR------------QLEEERnsLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAS 1385
Cdd:PTZ00108 900 EDYKEFLESETLKEKDVIVDYRdystantvhftvKLNDGV--LEQWEEEGIEKVFKLKSTISTTNMVLFDENGKIKKYSD 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1386 TVEALEEgkkrFqkeienltqqYEEKAAAYdklEKTKNRLQQELDDLVVDLDNQRQLV-----SNLEKKQRKFDQLLAE- 1459
Cdd:PTZ00108 978 ALDILKE----F----------YLVRLDLY---KKRKEYLLGKLERELARLSNKVRFIkhvinGELVITNAKKKDLVKEl 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1460 EKNISSKYADERDRAEAE--AREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLvsSKDDVGKNVHELEKSKRAL 1537
Cdd:PTZ00108 1041 KKLGYVRFKDIIKKKSEKitAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSL--TKEKVEKLNAELEKKEKEL 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1538 E----TQMEEM-KTQLEELEDELQATE--DAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERK 1610
Cdd:PTZ00108 1119 EklknTTPKDMwLEDLDKFEEALEEQEevEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNS 1198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1611 QRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKlqAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLM 1690
Cdd:PTZ00108 1199 KRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKK--SSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPK 1276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1691 QLQEDLAAAERARKQADlekeelAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLS 1770
Cdd:PTZ00108 1277 RVSAVQYSPPPPSKRPD------GESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSS 1350
|
490
....*....|....*
gi 13124875 1771 NELATERSTAQKNES 1785
Cdd:PTZ00108 1351 RLLRRPRKKKSDSSS 1365
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1473-1832 |
3.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1473 RAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKnvhELEKSKRALETQMEEMKTQlEELE 1552
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ---DYQAASDHLNLVQTALRQQ-EKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1553 DELQATEDAKLRLEVNMQALKGQFER--DLQARDEQNEEKRRQLQRQLHEYETELEDERK---QRALAAAAKKKLEGDLK 1627
Cdd:PRK04863 352 RYQADLEELEERLEEQNEVVEEADEQqeENEARAEAAEEEVDELKSQLADYQQALDVQQTraiQYQQAVQALERAKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1628 DLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARA-------------------SRDEIFATAKENEKKAKS---L 1685
Cdd:PRK04863 432 LPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkiagevSRSEAWDVARELLRRLREqrhL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1686 EADLMQLQEDLAAAERA-RKQADLEKEELAEELASSLSGRNA--LQDEKRRLEARI-------AQLEEELEEEQGNMEAM 1755
Cdd:PRK04863 512 AEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEdeLEQLQEELEARLeslsesvSEARERRMALRQQLEQL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1756 SDRVRKATQQA----------EQLSNELATERSTAQKNESARQQLERQNKELRSKLHEmegavkskfkstiaaLEAKIAQ 1825
Cdd:PRK04863 592 QARIQRLAARApawlaaqdalARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDE---------------LAARKQA 656
|
....*..
gi 13124875 1826 LEEQVEQ 1832
Cdd:PRK04863 657 LDEEIER 663
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1064-1277 |
3.93e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1064 ASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQK-- 1141
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQaa 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1142 --RDLGEELEAL-----KTELEDTLDSTATQQE---------LRAKREQEVTVLKKaldeeTRSH-EAQVQEMRQKHAQA 1204
Cdd:PRK11637 122 qeRLLAAQLDAAfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQ-----TREElAAQKAELEEKQSQQ 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 1205 VEELTEQLEQfkrakanldknKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGER---ARAE 1277
Cdd:PRK11637 197 KTLLYEQQAQ-----------QQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEReakARAE 261
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1016-1354 |
4.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1016 AEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAA 1095
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1096 LARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQE 1175
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1176 VTVLKKAL----DEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVE 1251
Cdd:COG4372 166 LAALEQELqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1252 HKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQK 1331
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|...
gi 13124875 1332 LNVSTKLRQLEEERNSLQDQLDE 1354
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLV 348
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1004-1136 |
4.02e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1004 LEERISDLTTNLAEEEEKAKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHE-------------- 1069
Cdd:PRK09039 58 LNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGragelaqeldsekq 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124875 1070 -------QIADLQAQIAELKMQLAKKEEELQAALARlddeiaqknnalkkIRELEGHISDLQEDLDSERAARNK 1136
Cdd:PRK09039 131 vsaralaQVELLNQQIAALRRQLAALEAALDASEKR--------------DRESQAKIADLGRRLNVALAQRVQ 190
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1192-1355 |
4.35e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1192 AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRvlgQAKQEVEHKKKKLEA-----QVQELQS 1266
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE---EVEARIKKYEEQLGNvrnnkEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1267 KCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEEtrqklnvstkLRQLEEERN 1346
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE----------LEELEAERE 166
|
....*....
gi 13124875 1347 SLQDQLDEE 1355
Cdd:COG1579 167 ELAAKIPPE 175
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1129-1362 |
4.45e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 42.15 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1129 SERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKR-EQEVTVLKKALdeetrsheaqvqemrQKHAQAVEE 1207
Cdd:pfam09726 356 TSSSSSKNSKKQKGPGGKSGARHKDPAENCIPNNQLSKPDALVRlEQDIKKLKAEL---------------QASRQTEQE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1208 LTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQE---------------------------VEHKKKKLE-- 1258
Cdd:pfam09726 421 LRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKdkqtvqqlekrlkaeqearasaekqlaEEKKRKKEEea 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1259 ------AQVQELQSKCSDG-ERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKL------AKDVASLSSQLQDTQEL-- 1323
Cdd:pfam09726 501 taaravALAAASRGECTESlKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELrkykesEKDTEVLMSALSAMQDKnq 580
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 13124875 1324 -----LQEETRQKLNVSTKL----RQLEEERNSLQDQLDEEMEAKQNL 1362
Cdd:pfam09726 581 hlensLSAETRIKLDLFSALgdakRQLEIAQGQIYQKDQEIKDLKQKI 628
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
980-1290 |
4.53e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 980 IKKLEDEILVMD-------DQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEvRLKKEEKSRQE 1052
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLE-KLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1053 LEK-LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEElQAALARLDDEIAQKNNALkkiRELEGHISDLQEDLdser 1131
Cdd:PLN02939 216 TEGlCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET-EERVFKLEKERSLLDASL---RELESKFIVAQEDV---- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1132 aarNKAEKQKRD-LGEELEalktELEDTLDSTATQQelrakrEQEVTVLKkaldeetrsheaQVQEMRQKhaqaVEELTE 1210
Cdd:PLN02939 288 ---SKLSPLQYDcWWEKVE----NLQDLLDRATNQV------EKAALVLD------------QNQDLRDK----VDKLEA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1211 QLEQfkrakANLDKnkqtLEKENADLagelrvlgqAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVE 1290
Cdd:PLN02939 339 SLKE-----ANVSK----FSSYKVEL---------LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
846-982 |
4.76e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 846 QVTRQEEEMQAKEDELQktkERQQKAENE-LKELEQKHSQLTEEKNLLQEQLQAETE---------LYAEAEEMRVRLAA 915
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQ---ERLKQLEKErLAAQEQKKQAEEAAKQAALKQKQAEEAaakaaaaakAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13124875 916 KKQELE-EILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQlEKVTAEAKIKK 982
Cdd:PRK09510 161 KKAAAEaKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-KKAAAEAKAAA 227
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1002-1152 |
4.87e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1002 KLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASD----FHEQIADLQAQ 1077
Cdd:smart00787 140 KLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTeldrAKEKLKKLLQE 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13124875 1078 IAELKMQLAKKEEELQAalarLDDEIAQKNNalkKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK 1152
Cdd:smart00787 220 IMIKVKKLEELEEELQE----LESKIEDLTN---KKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
971-1233 |
5.01e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 971 LEKVTAEAKIKKLEDEIlvmddqnnKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKkeeksr 1050
Cdd:PRK05771 59 LDKLRSYLPKLNPLREE--------KKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIE------ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1051 qELEKLKrKLEGDASDF-------------HEQIADLQAQIAELK----------------MQLAKKEEELQAALARLD- 1100
Cdd:PRK05771 125 -RLEPWG-NFDLDLSLLlgfkyvsvfvgtvPEDKLEELKLESDVEnveyistdkgyvyvvvVVLKELSDEVEEELKKLGf 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1101 --DEIAQKNNALKKIRELEGHISDLqedldseraarnkaEKQKRDLGEELEALKTELEDTLdsTATQQELRAKREQEVTV 1178
Cdd:PRK05771 203 erLELEEEGTPSELIREIKEELEEI--------------EKERESLLEELKELAKKYLEEL--LALYEYLEIELERAEAL 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 13124875 1179 LKKALDEETRSHEAQVQEMRqkhaqaVEELTEQLEQFKRAKANLDKNKQTLEKEN 1233
Cdd:PRK05771 267 SKFLKTDKTFAIEGWVPEDR------VKKLKELIDKATGGSAYVEFVEPDEEEEE 315
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1523-1688 |
5.34e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1523 VGKNVHELEKSKRALETQmEEMKTQLEELEDELQATEDAKLrLEVN--MQALKGQFERDLQARDEQNEEKRRQLQRQLHE 1600
Cdd:PRK12704 20 IGYFVRKKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1601 YETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRE--LEDARA-SRDEIFATAKE 1677
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKE 177
|
170
....*....|.
gi 13124875 1678 NEKKAKsLEAD 1688
Cdd:PRK12704 178 IEEEAK-EEAD 187
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1345-1585 |
5.39e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1345 RNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAST--VEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTK 1422
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1423 NRLQQELDDLVVDLDNQRQLVSNLEKKQRkFDQLLAEEKNISSKYADE-RDRAEAEAREKETKALslaraleealeakee 1501
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQ-LAELEAELAELSARYTPNhPDVIALRAQIAALRAQ--------------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1502 lertnkmLKAEMEDLVSSkddvgknvheLEKSKRALETQMEEMKTQLEELEDELQ---ATEDAKLRLEVNMQALKGQFER 1578
Cdd:COG3206 307 -------LQQEAQRILAS----------LEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYES 369
|
....*..
gi 13124875 1579 DLQARDE 1585
Cdd:COG3206 370 LLQRLEE 376
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1359-1679 |
5.66e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 41.68 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1359 KQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENltqqyEEKAAAYDKLEKTKNrlqqelddlvvdldn 1438
Cdd:pfam18971 558 RRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAE-----AKSTGNYDEVKKAQK--------------- 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1439 qrqlvsNLEKKQRKFDQLLAE-EKNISSKYADE-RDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDL 1516
Cdd:pfam18971 618 ------DLEKSLRKREHLEKEvEKKLESKSGNKnKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDK 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1517 VS--SKD--DVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvNMQALKGQFerdlqaRDEQNEEKRR 1592
Cdd:pfam18971 692 LEkiSKDlkDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVE-NLNAALNEF------KNGKNKDFSK 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1593 QLQRQlheyeTELEDERKQRALAAAAKkklegDLKDLELQADSAIKGREEaIKQLRKLQAQMKDFQRELEDARASRDEIF 1672
Cdd:pfam18971 765 VTQAK-----SDLENSVKDVIINQKVT-----DKVDNLNQAVSVAKAMGD-FSRVEQVLADLKNFSKEQLAQQAQKNEDF 833
|
....*..
gi 13124875 1673 ATAKENE 1679
Cdd:pfam18971 834 NTGKNSE 840
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1780-1905 |
5.72e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1780 AQKNESARQQLERQNKELRSKLHEMEGAVKSKFKstiaaleakiaQLEEQVEQEAREKQaatKSLKQKDKKLKEILLQVE 1859
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIH-----------KLRNEFEKELRERR---NELQKLEKRLLQKEENLD 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 13124875 1860 DERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRR-KLQR 1905
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqELER 146
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1257-1589 |
5.85e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1257 LEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVST 1336
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1337 KLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYD 1416
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1417 KLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADER----DRAEAEAREKETKALSLARAL 1492
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEleedKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1493 EEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL 1572
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330
....*....|....*..
gi 13124875 1573 KGQFERDLQARDEQNEE 1589
Cdd:COG4372 349 GLLDNDVLELLSKGAEA 365
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
849-952 |
6.35e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 849 RQEEEMQAkeDELQKTKERQQKAENELKELEQKH----SQLTEEKNLLQEQLQAETELYAEAEemrVRLAAKKQELEEIL 924
Cdd:pfam09787 53 RQERDLLR--EEIQKLRGQIQQLRTELQELEAQQqeeaESSREQLQELEEQLATERSARREAE---AELERLQEELRYLE 127
|
90 100
....*....|....*....|....*...
gi 13124875 925 HEMEARLEEEEDRGQQLQAERKKMAQQM 952
Cdd:pfam09787 128 EELRRSKATLQSRIKDREAEIEKLRNQL 155
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1023-1291 |
6.56e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 40.68 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1023 KNLTKLKNKHESMISELEVRLKKEEKSRQEL-EKLKRKLEGDASdfHEQIADLQAQIAELKmqlakkeeELQAALARLDD 1101
Cdd:pfam13949 27 DDLPKLKQRNREILDEAEKLLDEEESEDEQLrAKYGTRWTRPPS--SELTATLRAEIRKYR--------EILEQASESDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1102 EIAQK-NNALKKIRELEGHISDLQEDLDSERAARNKAEKQK-----RDLGEELEALKTELEDTLdstatqQELRAKREQ- 1174
Cdd:pfam13949 97 QVRSKfREHEEDLELLSGPDEDLEAFLPSSRRAKNSPSVEEqvaklRELLNKLNELKREREQLL------KDLKEKARNd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1175 ---EVTVLKKALDEETRSHEAQVQEMRQKHaqavEELTEQLEQFKRAKANLDKNkqtLEKENADLAGELRVLGQAKQEVE 1251
Cdd:pfam13949 171 disPKLLLEKARLIAPNQEEQLFEEELEKY----DPLQNRLEQNLHKQEELLKE---ITEANNEFLQDKRVDSEKQRQRE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 13124875 1252 HKKKKLEAQVQ---ELQSKCSDGERARAELNDKVHKLQNEVES 1291
Cdd:pfam13949 244 EALQKLENAYDkykELVSNLQEGLKFYNDLTEILEKLLKKVKD 286
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
856-1152 |
6.61e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 856 AKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEE 935
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 936 DRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNL 1015
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1016 AEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAA 1095
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 13124875 1096 LARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK 1152
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1415-1859 |
7.43e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.05 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1415 YDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEE 1494
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1495 ALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKG 1574
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1575 QFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQM 1654
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1655 KDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRL 1734
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1735 EARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKS 1814
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 13124875 1815 TIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVE 1859
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAAL 525
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1769-1925 |
7.92e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1769 LSNELAT-----ERSTAQKNESARQ-QLERQNKelrsklHEMEGAVkSKFKSTIAALEAKIAQLEEQVEQEAREKQAATK 1842
Cdd:PRK09039 44 LSREISGkdsalDRLNSQIAELADLlSLERQGN------QDLQDSV-ANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1843 SLKQKDKKLKEillqvedERKMAEQYKEQAEKGNARVKQLKRQL---EEAEEESQ-RINANRRKLQrelDEATESNEAMG 1918
Cdd:PRK09039 117 RAGELAQELDS-------EKQVSARALAQVELLNQQIAALRRQLaalEAALDASEkRDRESQAKIA---DLGRRLNVALA 186
|
....*..
gi 13124875 1919 REVNALK 1925
Cdd:PRK09039 187 QRVQELN 193
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1527-1924 |
8.57e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.78 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1527 VHELEKSKRAletqMEEMKTQLEELE-DELQATED---AKLRLEvNMQalKGQFERDLQARDEQNEEKRRQLQRQLHEYE 1602
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVE-EME--QGIADEASVAAKAQLEVAKARHAAAVAELK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1603 T---ELEDERKQRAlaaaakkklegdlkDLELQADSAIKGREEAI-------KQLRKLQAQMKDFQRELEDARASRDEI- 1671
Cdd:pfam05701 142 SvkeELESLRKEYA--------------SLVSERDIAIKRAEEAVsaskeieKTVEELTIELIATKESLESAHAAHLEAe 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1672 -----FATAKEN-----EKKAKSLEADLMQLQEDLAAAERARKQADLEkeelaeelaSSLsgrnaLQDEKRRLEARIAQL 1741
Cdd:pfam05701 208 ehrigAALAREQdklnwEKELKQAEEELQRLNQQLLSAKDLKSKLETA---------SAL-----LLDLKAELAAYMESK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1742 EEELEEEQGNMEAMSDRVRKATQQAEqlsNELATERSTAQKNESARQQLERQNKELRSKLhEMEGAVKSKFKSTIAALEA 1821
Cdd:pfam05701 274 LKEEADGEGNEKKTSTSIQAALASAK---KELEEVKANIEKAKDEVNCLRVAAASLRSEL-EKEKAELASLRQREGMASI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1822 KIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRR 1901
Cdd:pfam05701 350 AVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLE 429
|
410 420
....*....|....*....|...
gi 13124875 1902 KLQRELDEATESNEAMGREVNAL 1924
Cdd:pfam05701 430 AVLKEIEAAKASEKLALAAIKAL 452
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1820-1928 |
8.91e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1820 EAKIAQLEEQVEQEAREKQAATKSLKqkdkklKEILLQVEDE--RKMAEQYKEQAEKgNARVKQLKRQLEEAEEESQRIN 1897
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIK------KEALLEAKEEihKLRNEFEKELRER-RNELQKLEKRLLQKEENLDRKL 102
|
90 100 110
....*....|....*....|....*....|.
gi 13124875 1898 ANRRKLQRELDEATESNEAMGREVNALKSKL 1928
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEEL 133
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1635-1928 |
9.31e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1635 SAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAA--AERARKQADLEKEE 1712
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEkiAEYTKSIDIKKATE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1713 LAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQgnmEAMSDRVRKATQQAEQLSNELATERSTAQKNeSARQQLEr 1792
Cdd:COG5185 313 SLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQ---ESLTENLEAIKEEIENIVGEVELSKSSEELD-SFKDTIE- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1793 qnkELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQyKEQA 1872
Cdd:COG5185 388 ---STKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADE-ESQS 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 13124875 1873 EKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKL 1928
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKL 519
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1529-1900 |
9.35e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1529 ELEKSKRALETQMEEMKTQLEELEDELQATEDAklrlevnmQALKGQFERDLQARDEQNEEkRRQLQRQLHEYETELEDE 1608
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREA--------LQQTQQSHAYLTQKREAQEE-QLKKQQLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1609 RKQRALAAAAKKKLEGDLKDLELQADSaikgreEAIKQLRKlqaQMKDFQRELEDARASRDEIFATAKENEKKAKSLEAD 1688
Cdd:TIGR00618 273 RAQEAVLEETQERINRARKAAPLAAHI------KAVTQIEQ---QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1689 LMQLQEDLAAAERARKQADLEKeelaeelasslsGRNALQDEKRRLEARIAQLeeeleeeQGNMEAMSDRVRKATQQAEQ 1768
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVAT------------SIREISCQQHTLTQHIHTL-------QQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1769 LSNELATERSTAQKNESARQQLERQNKELRSKLhemegavksKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKD 1848
Cdd:TIGR00618 405 LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ---------RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1849 KKLKEILlqvederkmaEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANR 1900
Cdd:TIGR00618 476 QTKEQIH----------LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1509-1649 |
9.53e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1509 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFE-RDLQARDEQN 1587
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124875 1588 EEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRK 1649
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1752-1842 |
9.71e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 40.03 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124875 1752 MEAMSDRVRKATQQAEQLSNELATERSTAqKNESARQQLERQNKELRSKLHEMEGAVKSkfkSTIAALEAKIAQLEEQVE 1831
Cdd:COG4223 2 IAALEAAVAELPAQLTALEQRLAALEAAP-AAAAATAALEARLAALRAALAAAREAVAA---AAAAALEARLAALEAKAA 77
|
90
....*....|.
gi 13124875 1832 QEAREKQAATK 1842
Cdd:COG4223 78 APEAEAAAAAR 88
|
|
| |
