|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
115-792 |
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: 1339.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPasvstmsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLE 354
Cdd:cd14930 153 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 355 SLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 434
Cdd:cd14930 233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 435 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 514
Cdd:cd14930 313 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 515 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRD 594
Cdd:cd14930 393 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 595 QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTV 674
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 675 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 754
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*...
gi 1039779964 755 NAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14930 633 NAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
115-792 |
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: 1284.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPasvstmsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP--------GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETL 353
Cdd:cd14920 153 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQqDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 433
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 434 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 513
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 514 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLR 593
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 594 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMF 671
Cdd:cd14920 473 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgSAYKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 672 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 751
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1039779964 752 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14920 633 LTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
869-1949 |
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: 1283.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 869 TRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 948
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 949 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1028
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1029 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGR 1108
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1109 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1188
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1189 LRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSR 1268
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1269 QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEE 1348
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1349 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR 1428
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1429 LAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1508
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1509 LTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1588
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1589 TVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQL 1668
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1669 KKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAAT 1748
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1749 LEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAG 1828
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1829 ARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLE 1908
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1039779964 1909 EAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1949
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
115-792 |
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: 1275.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESG-------KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQ-ERELFQET 352
Cdd:cd01377 154 GSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVdDAEEFKLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd01377 234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 512
Cdd:cd01377 314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 513 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK-FQRPRN 591
Cdd:cd01377 393 HMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 592 LRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPRRGMF 671
Cdd:cd01377 471 KKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES---------GGGGGKKKKKGGSF 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 672 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 751
Cdd:cd01377 542 RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSI 621
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1039779964 752 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd01377 622 LAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
115-792 |
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: 1170.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPAsvstMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIA----LSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 353
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGqQDKELFAETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 433
Cdd:cd14932 237 EAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 434 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 513
Cdd:cd14932 317 AQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 514 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLR 593
Cdd:cd14932 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 594 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP-GGRPRRGMFR 672
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHgAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 673 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 752
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1039779964 753 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14932 637 TPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
115-792 |
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: 1138.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVPASVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 352
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 512
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 513 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPrNL 592
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 593 RDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQvSSLGDGPPGGRPRRGMFR 672
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 673 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 752
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1039779964 753 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14911 635 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
115-792 |
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: 1112.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstmsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG-----------ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETL 353
Cdd:cd14919 150 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 433
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 434 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 513
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 514 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLR 593
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 594 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP--GGRPRRGMF 671
Cdd:cd14919 470 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 672 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 751
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1039779964 752 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14919 630 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
115-792 |
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: 1099.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpASVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKD----QNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETL 353
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQdKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 433
Cdd:cd15896 237 EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 434 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 513
Cdd:cd15896 317 AQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 514 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLR 593
Cdd:cd15896 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 594 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRT 673
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 674 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 753
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670
....*....|....*....|....*....|....*....
gi 1039779964 754 PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd15896 637 PNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
115-792 |
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: 1095.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstmsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI--------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETL 353
Cdd:cd14921 153 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDdEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 433
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 434 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 513
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 514 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLR 593
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 594 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMF 671
Cdd:cd14921 473 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSlpSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 672 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 751
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1039779964 752 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14921 633 LAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
104-792 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1066.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 104 EDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ 183
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 184 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpasvstmsyGELERQLLQANPILEAFGNAKTVKNDNS 263
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV------------GRLEEQILQSNPILEAFGNAKTVRNNNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 264 SRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-P 342
Cdd:pfam00063 150 SRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTiD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 343 G-QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLT 421
Cdd:pfam00063 230 GiDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 422 PRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 501
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 502 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQG 581
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 582 SHPKFQRPRnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVssLGDGP 661
Cdd:pfam00063 467 KHPHFQKPR-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN--ESGKS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 662 PGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRIL 741
Cdd:pfam00063 544 TPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 742 FQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
96-804 |
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: 993.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 96 NPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTE 175
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 176 GAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstmsyGELERQLLQANPILEAFGNA 255
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV--------------GSVEDQILESNPILEAFGNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 256 KTVKNDNSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT 335
Cdd:smart00242 147 KTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 336 NGPSSS-PGQE-RELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNT-AAQKLCRLLGLGV 412
Cdd:smart00242 227 QGGCLTvDGIDdAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 413 TDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLN 492
Cdd:smart00242 307 EELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 493 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSF 572
Cdd:smart00242 386 SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 573 VEKVAQEQGSHPKFQRPRNlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgle 652
Cdd:smart00242 463 LEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS----- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 653 QVSSLGdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIC 732
Cdd:smart00242 537 NAGSKK-----------RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIR 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 733 RQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERD 804
Cdd:smart00242 606 RAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
94-1179 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 898.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 94 RMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAV 173
Cdd:COG5022 59 RIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 174 TEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvSTMSYGELERQLLQANPILEAFG 253
Cdd:COG5022 139 AEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSS-------------STVEISSIEKQILATNPILEAFG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 254 NAKTVKNDNSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRF 333
Cdd:COG5022 206 NAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 334 LTNGPSSSPGQ--ERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLG 411
Cdd:COG5022 286 LSQGGCDKIDGidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGID 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 412 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQL 491
Cdd:COG5022 365 PSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 492 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpANPPGLLALLDEECWFPKATDKS 571
Cdd:COG5022 444 NSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDES 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 572 FVEKVAQ--EQGSHPKFQRPRnLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIV 649
Cdd:COG5022 522 FTSKLAQrlNKNSNPKFKKSR-FRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 650 gleqvsslgdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGI 729
Cdd:COG5022 600 -----------------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETI 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 730 RICRQGFPNRILFQEFRQRYEILTPNA----IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDL 805
Cdd:COG5022 663 RISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDA 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 806 KVTDIIVSFQAAARGYLARRAFQRRQQQQSALRVMQRNCAAYLKLRNWQWWRLFIKVKPLLQVTRQDEVLQARAQELQKV 885
Cdd:COG5022 743 KLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL 822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 886 Q--ELQQQSAREvgelqgrvaQLEEERTRLAEQLRAEAelcSEAEEtrarlaARKQELELVVTELEARVGEEEECSRQLQ 963
Cdd:COG5022 823 QktIKREKKLRE---------TEEVEFSLKAEVLIQKF---GRSLK------AKKRFSLLKKETIYLQSAQRVELAERQL 884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 964 SEKKRLQQHIQELEShleaeegarQKLQLEKVTTEAKmKKFEEDLLL-LEDQNSKLSKERRLLEERlaEFSSQAAEEEEK 1042
Cdd:COG5022 885 QELKIDVKSISSLKL---------VNLELESEIIELK-KSLSSDLIEnLEFKTELIARLKKLLNNI--DLEEGPSIEYVK 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1043 VKSLNKLRL---KYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQK--QRAEELLAQLGRKEDELQAAL 1117
Cdd:COG5022 953 LPELNKLHEvesKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGalQESTKQLKELPVEVAELQSAS 1032
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1118 LRAEEEGGARAQlLKSLREAQAGLAEAQEDLEaervARAKAEKQRRDLGEELEALRGELEDT 1179
Cdd:COG5022 1033 KIISSESTELSI-LKPLQKLKGLLLLENNQLQ----ARYKALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
115-792 |
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: 836.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstmsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA---------SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-----PGQE-RE 347
Cdd:cd00124 152 FDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSgcdriDGVDdAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 348 LFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNT--DQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 425
Cdd:cd00124 232 EFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 426 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ-GASFLGILDIAGFEIFQLNSFEQLCINYTNE 504
Cdd:cd00124 312 VGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 505 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHP 584
Cdd:cd00124 392 KLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 585 KFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleqvsslgdgppgg 664
Cdd:cd00124 469 RFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ----------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 665 rprrgmfrtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 744
Cdd:cd00124 519 -------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDE 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039779964 745 FRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd00124 586 FLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
115-792 |
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: 775.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpASVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKA--QFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQET 352
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYdYHFCSQGVTTVDNmDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 511
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 512 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPR 590
Cdd:cd14927 397 HHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 591 ---NLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPR 667
Cdd:cd14927 474 pdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTEDPKSGVKEKRKK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 668 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 747
Cdd:cd14927 551 AASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039779964 748 RYEILTPNAIPK-GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14927 631 RYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
116-792 |
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: 752.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASS--PKGRKEpgvpasvSTMSyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKD-------SKMK-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQE 351
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVASiDDAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 352 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 430
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 431 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 509
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 510 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQR 588
Cdd:cd14913 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 589 PRNLRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRP 666
Cdd:cd14913 468 PKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT------ADADSGKKKVAKK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 667 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 746
Cdd:cd14913 542 KGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1039779964 747 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14913 622 QRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
115-792 |
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: 733.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpasvsTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEA--------AKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQET 352
Cdd:cd14909 153 GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNvDDGEEFSLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14909 233 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 512
Cdd:cd14909 313 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 513 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRN 591
Cdd:cd14909 392 HMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 592 LR---DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGDGPPGGRPRR 668
Cdd:cd14909 469 PKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-----QSGGGEQAKGGRGKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 669 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 748
Cdd:cd14909 544 GGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1039779964 749 YEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14909 624 YKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
115-792 |
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: 706.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvpasVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGK----------QSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQER-ELFQET 352
Cdd:cd14934 151 GTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPnPKEYHWVSQGVTVVDNMDDgEELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 512
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 513 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRN 591
Cdd:cd14934 390 HMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 592 LRD---QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgppggRPRR 668
Cdd:cd14934 467 GKGkgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK-----------QKRG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 669 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 748
Cdd:cd14934 536 SSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1039779964 749 YEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14934 616 YQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
116-792 |
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: 695.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvpasvSTMSygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSS------------SGET--QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELFQET 352
Cdd:cd01380 148 DKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPViDGvDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 511
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 512 HTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK--FQRP 589
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 590 RnlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqvsslgdgppggrprrg 669
Cdd:cd01380 464 R--FSNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK-------------------------------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 670 mfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 749
Cdd:cd01380 510 --KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRY 587
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1039779964 750 EILTPNAIPKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd01380 588 RVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
115-792 |
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: 692.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstmsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGA-----------LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 353
Cdd:cd14929 150 GARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESlDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 433
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 434 AQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 512
Cdd:cd14929 310 SQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 513 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRN 591
Cdd:cd14929 388 HMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 592 LRD--QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRrg 669
Cdd:cd14929 465 DKKkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYISTDSAIQFGEKKRKKGAS-- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 670 mFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 749
Cdd:cd14929 540 -FQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRY 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1039779964 750 EILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14929 619 CILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
116-792 |
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: 689.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASvstmsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 353
Cdd:cd14917 156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 511
Cdd:cd14917 315 KGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 512 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPR 590
Cdd:cd14917 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 591 NLRD--QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRR 668
Cdd:cd14917 470 NIKGkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAG------ADAPIEKGKGKAKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 669 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 748
Cdd:cd14917 544 SSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1039779964 749 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14917 624 YRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
116-792 |
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: 675.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVAS-SPKGRKEpgvpasVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKE------NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQET 352
Cdd:cd14916 156 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 431
Cdd:cd14916 236 DSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 432 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 510
Cdd:cd14916 315 TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 511 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRP 589
Cdd:cd14916 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 590 RNL--RDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRpr 667
Cdd:cd14916 470 RNVkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS-- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 668 rgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 747
Cdd:cd14916 548 ---FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039779964 748 RYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14916 625 RYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
117-792 |
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: 669.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 117 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 196
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 197 GAGKTENTKKVIQYLAHVASSPKGRKEPgvpasvSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI 276
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEE------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 277 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLE 354
Cdd:cd14918 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 355 SLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 433
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 434 AQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 512
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 513 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRN 591
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 592 LRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegiVGLEQVSSlgdGPPGGRPRRG 669
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY---ASAEADSG---AKKGAKKKGS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 670 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 749
Cdd:cd14918 545 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRY 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1039779964 750 EILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14918 625 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
116-792 |
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: 665.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStmsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETL 353
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14912 238 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 511
Cdd:cd14912 317 KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 512 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPR 590
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 591 NLRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRR 668
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---SGAQTAEGASAGGGAKKGGKKKG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 669 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 748
Cdd:cd14912 549 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1039779964 749 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14912 629 YKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
116-792 |
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: 661.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStmsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 353
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14910 238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 511
Cdd:cd14910 317 KGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 512 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPR 590
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 591 NLRD--QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEqvSSLGDGPPGGRPRR 668
Cdd:cd14910 472 PAKGkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF---SGAAAAE--AEEGGGKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 669 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 748
Cdd:cd14910 547 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1039779964 749 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14910 627 YKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
116-792 |
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: 658.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSPKGRKEpgvpASVSTMSyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKE----QQPGKMQ-GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------EREL 348
Cdd:cd14923 157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDF----PFVSQGEvtvasidDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 349 FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVG 427
Cdd:cd14923 232 LLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 428 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKL 506
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 507 QQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPK 585
Cdd:cd14923 389 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 586 FQRPRNLRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivglEQVSSLGDGPPG 663
Cdd:cd14923 466 FQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG----AEAGDSGGSKKG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 664 GRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 743
Cdd:cd14923 542 GKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYA 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1039779964 744 EFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14923 622 DFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
116-792 |
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: 656.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStmsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 353
Cdd:cd14915 158 ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYdFAFVSQGEITVPSiDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 511
Cdd:cd14915 317 KGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 512 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPR 590
Cdd:cd14915 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 591 NLRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGDGPPGGRPRR 668
Cdd:cd14915 472 PAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-----GQTAEAEGGGGKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 669 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 748
Cdd:cd14915 547 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1039779964 749 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14915 627 YKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
116-792 |
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: 632.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGG-------------SESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETL 353
Cdd:cd01378 149 FKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGiDDAADFKEVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---RDY 430
Cdd:cd01378 229 NAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 431 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 510
Cdd:cd01378 308 YEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 511 nhTMFVL--EQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFVEKVAQEQGSHPKFQ 587
Cdd:cd01378 388 --IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 588 RPRNLRD--QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSlgdgppggr 665
Cdd:cd01378 463 CPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE-----GVDLDSK--------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 666 prrGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 745
Cdd:cd01378 529 ---KRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKF 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1039779964 746 RQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd01378 606 LERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
116-792 |
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: 630.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpasvstmsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-----------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGE--QLKADLLLEPCSHYRFLT-NGPSSSPG-QERELFQE 351
Cdd:cd14883 145 ASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNiNDKKDFDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 352 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKK-ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 430
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 431 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRsPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 510
Cdd:cd14883 305 TEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNP-GQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 511 NHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPR 590
Cdd:cd14883 384 NHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 591 NLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQVSSLGDGPPGGRPRRGM 670
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSRGTSKG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 671 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 750
Cdd:cd14883 540 KPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1039779964 751 ILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14883 620 CLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
116-792 |
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: 621.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRgkKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvstmsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-----------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETL 353
Cdd:cd01383 143 AAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNClTIDGvDDAKKFHELK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 433
Cdd:cd01383 223 EALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 434 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 513
Cdd:cd01383 303 KLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 514 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLR 593
Cdd:cd01383 383 LFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 594 dqadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivGLEQVSSLGDGPPGGRPRRGMFRT 673
Cdd:cd01383 460 ----FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFAS------KMLDASRKALPLTKASGSDSQKQS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 674 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 753
Cdd:cd01383 530 VATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLL 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 1039779964 754 PNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd01383 610 PEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
115-792 |
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: 591.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVAsspkGRKepgvpasvstmSYgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----GQH-----------SW--IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQET 352
Cdd:cd01381 144 NKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRdDAAEFADI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKK--ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 430
Cdd:cd01381 224 RSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGET 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 431 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS--FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 508
Cdd:cd01381 304 VVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 509 LFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQ 587
Cdd:cd01381 384 FFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 588 RPRNlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPr 667
Cdd:cd01381 460 KPKS-DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------GSETRKKSP- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 668 rgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 747
Cdd:cd01381 529 -----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVE 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1039779964 748 RYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd01381 604 RYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
115-792 |
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: 589.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAHVAsspkGRKEPGVpASVstmsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEG-RSV--------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQE 351
Cdd:cd01384 148 FDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDgvDDAEEYRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 352 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTpRIKVGR 428
Cdd:cd01384 228 TRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 429 D-YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQ 507
Cdd:cd01384 307 DgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 508 QLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQ 587
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 588 RPRnlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSLGDGPPGGRPR 667
Cdd:cd01384 463 KPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPF----------------VAGLFPPLPREGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 668 RGM-FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 746
Cdd:cd01384 525 SSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039779964 747 QRYEILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 792
Cdd:cd01384 605 DRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
115-792 |
1.01e-179 |
|
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: 560.33 E-value: 1.01e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstmSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGS----------------GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPcshyrfLTNGPSSspgqerelFQETL 353
Cdd:cd01382 145 FNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP------LLDDVGD--------FIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 354 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQA-TMPDNTAAQKL---CRLLGLGVTDF-----SRALLTPRI 424
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 425 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSprqgASFLGILDIAGFEIFQLNSFEQLCINYT 502
Cdd:cd01382 291 GAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETS----SYFIGVLDIAGFEYFEVNSFEQFCINYC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 503 NEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGS 582
Cdd:cd01382 367 NEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 583 HPKFQRPR--------NLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegIVGLEQV 654
Cdd:cd01382 444 HFRLSIPRksklkihrNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKF----------IRSLFES 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 655 SSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd01382 514 STNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQG 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 735 GFPNRILFQEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd01382 594 GFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
115-792 |
3.34e-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: 556.70 E-value: 3.34e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ----DREDQS 189
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 190 ILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTMS--YGELERQLLQANPILEAFGNAKTVKNDNSSRFG 267
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 268 KFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-R 346
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDdA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 347 ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmpDNTAAQKL---CRLLGLGVTDFSRALLTPR 423
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLklaAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 424 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 503
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 504 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIE-RPANPPGLLALLDEeCWFPKAT--DKSFV------- 573
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLDD-CWRFKGEeaNKKFVsqlhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 574 ------EKVAQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdveg 647
Cdd:cd14890 476 grksgsGGTRRGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 648 ivGLEQVSslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 727
Cdd:cd14890 543 --SIREVS------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 728 GIRICRQGFPNRILFQEFRQRYEILTPNAipkgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14890 603 AIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
115-792 |
1.69e-171 |
|
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: 538.21 E-value: 1.69e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvstmsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAgeqlkadlllEPCSHYRFLTNGPSSSPGQEREL------ 348
Cdd:cd14872 144 DNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP----------DPASRGGWGSSAAYGYLSLSGCIevegvd 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 349 ----FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCR---LLGLGVTDFSRALLT 421
Cdd:cd14872 214 dvadFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 422 PRIKV-GRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCIN 500
Cdd:cd14872 294 RLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCIN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 501 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQ 580
Cdd:cd14872 374 FTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 581 GSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvsslgdg 660
Cdd:cd14872 451 AAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 661 ppggrPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 740
Cdd:cd14872 518 -----DQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRY 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1039779964 741 LFQEFRQRYEILtPNAIPKGFM-DGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14872 593 SHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
116-792 |
6.59e-166 |
|
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: 522.22 E-value: 6.59e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVASSPkgrkepgvpasvstmsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKAN----------------NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPSSSPGQE-----RELF 349
Cdd:cd01379 146 STGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVnnsgnREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 350 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL----KKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 425
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 426 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 503
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 504 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCID-LIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGS 582
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 583 HPkFQRPRnlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgpp 662
Cdd:cd01379 462 KY-YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ---------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 663 ggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 742
Cdd:cd01379 517 ----------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILF 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1039779964 743 QEFRQRYEILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKIFFR 792
Cdd:cd01379 587 ADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
115-792 |
2.61e-163 |
|
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: 515.39 E-value: 2.61e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKK-RHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstmsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD----------------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-------- 345
Cdd:cd14897 145 FTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdseeleyy 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 346 RELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 425
Cdd:cd14897 225 RQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 426 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 501
Cdd:cd14897 305 IRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 502 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQG 581
Cdd:cd14897 385 SNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 582 SHPKFQRPrnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslgdgp 661
Cdd:cd14897 462 ESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT------------------ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 662 pggrprrgmfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRIL 741
Cdd:cd14897 522 --------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIK 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 742 FQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 792
Cdd:cd14897 588 YEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
115-792 |
1.19e-162 |
|
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: 514.30 E-value: 1.19e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvPASVStmsygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVT--------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DiAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS-SPGQ-ERELFQET 352
Cdd:cd01387 145 E-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCeIAGKsDADDFRRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD-QATMPDNTAA--QKLCRLLGLGVTDFSRALLTPRIKVGRD 429
Cdd:cd01387 224 LAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAeiQWVAHLLQISPEGLQKALTFKVTETRRE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 430 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNrALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 509
Cdd:cd01387 304 RIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 510 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRP 589
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAFA-DNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 590 RnlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGiVGLEQVSSLGDGPPGGRPRRG 669
Cdd:cd01387 460 R--MPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRA-QTDKAPPRLGKGRFVTMKPRT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 670 mfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 749
Cdd:cd01387 537 --PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRY 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1039779964 750 EILTPNAIPKGfMDGKQACEKMIQALELDP-NLYRVGQSKIFFR 792
Cdd:cd01387 615 RCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
115-792 |
1.23e-161 |
|
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: 511.63 E-value: 1.23e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAHVASspkgrkepGVPASVStmsygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--------GLNDSTI--------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLggAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQE 351
Cdd:cd14903 145 FDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGmSDRKHFAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 352 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATM--PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 429
Cdd:cd14903 223 TKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 430 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 509
Cdd:cd14903 303 VYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 510 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAqeqGSHPKFQR- 588
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDv 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 589 ---PRNLRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGR 665
Cdd:cd14903 455 iefPRTSRTQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 666 PRRGMfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 745
Cdd:cd14903 533 GALTT-TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEF 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1039779964 746 RQRYEILTPNAiPKGFMDGKQACEKMIQALELD-PNLYRVGQSKIFFR 792
Cdd:cd14903 612 LDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
115-790 |
3.75e-160 |
|
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: 507.40 E-value: 3.75e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY------RGKKRHEVPPHVYAVTEGAYRSMLQDRE-- 186
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 187 --DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvSTMSYGELERQLLQANPILEAFGNAKTVKNDNSS 264
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQ--------NATERENVRDRVLESNPILEAFGNARTNRNNNSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 265 RFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngpSSSPGQ 344
Cdd:cd14901 153 RFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----NSSQCY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 345 ER-------ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNI-VLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFS 416
Cdd:cd14901 229 DRrdgvddsVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLcFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 417 RALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS-FLGILDIAGFEIFQLNSFE 495
Cdd:cd14901 309 KTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 496 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEK 575
Cdd:cd14901 389 QLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 576 VAQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVS 655
Cdd:cd14901 466 YYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF----------------LS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 656 SlgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQG 735
Cdd:cd14901 530 S----------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 736 FPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQA------LELDPNLYrVGQSKIF 790
Cdd:cd14901 594 YPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
115-792 |
2.17e-158 |
|
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: 503.83 E-value: 2.17e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLahVASSPKGrkepgvpasvstmsYGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG--------------YGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGQERELFQE 351
Cdd:cd01385 145 YRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCYTLEGEDEKYEFER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 352 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKER-NTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLTPRIKVGRD 429
Cdd:cd01385 225 LKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 430 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEK 505
Cdd:cd01385 305 TLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEH 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 506 LQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK 585
Cdd:cd01385 384 LQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 586 FQRPRnLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQVSSL-------- 657
Cdd:cd01385 461 YEKPQ-VMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF-------VRELIGIDPVAVFrwavlraf 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 658 ----------GDGPPGGRPRRGMFR------------------TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAG 709
Cdd:cd01385 532 framaafreaGRRRAQRTAGHSLTLhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPL 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 710 KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKI 789
Cdd:cd01385 612 RFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKV 687
|
...
gi 1039779964 790 FFR 792
Cdd:cd01385 688 FLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
115-754 |
1.19e-156 |
|
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: 498.45 E-value: 1.19e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvSTmsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKR--------SL-----VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDI---------AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQL----------------------LGGAGEQLKAD 322
Cdd:cd14888 147 FSKlkskrmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntglsyeendeklaKGADAKPISID 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 323 LLL-EPCSHYRFLT-NGPSSSPG-QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNT 399
Cdd:cd14888 227 MSSfEPHLKFRYLTkSSCHELPDvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSAS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 400 AAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS 476
Cdd:cd14888 307 CTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 477 FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLA 556
Cdd:cd14888 387 FCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 557 LLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlrDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDR 636
Cdd:cd14888 464 MLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 637 LTAEIWKdvegivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 716
Cdd:cd14888 542 FISNLFS------------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISV 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 1039779964 717 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 754
Cdd:cd14888 610 NEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
115-792 |
2.00e-156 |
|
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: 497.01 E-value: 2.00e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVstmsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCV--------EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQE 351
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTiSDQESFRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 352 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIvlkKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 431
Cdd:cd14873 233 VITAMEVMQFSKEEVREVSRLLAGILHLGNI---EFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 432 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 511
Cdd:cd14873 310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 512 HTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRN 591
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 592 LRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRRGMF 671
Cdd:cd14873 464 AVNN--FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRR 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 672 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 751
Cdd:cd14873 533 PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKV 612
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1039779964 752 LTPNAIPKGFMDGKqaCEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14873 613 LMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
115-792 |
3.68e-155 |
|
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: 493.89 E-value: 3.68e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEV---PPHVYAVTEGAYRSMLQDR----ED 187
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 188 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTmsygELERQLLQANPILEAFGNAKTVKNDNSSRFG 267
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHE----SIEECVLLSNLILEAFGNAKTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 268 KFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PGQER 346
Cdd:cd14892 157 KYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEvDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 347 EL-FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNivLKKERNTDQATMP----DNTAAQKLCRLLGLGVTDFSRALLT 421
Cdd:cd14892 237 ATeFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVFaqsaDGVNVAKAAGLLGVDAAELMFKLVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 422 PRIKVGRDYV-QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ---------GASFLGILDIAGFEIFQL 491
Cdd:cd14892 315 QTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 492 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFP-KATDK 570
Cdd:cd14892 395 NSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 571 SFVEKVAQEQ-GSHPKFQRPRNLRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegiv 649
Cdd:cd14892 472 QLLTIYHQTHlDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 650 gleqvsslgdgppggrprrgmFRTvgqlykeSLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGI 729
Cdd:cd14892 536 ---------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 730 RICRQGFPNRILFQEFRQRYEILTPN-AIPKGFMDGKQACEKM-----IQALELDPNLYRVGQSKIFFR 792
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
115-792 |
5.17e-149 |
|
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: 477.22 E-value: 5.17e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH--------EVPPHVYAVTEGAYRSMLQDR 185
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 186 EDQSILCTGESGAGKTENTKKVIQYL------AHVASSPKGRKEPGVPASVSTMSygeLERQLLQANPILEAFGNAKTVK 259
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqEQNSEEVLTLTSSIRATSKSTKS---IEQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 260 NDNSSRFGKFIRINFDI-AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYRFLTNG 337
Cdd:cd14907 158 NDNSSRFGKYVSILVDKkKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 338 PSSSPGQER----ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLK-KERNTDQATMPDNTAA-QKLCRLLGLG 411
Cdd:cd14907 238 KSNCYEVDTindeKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 412 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL------DRSPRQGASF-LGILDIA 484
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 485 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTF--LDFgLDLQPCIDLIERPanPPGLLALLDEEC 562
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKP--PIGIFNLLDDSC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 563 WFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIW 642
Cdd:cd14907 475 KLATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 643 KDVEGivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRC 722
Cdd:cd14907 554 SGEDG--------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 723 NGVLEGIRICRQGFPNRILFQEFRQRYEILTPNaipkgfmdgkqacekmiqaleldpnlYRVGQSKIFFR 792
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN--------------------------VLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
117-792 |
5.16e-141 |
|
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: 454.75 E-value: 5.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 117 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSML----QDREDQSILC 192
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 193 TGESGAGKTENTKKVIQYLAHVAsspKGRKEpgvpasvstmsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 272
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQ--------------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 273 NFDiAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPcSHYRFLTN--GPSSSPGQERELF 349
Cdd:cd14889 146 RFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNgaGCKREVQYWKKKY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 350 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLK-KERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGR 428
Cdd:cd14889 224 DEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEmDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 429 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASF----LGILDIAGFEIFQLNSFEQLCINYTNE 504
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVelreIGILDIFGFENFAVNRFEQACINLANE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 505 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHP 584
Cdd:cd14889 382 QLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 585 KFQRPRNlrDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG 664
Cdd:cd14889 459 YYGKSRS--KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 665 RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 744
Cdd:cd14889 537 NFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAE 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1039779964 745 FRQRYEIL--TPNaIPKgfmdGKQACEKMIQALELDPnlYRVGQSKIFFR 792
Cdd:cd14889 617 FAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
116-752 |
5.58e-138 |
|
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: 445.13 E-value: 5.58e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMY-----------RGKKRHEVPPHVYAVTEGAYRSM-- 181
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 182 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgVPASVSTMSYGE-LERQLLQANPILEAFGNAKTV 258
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNN-------LAASVSMGKSTSgIAAKVLQTNILLESFGNARTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 259 KNDNSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKAdlllepcshyrfltngp 338
Cdd:cd14900 155 RNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK----------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 339 ssspgqeRELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD-QATMPDNTAAQKL------CRLLGLG 411
Cdd:cd14900 218 -------RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 412 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGAS-FLGILDIAGFE 487
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 488 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKA 567
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 568 TDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDplndnvaaLLHQstdrltaeiwkdveg 647
Cdd:cd14900 448 SDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQ--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 648 ivglEQVSslgdgppggrprrgMFRTVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 727
Cdd:cd14900 505 ----EAVD--------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660
....*....|....*....|....*
gi 1039779964 728 GIRICRQGFPNRILFQEFRQRYEIL 752
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
115-792 |
8.84e-135 |
|
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: 437.07 E-value: 8.84e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAHVASspkGRKEPGVPasvstmsygelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS--PG-QERELFQ 350
Cdd:cd14904 145 FDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqiPGlDDAKLFA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 351 ETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLkKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 430
Cdd:cd14904 225 STQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 431 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 510
Cdd:cd14904 304 VTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 511 NHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKV---AQEQGSHPKFQ 587
Cdd:cd14904 384 TTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESID 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 588 RPRNLRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgLEQVSSLGDGPPGGRPR 667
Cdd:cd14904 460 FPKVKRTQ--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSGKGTKAP 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 668 rgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 747
Cdd:cd14904 534 ----KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELAT 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1039779964 748 RYEILTPNAIPKGfmDGKQACEKMIQAL-ELDPNLYRVGQSKIFFR 792
Cdd:cd14904 610 RYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
115-792 |
1.06e-132 |
|
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: 431.00 E-value: 1.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKQLPiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE---D 187
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 188 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTMSYG--ELERQLLQANPILEAFGNAKTVKNDNSSR 265
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 266 FGKFIRINFDIAGY-IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSSPG 343
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 344 -QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKK----ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRA 418
Cdd:cd14891 236 iDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 419 LLTPRIkVGRDYVQKAQ-TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRqGASFLGILDIAGFEIFQL-NSFEQ 496
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-PLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 497 LCINYTNEKLQQLFNHTMFVLEQEEYQREGIpwtflDFGLDLQP----CIDLIErpANPPGLLALLDEECWFPKATDKSF 572
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGI-----DVGVITWPdnreCLDLIA--SKPNGILPLLDNEARNPNPSDAKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 573 VEKVAQEQGSHPKFQRP--RNLRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQStdrltaeiwkdvegivg 650
Cdd:cd14891 467 NETLHKTHKRHPCFPRPhpKDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 651 leqvsslgdgppggrprrgmfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIR 730
Cdd:cd14891 528 -------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCE 582
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779964 731 ICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQA-CEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14891 583 VLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
115-754 |
3.26e-128 |
|
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: 420.84 E-value: 3.26e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYR--------GKKRHEVPPHVYAVTEGAYRSMLQ-D 184
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 185 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASvstmsygELERQLLQANPILEAFGNAKTVKNDNSS 264
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV-------EIGKRILQTNPILESFGNAQTIRNDNSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 265 RFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG 343
Cdd:cd14902 154 RFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnSYGPSFARK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 344 QER-----ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDF 415
Cdd:cd14902 234 RAVadkyaQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 416 SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--------RSPRQGASFLGILDIAGFE 487
Cdd:cd14902 314 ETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 488 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKA 567
Cdd:cd14902 394 SLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 568 TDKSFVEKVAQEQGShpkfqrprnlRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEG 647
Cdd:cd14902 471 SNQALSTKFYRYHGG----------LGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEV-------VVA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 648 IVGLEQVSSLG-DGPPGGRPRRGMFRT--VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 724
Cdd:cd14902 532 IGADENRDSPGaDNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611
|
650 660 670
....*....|....*....|....*....|
gi 1039779964 725 VLEGIRICRQGFPNRILFQEFRQRYEILTP 754
Cdd:cd14902 612 VLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
115-792 |
4.92e-127 |
|
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: 414.95 E-value: 4.92e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvstmsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR----------------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DiAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQET 352
Cdd:cd14896 145 Q-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACrlQGKEDAQDFEGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQ--ATMPDNTAAQKLCRLLGLGvTDFSRALLTPRIKV-GRD 429
Cdd:cd14896 224 LKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 430 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdRSPRQGASF--LGILDIAGFEIFQLNSFEQLCINYTNEKLQ 507
Cdd:cd14896 303 RVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWL-APPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 508 QLFNHTMFVLEQEEYQREGIPWTFLDfGLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQ 587
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 588 RPRNlrDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrpr 667
Cdd:cd14896 459 KPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 668 rgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 747
Cdd:cd14896 526 -----TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLA 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1039779964 748 RYEILTpNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14896 601 RFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
115-792 |
2.64e-126 |
|
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: 414.31 E-value: 2.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR--GKKRHE-------VPPHVYAVTEGAYRSMLQD- 184
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 185 REDQSILCTGESGAGKTENTKKVIQYLAHVasspkGRKEPGVPASVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSS 264
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTL-----GNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 265 RFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKA--------DLLLEPCSHYRFLTN 336
Cdd:cd14908 156 RFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 337 G--PSSSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQK----LCRLLGL 410
Cdd:cd14908 236 GgaPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 411 GVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIF 489
Cdd:cd14908 315 DVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 490 QLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFP-KAT 568
Cdd:cd14908 395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 569 DKSFVEKV--------AQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLM-KNMDPLNdnvaallhqstdrLTA 639
Cdd:cd14908 472 DANYASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------LTA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 640 EIwkdvegivgleqvsslgdgppggrprrgMFRTvGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQ 719
Cdd:cd14908 539 DS----------------------------LFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQ 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 720 LRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPnAIPKGFM-------DGKQACEKMI----------QALELDPNL- 781
Cdd:cd14908 590 LRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVKKMckdlvkgvlsPAMVSMKNIp 668
|
730
....*....|....
gi 1039779964 782 ---YRVGQSKIFFR 792
Cdd:cd14908 669 edtMQLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
113-803 |
6.42e-125 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 414.81 E-value: 6.42e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 113 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHE-VPPHVYAVTEGAYRSMLQDREDQSIL 191
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 192 CTGESGAGKTENTKKVIQYLAhvaSSPKGrkepgvpasvsTMSyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 271
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSG-----------NMD-LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 272 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQ 350
Cdd:PTZ00014 253 LQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGiDDVKDFE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 351 ETLESLRVLGLLPEEITAMLRTVSAVLQFGNI-VLKKERN--TDQAT-MPDNTAA-QKLCRLLGLGVTDFSRALLTPRIK 425
Cdd:PTZ00014 333 EVMESFDSMGLSESQIEDIFSILSGVLLLGNVeIEGKEEGglTDAAAiSDESLEVfNEACELLFLDYESLKKELTVKVTY 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 426 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNE 504
Cdd:PTZ00014 413 AGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 505 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHP 584
Cdd:PTZ00014 491 MLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNP 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 585 KFQRPRNLRDQaDFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE---GIVGLEQVsslgdgp 661
Cdd:PTZ00014 568 KYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEvekGKLAKGQL------- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 662 pggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRIL 741
Cdd:PTZ00014 640 ------------IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRT 707
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 742 FQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR---AGVLAQLEEER 803
Cdd:PTZ00014 708 FAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREK 772
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
115-788 |
2.05e-122 |
|
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: 404.36 E-value: 2.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDREDQSILC 192
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 193 TGESGAGKTENTKKVIQYLAHVASSPKGRKepgvpaSVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 272
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQN------NNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 273 NFDIAGYIV-GANIETYLLEKSR-AIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFL-------------TN 336
Cdd:cd14906 155 EFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 337 GPSSSPGQEREL---FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQAT--MPDNTAA-QKLCRLLGL 410
Cdd:cd14906 235 NKNSNHNNKTESiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 411 GVTDFSRALLTPRIKV-GRDYVQ-KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR----------SPRQGASFL 478
Cdd:cd14906 315 IESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 479 GILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALL 558
Cdd:cd14906 395 GVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 559 DEECWFPKATDKSFVEKVAQEQGSHPKFQRpRNLrDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLt 638
Cdd:cd14906 472 DDECIMPKGSEQSLLEKYNKQYHNTNQYYQ-RTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 639 aeiwkdvegIVGLEQVSSLGDGPPGGRPRRGMfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 718
Cdd:cd14906 549 ---------KKSLFQQQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLS 617
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 719 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSK 788
Cdd:cd14906 618 QLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
115-790 |
1.94e-121 |
|
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: 398.98 E-value: 1.94e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAhvasspkgrkepgvpASVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---------------SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 352
Cdd:cd14876 146 VASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGiDDVADFEEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGN--IVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTPRIKVG 427
Cdd:cd14876 226 LESLKSMGLTEEQIDTVFSIVSGVLLLGNvkITGKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKRELTVKVTKAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 428 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKL 506
Cdd:cd14876 306 GQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEML 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 507 QQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKF 586
Cdd:cd14876 384 QKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 587 QRPRNLRDQaDFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppggrp 666
Cdd:cd14876 461 KPAKVDSNI-NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSL--------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 667 rrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 746
Cdd:cd14876 531 -------IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1039779964 747 QRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIF 790
Cdd:cd14876 604 YQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
116-753 |
8.94e-119 |
|
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: 393.55 E-value: 8.94e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPiyteaivEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQ----- 183
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 184 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGrkepGVPASVSTMSYGElerQLLQANPILEAFGNAKTVKND 261
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTA----TSSSKRRRAISGS---ELLSANPILESFGNARTLRND 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 262 NSSRFGKFIRINF-----DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFL 334
Cdd:cd14895 148 NSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 335 TNG---PSSSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD---------------QATMP 396
Cdd:cd14895 228 SGGqcyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 397 DNTAAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR---- 469
Cdd:cd14895 308 SLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 470 -SPRQGAS-----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCID 543
Cdd:cd14895 388 lNPNKAANkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 544 LIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQAD--FSVLHYAGKVDYKASEWLMKNMDP 621
Cdd:cd14895 467 MLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 622 LNDNVAALLHQSTDRLTAEIWKDVEGIVglEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIV 701
Cdd:cd14895 543 PNAELFSVLGKTSDAHLRELFEFFKASE--SAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 702 PNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 753
Cdd:cd14895 621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
115-792 |
2.41e-117 |
|
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: 388.59 E-value: 2.41e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstMSYGELErqllQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----------LSVEKLN----AALTVLEAFGNVRTALNGNATRFSQLFSLDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC--SHYRFLTngPSSSPGQEREL---F 349
Cdd:cd01386 146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIV--PLQKPEDKQKAaaaF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 350 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRAL---------- 419
Cdd:cd01386 224 SKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpq 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 420 --LTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFeifQLN----- 492
Cdd:cd01386 304 qsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGF---QNPahsgs 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 493 ----SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP---ANPP---------GLLA 556
Cdd:cd01386 380 qrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLW 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 557 LLDEECWFPKATDKSFVEKV--AQEQGSHPKFQRPRNLRDQA-DFSVLHYAGK--VDYKASEWLMK-NMDPLNDNVAALL 630
Cdd:cd01386 460 LLDEEALYPGSSDDTFLERLfsHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 631 HQSTDRLTAEIWKDVegivgleqvsslgdgppggrprrgmfrtVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEkrAGK 710
Cdd:cd01386 540 QESQKETAAVKRKSP----------------------------CLQI-KFQVDALIDTLRRTGLHFVHCLLPQHN--AGK 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 711 LEPR--------------LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF-----MDGKQACEKM 771
Cdd:cd01386 589 DERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEEL 668
|
730 740
....*....|....*....|.
gi 1039779964 772 IQALELDPNLYRVGQSKIFFR 792
Cdd:cd01386 669 LEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
115-754 |
4.94e-110 |
|
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: 366.48 E-value: 4.94e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDRE--DQSI 190
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 191 LCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgvpASVSTMSYGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKF 269
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP---------TSWESHKIAErIEQRILNSNPVMEAFGNACTLRNNNSSRFGKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 270 IRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngPSSSPGQERELF 349
Cdd:cd14880 152 IQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL---PNPERNLEEDCF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 350 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTA---AQKLCRLLGLGVTDFSRALLTPRIKV 426
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 427 GRDYV--QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNE 504
Cdd:cd14880 309 GKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 505 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKS-FVEKVAQEQGSH 583
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 584 PKFQRPRnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppg 663
Cdd:cd14880 466 PCLGHNK-LSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 664 grPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 743
Cdd:cd14880 538 --QSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQ 615
|
650
....*....|.
gi 1039779964 744 EFRQRYEILTP 754
Cdd:cd14880 616 NFVERYKLLRR 626
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
115-792 |
4.21e-109 |
|
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: 363.82 E-value: 4.21e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH-----EVPPHVYAVTEGAYRSMLQDREDQ 188
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 189 SILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstmSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 268
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST----------------SSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 269 FIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QER 346
Cdd:cd14886 145 FIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGiDDQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 347 ELFQETLESLRVLgLLPEEITAMLRTVSAVLQFGNIVLKKERN--TDQATMPDNTAA-QKLCRLLGLGVTDFSRALLTPR 423
Cdd:cd14886 225 KEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 424 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQgasFLGILDIAGFEIFQLNSFEQLCINY 501
Cdd:cd14886 304 VVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfDADARP---WIGILDIYGFEFFERNTYEQLLINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 502 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVE----KVA 577
Cdd:cd14886 381 ANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSscksKIK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 578 QE-----QGShpkfqrprnlrdQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLE 652
Cdd:cd14886 458 NNsfipgKGS------------QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 653 QvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIC 732
Cdd:cd14886 526 K-----------------GKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTI 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 733 RQGFPNRILFQEFRQRYEILT--PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14886 589 HRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
115-792 |
1.51e-102 |
|
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: 345.26 E-value: 1.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG-KKRHEVPPHVYAVTEGAYRSM-LQDREDQSIL 191
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 192 CTGESGAGKTENTKKVIQYL---AHVASSPKGRKepgvpaSVSTmsygELERQLLQANPILEAFGNAKTVKNDNSSRFGK 268
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQR------SIAD----KIDENLKWSNPVMESFGNARTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 269 FIRINFD-IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYR-------FLTNGPS 339
Cdd:cd14875 151 YIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFVRRGVD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 340 SSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRAL 419
Cdd:cd14875 231 GKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 420 LtprIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPR---QGASFLGILDIAGFEIFQLNSFEQ 496
Cdd:cd14875 310 L---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASIT--PQgdcSGCKYIGLLDIFGFENFTRNSFEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 497 LCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKV 576
Cdd:cd14875 385 LCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 577 AQE-QGSHPKFQRPRN-LRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQv 654
Cdd:cd14875 462 WDQwANKSPYFVLPKStIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRKQ- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 655 sslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQ 734
Cdd:cd14875 539 ------------------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQ 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 735 GFPNRILFQEFRQRYEILTPNAIPKGFMDGK--QACEKMIQALE-----LDPNlYRVGQSKIFFR 792
Cdd:cd14875 601 GYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
115-749 |
2.28e-100 |
|
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: 340.53 E-value: 2.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVP------------PHVYAVTEGAYRSM 181
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGY--AYDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 182 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVS-TMSYGELERQLLQANPILEAFGNAKTVKN 260
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPaSPSRTTIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 261 DNSSRFGKFIRINF-DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-----AGEQLKADLLLEPCSHYRFL 334
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 335 TNGPSSSPG---QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL-----KKERNT--DQATMPDNTAA--- 401
Cdd:cd14899 239 NQSLCSKRRdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 402 --QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP-------- 471
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 472 ------RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLI 545
Cdd:cd14899 399 sdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 546 ERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE---QGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPL 622
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 623 NDNVAALLHQSTDRLTAEIW--KDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCI 700
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALAagSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1039779964 701 VPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 749
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
116-756 |
1.31e-96 |
|
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: 324.93 E-value: 1.31e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQlpIYTEAIVEMYRGKKRHeVPPHVYAVTEGAYRSMLQdREDQSILCTGE 195
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHvasspkgrkepgvpasvSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-----------------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 iaGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLlepcsHYRFLTnGPSSSPGQERELFQETLES 355
Cdd:cd14898 141 --GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTA-GNKESIVQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 356 LRVLGLLpeEITAMLRTVSAVLQFGNIVLKKERNTdqaTMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 435
Cdd:cd14898 213 MKSLGIA--NFKSIEDCLLGILYLGSIQFVNDGIL---KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 436 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSprqGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 515
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 516 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAqeqgshpKFQRpRNLRDQ 595
Cdd:cd14898 365 RAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIK-------KYLN-GFINTK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 596 AD--FSVLHYAGKVDYKASEWLMKNmdplndnvaallhqsTDRLTAEIWKDvEGIVGLEQVSSLgdgppggrprrgmfrt 673
Cdd:cd14898 433 ARdkIKVSHYAGDVEYDLRDFLDKN---------------REKGQLLIFKN-LLINDEGSKEDL---------------- 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 674 vGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 753
Cdd:cd14898 481 -VKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILG 559
|
...
gi 1039779964 754 PNA 756
Cdd:cd14898 560 ITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
115-792 |
7.13e-95 |
|
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: 324.68 E-value: 7.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE 186
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 187 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstmsygeLERQLLQANPILEAFGNAKTVKNDNSSRF 266
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG------------LEARLLQSGPVLEAFGNAHTVLNANSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 267 GKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGgaGEQLKADLLLEPCSHYRFLTNgpssspgqer 346
Cdd:cd14887 149 GKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCN--AAVAAATQKSSAGEGDPESTD---------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 347 elFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTA--------AQKLCRLL-------GLG 411
Cdd:cd14887 217 --LRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 412 VTDFSRALLT--------PRIKVGRDYV------------QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP 471
Cdd:cd14887 295 VTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 472 R-------------QGASFLGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGI-------- 527
Cdd:cd14887 375 KpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqdcsa 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 528 -PWTF-LDFGLDLQP--CIDLIERP--------ANPPGL---------LALLDEECWFPKATDKSFVEKVAQ--EQGSHP 584
Cdd:cd14887 455 fPFSFpLASTLTSSPssTSPFSPTPsfrsssafATSPSLpsslsslssSLSSSPPVWEGRDNSDLFYEKLNKniINSAKY 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 585 KFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLhQSTDRLTAEIwkdvegivgleqvssLGDGPPGG 664
Cdd:cd14887 535 KNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRLV---------------GSKKNSGV 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 665 RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 744
Cdd:cd14887 599 RAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVE 678
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1039779964 745 FRQRYEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 792
Cdd:cd14887 679 LWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
112-791 |
1.29e-90 |
|
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: 309.87 E-value: 1.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 112 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKQLPIYTEAIVEMYR-------GKKRHEVPPHVYAVTEGAYRSM 181
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 182 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSPKGRKepgvpasvstmsygeLERQLLQANPILEAFGNAKTVKN 260
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK---------------LSSQISAAEFVLDSFGNAKTLTN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 261 DNSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--- 337
Cdd:cd14879 144 PNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYgch 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 338 --PSSSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNI--VLKKERNTDqATMPDNTAA-QKLCRLLGLGV 412
Cdd:cd14879 224 plPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLefTYDHEGGEE-SAVVKNTDVlDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 413 TDFsRALLTPRIK-VGRD----YVQKAQTKEQADfaleALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFE 487
Cdd:cd14879 303 EDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 488 ifQL-----NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEEC 562
Cdd:cd14879 378 --NRsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 563 -WFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD---FSVLHYAGKVDYKASEWLMKNMDPLndnvaallhqSTDRLT 638
Cdd:cd14879 453 rRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPDFVN 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 639 aeiwkdvegivgleqvsslgdgppggrprrgMFRTVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 718
Cdd:cd14879 523 -------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKA 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779964 719 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPnaipkgFMDGKQACEKMIQALELDPNLYRVGQSKIFF 791
Cdd:cd14879 571 QIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
115-792 |
1.74e-89 |
|
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: 306.74 E-value: 1.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR---GKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 191
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 192 CTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstmSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 271
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS----------------SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 272 INF-DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-PSSSPGQERELF 349
Cdd:cd14878 145 LQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmREDVSTAERSLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 350 QETL----ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 425
Cdd:cd14878 225 REKLavlkQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 426 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS---FLGILDIAGFEIFQLNSFEQLCINYT 502
Cdd:cd14878 305 FKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 503 NEKLQQLFNHTMFVLEQEEYQREGIPW----------TFLDFGLDlqpcidlierpaNPPGLLALLDEEC---W-----F 564
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMetayspgnqtGVLDFFFQ------------KPSGFLSLLDEESqmiWsvepnL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 565 PKATdKSFVEKVAQEQGSHPKFQRPRN--LRDQ-ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEI 641
Cdd:cd14878 453 PKKL-QSLLESSNTNAVYSPMKDGNGNvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 642 WKdvegivgleqvSSLGdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLR 721
Cdd:cd14878 532 FQ-----------SKLV--------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQ 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 722 CNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 792
Cdd:cd14878 587 YIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
115-792 |
1.50e-85 |
|
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: 294.62 E-value: 1.50e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAhvasspKGRKEPGvpasvstmsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN-----------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG----PSSSPGQERELFQ 350
Cdd:cd14937 140 DEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKnvviPEIDDAKDFGNLM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 351 ETLESLRVLGLLPEeitaMLRTVSAVLQFGNIV---LKKERNTDQATMPDNT--AAQKLCRLLGLGVTDFSRALLTPRIK 425
Cdd:cd14937 220 ISFDKMNMHDMKDD----LFLTLSGLLLLGNVEyqeIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 426 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEK 505
Cdd:cd14937 296 IANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNN-KELNNYIGILDIFGFEIFSKNSLEQLLINIANEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 506 LQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGSHPK 585
Cdd:cd14937 375 IHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 586 FQRPRnlRD-QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgleqVS-SLGdgppg 663
Cdd:cd14937 451 YASTK--KDiNKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE-------VSeSLG----- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 664 gRPRRGMFRtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIcRQGFPNRILFQ 743
Cdd:cd14937 517 -RKNLITFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFD 589
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1039779964 744 EFRQRYEILTPNAIPKGFMDGKQACEKMIQAlELDPNLYRVGQSKIFFR 792
Cdd:cd14937 590 VFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
115-744 |
5.50e-79 |
|
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: 276.79 E-value: 5.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQDRE 186
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 187 DQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstMSYGELERQLLQANPILEAFGNAKTVKNDNSSRF 266
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTD---------------SQMTERIDKLIYINNILESMSNATTIKNNNSSRC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 267 GKFIRINFD---------IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPCSHYRFL-- 334
Cdd:cd14884 146 GRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 335 ------------------TNGPSSSPGQEREL-FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKkerntdqatm 395
Cdd:cd14884 226 deshqkrsvkgtlrlgsdSLDPSEEEKAKDEKnFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK---------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 396 pdntAAqklCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL-------- 467
Cdd:cd14884 296 ----AA---AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekde 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 468 ---DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFlDFGLDLQPCIDL 544
Cdd:cd14884 369 sdnEDIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 545 IERpanppgLLALLDE-----ECWFPKATDKSFV-----EKVAQEQGSH------PKFQRPRNLRDQAD---FSVLHYAG 605
Cdd:cd14884 448 IAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADGTAKKQNIKkniFFIRHYAG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 606 KVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgpPGGRPRRGMFRTVGQLYKESLSRL 685
Cdd:cd14884 522 LVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE---------------------ANNGGNKGNFLSVSKKYIKELDNL 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 686 MATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 744
Cdd:cd14884 581 FTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
116-791 |
2.43e-71 |
|
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: 252.73 E-value: 2.43e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYkqlpiyteaiveMYRGKKRHEVPPHVYA-------VTEGAYRSMLQDREDQ 188
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 189 SILCTGESGAGKTENTKKVIQYLAHVASspkgrkepGVPASvstmsygELERQLLQANPILEAFGNAKTVKNDNSSRFGK 268
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPET-------DAFKHLAAAFTVLRSLGSAKTATNSESSRIGH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 269 FIRINFDiAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNGPSSSPGQER 346
Cdd:cd14881 135 FIEVQVT-DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 347 EL-FQETLESLRVLGLlpeEITAMLRTVSAVLQFGNIVLKkERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 425
Cdd:cd14881 214 AArFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 426 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrspRQGAS--------FLGILDIAGFEIFQLNSFEQL 497
Cdd:cd14881 290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 498 CINYTNEKLQQLFNHTMFVLEQEEYQREGIPwTFLDFG-LDLQPCIDLIErpANPPGLLALLDEECwFPKATDKSFVEKV 576
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 577 AQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQstdrltaeiwkdvegivgleQVSS 656
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK--------------------QNCN 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 657 LGdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGF 736
Cdd:cd14881 501 FG------------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGY 568
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 737 PNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQ--ALELDPNL-------YRVGQSKIFF 791
Cdd:cd14881 569 PHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPPSKlssvstsWALGKRHIFL 632
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
116-752 |
7.67e-68 |
|
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: 242.72 E-value: 7.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 196 SGAGKTENTKKVIQYLAHVasspkGRKEPGVPASVstmsygelerqlLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 275
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRV------------ESSIKAILALVNAGTPLNADSTRCILQYQLTFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 276 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKaDLLLEPCSHYRFLTNGPSSSPGQER------- 346
Cdd:cd14882 145 STGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSKLKyrrddpe 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 347 ---ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKerNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPR 423
Cdd:cd14882 224 gnvERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 424 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 501
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 502 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECwfPKATDKSFV-EKVAQEQ 580
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYImDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 581 GSHPKfqrprnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivglEQVSSLgdg 660
Cdd:cd14882 457 SQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 661 ppggrprrgmfRTVGQLYKESLSRLMATLS-NTNPS---FVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGF 736
Cdd:cd14882 521 -----------RTLAATFRATSLELLKMLSiGANSGgthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
650
....*....|....*.
gi 1039779964 737 PNRILFQEFRQRYEIL 752
Cdd:cd14882 590 SYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
116-792 |
2.34e-66 |
|
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: 239.22 E-value: 2.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLahvasspkgrkepgVPASVSTMSYgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 274
Cdd:cd14905 80 ESGSGKSENTKIIIQYL--------------LTTDLSRSKY--LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 275 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ--ERELFQET 352
Cdd:cd14905 144 SLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 353 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtdQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 432
Cdd:cd14905 224 KMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 433 KAqtkeqadfalEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 512
Cdd:cd14905 302 NR----------DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 513 TMFVLEQEEYQREGIPW-TFLDFGlDLQPCIDLIERPANppgllaLLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRN 591
Cdd:cd14905 370 TVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEKIIN------LLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKPN 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 592 lrdqaDFSVLHYAGKVDYKASEWLMKNMDPLNDNvAALLHQSTdrLTAEIWKDvEGIVGLEQVSSlgdgppggrPRRGMF 671
Cdd:cd14905 443 -----KFGIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS--ITKYLFSR-DGVFNINATVA---------ELNQMF 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 672 RTVGQLYKESLS--RLMATLSNTNPS-----------------------------------------------FVRCIVP 702
Cdd:cd14905 505 DAKNTAKKSPLSivKVLLSCGSNNPNnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfhFIRCIKP 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 703 NHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFP----NRILFqefrQRYEILTPNAipKGFMD-GKQACEKMIQALEL 777
Cdd:cd14905 585 NSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFF----DRFSFFFQNQ--RNFQNlFEKLKENDINIDSI 658
|
730
....*....|....*
gi 1039779964 778 DPNLYRVGQSKIFFR 792
Cdd:cd14905 659 LPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
115-757 |
4.94e-65 |
|
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: 234.38 E-value: 4.94e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgkkrhevppHVYAVTEGAYRSMLQDRED-QSILCT 193
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 194 GESGAGKTENTKKVIQYLAhvaSSPKgrkepgvpASVSTMSYGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRIN 273
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPK--------SKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 274 FDiAGYIVGANIE-TYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQE 351
Cdd:cd14874 133 YK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDvNHFKH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 352 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD---QATMPDNTAAQKLCRLLgLGVtDFSR--ALLTPRIKV 426
Cdd:cd14874 212 LEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFL-LEV-DFDQlvNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 427 GrdyvqKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAsfLGILDIAGFEIFQLNSFEQLCINYTNEKL 506
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 507 QQLFNHTMFVLEQEEYQREGIPWTF-LDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK 585
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 586 FQRPRNlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSslgdgppggr 665
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVS---------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 666 prrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 745
Cdd:cd14874 510 --------QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
650
....*....|..
gi 1039779964 746 RQRYEILTPNAI 757
Cdd:cd14874 582 ARQYRCLLPGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
118-750 |
1.31e-61 |
|
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: 226.78 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 118 LHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKR----------HEVPPHVYAVTEGAYRSMLQDRED 187
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 188 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEpGVPASVSTMSYGElerQLLQANPILEAFGNAKTVKNDNSSRFG 267
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD-SEGASGVLHPIGQ---QILHAFTILEAFGNAATRQNRNSSRFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 268 KFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ--LKADLLLEPCSH-YRFLTNGP--SSSP 342
Cdd:cd14893 160 KMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVNeFVMLKQADplATNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 343 GQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL------KKERNTDQATMPDNTAAqklCRLLGLGVTDFS 416
Cdd:cd14893 240 ALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGGANSTTVSDAQS---CALKDPAQILLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 417 RALLTPRIKVGRDYVQKAQ----------------TKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQG-- 474
Cdd:cd14893 317 AKLLEVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNiv 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 475 --ASFLGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IPWTFLDFGLDLQPCID 543
Cdd:cd14893 397 inSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 544 LIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD------------FSVLHYAGKVDYKA 611
Cdd:cd14893 477 LFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 612 SEWLMKNMDPLNDNVAALLHQSTDrltaeiwkDVEGIVGLEQVSSL-----GDGPPGGRPRRGMFRTVGQLYKESLS--- 683
Cdd:cd14893 555 KGLSSKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAAssekaAKQTEERGSTSSKFRKSASSARESKNitd 626
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 684 -----------RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 750
Cdd:cd14893 627 saatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
137-279 |
1.35e-59 |
|
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: 202.57 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 137 FCVVINPYKQLPIYTEAIV-EMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 215
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 216 SSPKGRKEPGVPASVSTMsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 279
Cdd:cd01363 81 FNGINKGETEGWVYLTEI-TVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
116-790 |
9.87e-54 |
|
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: 202.37 E-value: 9.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR-GKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPAS-------VSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFG 267
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEednihneENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 268 KFIRINFDiAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNgpSSSPGQERE 347
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNN--EKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 348 LFQETLESLRVLGLL---PEEITAMLRTVSAVLQFGNI----------VLKKER----------------NTDQATMPDN 398
Cdd:cd14938 239 YSGKILELLKSLNYIfddDKEIDFIFSVLSALLLLGNTeivkafrkksLLMGKNqcgqninyetilseleNSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 399 TAAQKL-CRLLGLGVTDFSRALLTPRIkVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGA 475
Cdd:cd14938 319 VKNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 476 SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANpPGLL 555
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE-GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 556 ALLDEECwFPKATDKS-FVEKVAQEQGSHPKFQRPRN-LRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQS 633
Cdd:cd14938 477 SLLENVS-TKTIFDKSnLHSSIIRKFSRNSKYIKKDDiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 634 TDRLTAEIWK----DVEGIVGLEQ-----VSSLGDGPPGGRPRRGMFRTvgqLYKESLSRLMATLSNTNPSFVRCIVPNH 704
Cdd:cd14938 556 ENEYMRQFCMfynyDNSGNIVEEKrrysiQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 705 EKRA-GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIltPNAipkgfmDGKQACEKMIQALELDPNLYR 783
Cdd:cd14938 633 SKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 1039779964 784 VGQSKIF 790
Cdd:cd14938 705 IGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1040-1692 |
5.78e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.59 E-value: 5.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1040 EEKVKSLNKLRlkyeatisDMEDRLKKEEKGRQELEklkRRLDgessELQEQmVEQKQRAEELLAQLgrKEDELQAALLR 1119
Cdd:COG1196 172 ERKEEAERKLE--------ATEENLERLEDILGELE---RQLE----PLERQ-AEKAERYRELKEEL--KELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1120 AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELedtldstnaqQELRSKREQevte 1199
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----------YELLAELAR---- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1200 lkkalEEESRAHEvsmQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLE 1279
Cdd:COG1196 300 -----LEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1280 SQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRV 1359
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1360 RALEAEAAGLREQMEEEvvARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL 1439
Cdd:COG1196 452 AELEEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1440 ERARRRLQQELDDATVDLGQQKQLLSTLEKKQRkfdqlLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEA 1519
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAA-----IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1520 REELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQA--ASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQH 1597
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLreVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1598 ERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE 1677
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
650
....*....|....*
gi 1039779964 1678 LWREVEETRSSRDEM 1692
Cdd:COG1196 765 LERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
928-1537 |
9.24e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.20 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 928 EETRARLAarkqELELVVTELEARVGEEEEcsrqlQSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtteAKMKKFEED 1007
Cdd:COG1196 182 EATEENLE----RLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLRELE-----AELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1008 LLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQEL----EKLKRRLDg 1083
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerlEELEEELA- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1084 essELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1163
Cdd:COG1196 327 ---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1164 DLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEvsmqELRQRHSQALVEMAEQLEQARRGKGVW 1243
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA----ELEEEEEALLELLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1244 EKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQ--RAQAELESVSTALSEAE 1321
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQNIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1322 SKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1401
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1402 EEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEE 1481
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1482 KAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRA----LRAELEAL 1537
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERelerLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
875-1403 |
4.14e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.89 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 875 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE 954
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 955 EEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKLSKERRLLEERLAEFSS 1034
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE---ALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1035 QAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQ 1114
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1115 AALLRAEEEGGARAQLLKSLREAQAGL-AEAQEDLEAERVARAKAEKQRRDLGEELEALR--GELEDTLDSTNAQQELRS 1191
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLeAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgvEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1192 KREQEVTELKKALEE-----ESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQT 1266
Cdd:COG1196 551 IVVEDDEVAAAAIEYlkaakAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1267 SRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSA----ESQLHDTQ 1342
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAllaeEEEERELA 710
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1343 ELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEE 1403
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1155-1751 |
4.62e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.89 E-value: 4.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1155 RAKAEKQ----RRDLgEELEALRGELEDTLDSTnaqqelrsKREQEVTELKKALEEESRAHEVSMQELRQRHSQA-LVEM 1229
Cdd:COG1196 174 KEEAERKleatEENL-ERLEDILGELERQLEPL--------ERQAEKAERYRELKEELKELEAELLLLKLRELEAeLEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1230 AEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAE 1309
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1310 LESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQS 1389
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1390 TQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEK 1469
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1470 KQRKfdqllAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLsskddVGKNVH 1549
Cdd:COG1196 485 ELAE-----AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL-----QNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1550 ELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEE 1629
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1630 RKQRALAMAARKKLELELEELKAQT-SAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEmfTLSRENEKKLKGLEA 1708
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGgSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE--ALLAEEEEERELAEA 712
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1039779964 1709 EVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEE 1751
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1621 |
2.25e-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: 121.70 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 870 RQDEVLQARAQELQKVQELQQQ-SAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 948
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKELKAElRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 949 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1028
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1029 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELlaqlgr 1108
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA------ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1109 kedELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1188
Cdd:TIGR02168 434 ---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1189 LRSKREQE------VTELKKALEEESRAHEVSMQELRQ----RHSQALVEMAEQLEQARRGKGVW----EKTRLSLEAEV 1254
Cdd:TIGR02168 511 LLKNQSGLsgilgvLSELISVDEGYEAAIEAALGGRLQavvvENLNAAKKAIAFLKQNELGRVTFlpldSIKGTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1255 SELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSeAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSA 1334
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDN-ALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1335 ESQLHDTQELlqEETRAKLA-LGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEE 1413
Cdd:TIGR02168 670 SSILERRREI--EELEEKIEeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1414 ARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRE 1493
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1494 RIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELE 1573
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1039779964 1574 DELTAAEDAKLRLevtvQALKAQHERDLQGrddaGEERRRQLAKQLRD 1621
Cdd:TIGR02168 908 SKRSELRRELEEL----REKLAQLELRLEG----LEVRIDNLQERLSE 947
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
121-733 |
1.01e-25 |
|
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: 116.00 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 121 LRERYYSGLIYTYSGLFCV-VINPYKQL------PIYTEAIVEMYRGKKRHE--VPPHVYAV------------------ 173
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 174 --TEGAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVASSP--KGRKE----------PGVPASVST------- 232
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPAlsKGSEEtckvsgstrqPKIKLFTSStkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 233 ----------------------------------------------------------MSYGELERQL------------ 242
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyekLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 243 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDIAGY---IVGANIETYLLEKSRAIRQA------KDECSFHI 307
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 308 FYQLLGGAG-----EQLKADLLLE--PCSHYRFLTNGPSSSPG---------QERELFQETLESLRVLGLLPEEITAMLR 371
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGfvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 372 TVSAVLQFGNIVLKKERNTDQATMPDN---TAAQKLCRLLGLG-VTDFSRALLTPRIKV--GRDYVQKAQTKEQADFALE 445
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGsVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 446 ALAKATYERLFRWLVLRLNRAL----------------DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQql 509
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY-- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 510 fnhtmfvleQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKAT----------DKSFVEKVAQE 579
Cdd:cd14894 564 ---------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 580 QGSHPKfQRPRNLRDQA----------DFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE--G 647
Cdd:cd14894 635 NSSRLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlG 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 648 IVGLEQVSSLGDGPPGGRPRRGMfrtVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 727
Cdd:cd14894 714 WSPNTNRSMLGSAESRLSGTKSF---VGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIR 789
|
....*.
gi 1039779964 728 GIRICR 733
Cdd:cd14894 790 QMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1152-1951 |
1.56e-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: 112.46 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1152 RVARAKAEKQRRDLgEELEALRGELEDTLDSTNAQ-------QELRSKREQ--------EVTELKKALEEeSRAHEVSMQ 1216
Cdd:TIGR02168 175 KETERKLERTRENL-DRLEDILNELERQLKSLERQaekaeryKELKAELRElelallvlRLEELREELEE-LQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1217 ELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERAR 1296
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1297 SEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEE 1376
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1377 VVARERAGRELQS-----TQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELD 1451
Cdd:TIGR02168 413 EDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1452 DATVDLGQQKQL---LSTLEKKQRKFDQLL----------AEEKAAVLRAV-EDRERIEAEGREREARALS-LTRALEEE 1516
Cdd:TIGR02168 493 SLERLQENLEGFsegVKALLKNQSGLSGILgvlselisvdEGYEAAIEAALgGRLQAVVVENLNAAKKAIAfLKQNELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1517 QEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLE----VTVQA 1592
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyriVTLDG 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1593 LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQ 1672
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1673 VQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNlskaatlEEK 1752
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EAL 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1753 RQLEGRLsqleeeleeeqnnsELLKDHYRKLVLQVESLTTELSAersfsakAESGRQQLERQIQELRARLgEEDAGARAR 1832
Cdd:TIGR02168 806 DELRAEL--------------TLLNEEAANLRERLESLERRIAA-------TERRLEDLEEQIEELSEDI-ESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1833 QKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAee 1912
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL-- 941
|
810 820 830
....*....|....*....|....*....|....*....
gi 1039779964 1913 easrAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1951
Cdd:TIGR02168 942 ----QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1293-1884 |
2.26e-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: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1293 ERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQ 1372
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1373 MEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDD 1452
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1453 ATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRA 1532
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1533 ELEALLSSKDDVGKnvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERR 1612
Cdd:COG1196 464 LLAELLEEAALLEA---ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1613 RQLAKQLRDAEVERDEER--------KQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEE 1684
Cdd:COG1196 541 EAALAAALQNIVVEDDEVaaaaieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1685 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEE 1764
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1765 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSfsakAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKL 1844
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAERE----ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1845 AQ-------AEEQL-EQESRERILSGKL--VRRAEKRLKEVVLQVDEERR 1884
Cdd:COG1196 777 EAlgpvnllAIEEYeELEERYDFLSEQRedLEEARETLEEAIEEIDRETR 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
878-1533 |
4.08e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 111.77 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 878 RAQELQKVQELQQ-QSAREVGELQGRVAQLEEERTRLAEQLRaEAELCSEAEETRARLAARKQElELVVTELEARVGEEE 956
Cdd:PTZ00121 1171 KAEDAKKAEAARKaEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 957 ECSRQLQSEKKRLQQHIQELESHLEAEEgARQKLQLEKvtteAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQA 1036
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKK----AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1037 AEEEEKvkSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRldGESSELQEQmvEQKQRAEELL--AQLGRKEDELQ 1114
Cdd:PTZ00121 1324 AEEAKK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKE--EAKKKADAAKkkAEEKKKADEAK 1397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1115 aallRAEEEGGARAQLLKSLREAQAGLAEAQEdlEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKRE 1194
Cdd:PTZ00121 1398 ----KKAEEDKKKADELKKAAAAKKKADEAKK--KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1195 QEvtELKKALEEESRAHEVsmqelrQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSE--LKAELSSLQTSRQEGE 1272
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKADEA------KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAKKAE 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1273 QKRRRLEsqLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAK 1352
Cdd:PTZ00121 1544 EKKKADE--LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1353 LALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAE- 1431
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEa 1701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1432 -KTEAVERLERARRRLQQELDDA-TVDLGQQKQLLSTLEKKQRKFDQLLAEEkaavlravEDRERIEAEGREREARALSL 1509
Cdd:PTZ00121 1702 kKAEELKKKEAEEKKKAEELKKAeEENKIKAEEAKKEAEEDKKKAEEAKKDE--------EEKKKIAHLKKEEEKKAEEI 1773
|
650 660
....*....|....*....|....
gi 1039779964 1510 TRALEEEQEAREELERQNRALRAE 1533
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
928-1740 |
1.06e-23 |
|
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: 109.76 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 928 EETRARLAARKQELELV---VTELEARVGeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteaKMKKF 1004
Cdd:TIGR02168 175 KETERKLERTRENLDRLediLNELERQLK-----SLERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1005 EEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLkkeekgrQELEKLKRRLDGE 1084
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-------QILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1085 SSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRD 1164
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1165 LGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALeEESRAHEVSMQelrqrhsqaLVEMAEQLEQarrgkgvwe 1244
Cdd:TIGR02168 398 LNNEIERLEARLERL-------EDRRERLQQEIEELLKKL-EEAELKELQAE---------LEELEEELEE--------- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1245 ktrlsLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRssdserarseaAEKLQRAQAELESVSTALSEAESKA 1324
Cdd:TIGR02168 452 -----LQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-----------LDSLERLQENLEGFSEGVKALLKNQ 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1325 IRLGKELSSAESQLHDTQELlqeETRAKLALGSRVRAL----EAEAAGLREQMEEEVVAR-------ERAGRELQSTQAQ 1393
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGY---EAAIEAALGGRLQAVvvenLNAAKKAIAFLKQNELGRvtflpldSIKGTEIQGNDRE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1394 LSEWrrrQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQEL-------------------DDAT 1454
Cdd:TIGR02168 593 ILKN---IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTN 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1455 VDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRaleeeqeareelerQNRALRAEL 1534
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR--------------QISALRKDL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1535 EALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQH---ERDLQG-RDDAGEE 1610
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDElRAELTLL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1611 RRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTS--AAGQGKEEAVKQLKKMQVQMKELWREVEETRSS 1688
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSE 895
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1689 RDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAS 1740
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1396 |
1.40e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 109.85 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 849 KLRNWQWWRLFIKVKPLLQVTRQ-----------DEVLQA----------RAQELQKVQELQQQS--AREVGELQGRVaq 905
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaikaeearkaDELKKAeekkkadeakKAEEKKKADEAKKKAeeAKKADEAKKKA-- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 906 leEERTRLAEQLRAEAELCSEAEET-RARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 984
Cdd:PTZ00121 1325 --EEAKKKADAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 985 GARQKLQLEKvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKlrlKYEATISDMEDRL 1064
Cdd:PTZ00121 1403 DKKKADELKK--AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK---KAEEAKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1065 KKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL-AQLGRKEDELQAALLRAEEEGGARAQLLKSLREaqagLAE 1143
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE----LKK 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1144 AQEDLEAERVARA----KAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEvtELKKALEEESRAHEV-SMQEL 1218
Cdd:PTZ00121 1554 AEELKKAEEKKKAeeakKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELkKAEEE 1631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1219 RQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE 1298
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1299 A-----AEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEaaGLREQM 1373
Cdd:PTZ00121 1712 AeekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEED 1789
|
570 580
....*....|....*....|...
gi 1039779964 1374 EEEVVARERAGRELQSTQAQLSE 1396
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
870-1503 |
6.80e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 107.53 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 870 RQDEVLQARAQELQKVQELQQ-QSAREVGELQGRVAQLEEERTRLAEQLRaEAELCSEAEETRARLAARKQELELVVTEL 948
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVRKAEEL 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 949 ----EARVGEE----EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL--LLEDQNSKL 1018
Cdd:PTZ00121 1194 rkaeDARKAEAarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMahFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1019 SKERRLLEE-RLAEFSSQAAE--EEEKVKSLNKLRLKYEATisdmedrlKKEEKGRQELEKLKRRLDgessELQEQMVEQ 1095
Cdd:PTZ00121 1274 AEEARKADElKKAEEKKKADEakKAEEKKKADEAKKKAEEA--------KKADEAKKKAEEAKKKAD----AAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1096 KQRAEELLAQLGRKEDELQAALLRAE------EEGGARAQLLK----SLREAQAGLAEAQED-LEAERVARAKAEKQRRD 1164
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEaaekkkEEAKKKADAAKkkaeEKKKADEAKKKAEEDkKKADELKKAAAAKKKAD 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1165 lgeelealrgELEDTLDSTNAQQELRSKREQ--EVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGV 1242
Cdd:PTZ00121 1422 ----------EAKKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1243 WEKTRlsLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARS-------EAAEKLQRAQaELESVST 1315
Cdd:PTZ00121 1492 AEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkadelKKAEELKKAE-EKKKAEE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1316 ALSEAESK--AIRLGKELSSAESQLHDTQELLQEETRAKLALGSRvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQ 1393
Cdd:PTZ00121 1569 AKKAEEDKnmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1394 LSEWRRRQEEEAAVLEAGEEARRRAAReaetltqrlaEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRK 1473
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDK----------KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
650 660 670
....*....|....*....|....*....|
gi 1039779964 1474 FDQLLAEEKAAVLRAVEDRERIEAEGRERE 1503
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
867-1504 |
1.19e-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: 106.29 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 867 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 946
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 947 ELEARVgeeeecsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEedlllLEDQNSKLSKERRLLE 1026
Cdd:TIGR02168 383 TLRSKV-------AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1027 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEdrlkkEEKGRQE-LEKLKRRLDGESSELQEQMVEQKQRAEEL--L 1103
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELA-----QLQARLDsLERLQENLEGFSEGVKALLKNQSGLSGILgvL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1104 AQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAGLA-EAQEDLEAERVA-----RAKAEKQRRDLGEELEALRGELE 1177
Cdd:TIGR02168 526 SELISVDEGYEAAI---EAALGGRLQAVVVENLNAAKKAiAFLKQNELGRVTflpldSIKGTEIQGNDREILKNIEGFLG 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1178 --------------------------DTLDSTNAQQEL-------------------------------RSKREQEVTEL 1200
Cdd:TIGR02168 603 vakdlvkfdpklrkalsyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEEL 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1201 KKALEE-ESRAHEVSMQelRQRHSQALVEMAEQLEQARRGKgvwektrLSLEAEVSELKAELSSLQTSRQEGEQKRRRLE 1279
Cdd:TIGR02168 683 EEKIEElEEKIAELEKA--LAELRKELEELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1280 SQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRV 1359
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1360 RALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL 1439
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1440 ERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVED-----RERIEAEGREREA 1504
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDdeeeaRRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
871-1744 |
5.44e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.45 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 871 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQElelvvtelEA 950
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE--------DA 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 951 RVGEEeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERRLLEERLA 1030
Cdd:PTZ00121 1140 RKAEE---ARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKA 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1031 EfSSQAAEEEEKVKSLNKLRlkyEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQM-VEQKQRAEELL-AQLGR 1108
Cdd:PTZ00121 1215 E-EARKAEDAKKAEAVKKAE---EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELKkAEEKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1109 KEDEL-QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQ 1187
Cdd:PTZ00121 1291 KADEAkKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1188 ELRSKREQEVTELKKALEEESRAHEVSMQ-ELRQRHSQALVEMAEQLEQARRGKGVWEKTRlslEAEVSELKAELS-SLQ 1265
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADELKKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAkKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1266 TSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvstalsEAESKAirlgKELSSAESQLHDTQELL 1345
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-------EAKKKA----DEAKKAAEAKKKADEAK 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1346 QEEtRAKLALGSRvRALEAEAAGLREQMEEEVVARE-RAGREL-QSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAE 1423
Cdd:PTZ00121 1517 KAE-EAKKADEAK-KAEEAKKADEAKKAEEKKKADElKKAEELkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1424 TLTQRLAEKTEAVERLERARRRLQ----QELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEG 1499
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1500 REREAralslTRALEEEQEAREELERQNRALRAELEALlssKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAA 1579
Cdd:PTZ00121 1675 KKAEE-----AKKAEEDEKKAAEALKKEAEEAKKAEEL---KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1580 EDAKLRLEvtvQALKAQHERdlQGRDDAGEERRRQLAKQLRDAEVERDEERKQRA--LAMAARKKLELELEELKAQTSAA 1657
Cdd:PTZ00121 1747 EEAKKDEE---EKKKIAHLK--KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFANIIEGGKEGNLVI 1821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1658 GQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEE 1737
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
....*..
gi 1039779964 1738 VASGNLS 1744
Cdd:PTZ00121 1902 IPNNNMA 1908
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
885-1403 |
1.40e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 102.45 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 885 VQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELElvvtELEARVGEEEECSRQLQS 964
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 965 EKKRLQQHIQELESHlEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVK 1044
Cdd:PRK03918 267 RIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1045 SLNKLRLKYEAtisdMEDRLKKEEKGRQ---ELEKLKRRLDGESSELQEQMVEQKQRAEEllaQLGRKEDELQAALLRAE 1121
Cdd:PRK03918 346 KLKELEKRLEE----LEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1122 EEGGARAQLLKSLREAQAGL----AEAQEDLEAERVARAKAE-----KQRRDLGEELEALRGELEDTLDSTNAQQELRsk 1192
Cdd:PRK03918 419 KEIKELKKAIEELKKAKGKCpvcgRELTEEHRKELLEEYTAElkrieKELKEIEEKERKLRKELRELEKVLKKESELI-- 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1193 REQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLE--------QARRGKGVwEKTRLSLEAEVSELKAELSSL 1264
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeikslkkELEKLEEL-KKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1265 QTS-RQEGEQKRRRLESQLQEVQGRSSDSERARSeAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQE 1343
Cdd:PRK03918 576 LKElEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1344 LLQEETRAKLAlgSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEE 1403
Cdd:PRK03918 655 KYSEEEYEELR--EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
956-1751 |
1.91e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.91 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 956 EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----RRLLEERLAE 1031
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKaedaRKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1032 FSSQA-----AEEEEKVKSLNKlrlkyeatisdMEDRLKKEEKGRQELEklkRRLDGESSELQEQMVEQKQRAEELlaql 1106
Cdd:PTZ00121 1174 DAKKAeaarkAEEVRKAEELRK-----------AEDARKAEAARKAEEE---RKAEEARKAEDAKKAEAVKKAEEA---- 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1107 grKEDELQAAllRAEEEggaraqllkSLREAQAGLAEAQEDLEAERVARAKAEKQRRdlgeelealRGELEDTLDSTNAQ 1186
Cdd:PTZ00121 1236 --KKDAEEAK--KAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARK---------ADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1187 QELRSKREQEVTELKKALEEESRAHEVSMQ-ELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSlEAEVSELKAELSSLQ 1265
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-EAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1266 TSrqEGEQKRRRLESQLQEVqgRSSDSERARSE----AAEKLQRAQAELESVSTALSEAESKaiRLGKELSSAESQLHDT 1341
Cdd:PTZ00121 1373 KE--EAKKKADAAKKKAEEK--KKADEAKKKAEedkkKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1342 QELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEaavleageearrraarE 1421
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK----------------K 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1422 AETLTQRLAEKTEAVERLERARRRLQQELDDAtvdlgqqkqllstleKKQRKFDQLlaeEKAAVLRAVEDRERIEAEGRE 1501
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKA---------------EEKKKADEL---KKAEELKKAEEKKKAEEAKKA 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1502 REARALSLTRALeeeqeareelerqnralraELEALLSSKDDVGKNVHELERARKAaeqaasdlrtqvteleDELTAAED 1581
Cdd:PTZ00121 1573 EEDKNMALRKAE-------------------EAKKAEEARIEEVMKLYEEEKKMKA----------------EEAKKAEE 1617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1582 AKLRLEvtvQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVE---RDEERKQRALAMAARKKLELELEELKAQTSAAG 1658
Cdd:PTZ00121 1618 AKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1659 QGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKlkglEAEVLRLQEELAASDRARRQAQQDRDEMAEEV 1738
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
810
....*....|...
gi 1039779964 1739 ASGNLSKAATLEE 1751
Cdd:PTZ00121 1771 EEIRKEKEAVIEE 1783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
866-1585 |
1.99e-20 |
|
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: 98.99 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 866 LQVTRQDEVLQAraqELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVV 945
Cdd:TIGR02169 290 LRVKEKIGELEA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 946 TELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLL 1025
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1026 EERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAE---EL 1102
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGT 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1103 LAQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAglAEAQEDLEAERVARA------KAEKQRRDLGEELEAlrGEL 1176
Cdd:TIGR02169 527 VAQLGSVGERYATAI---EVAAGNRLNNVVVEDDAVA--KEAIELLKRRKAGRAtflplnKMRDERRDLSILSED--GVI 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1177 EDTLDSTNAQQELRSKREQEV--TELKKALEEESRAhevsMQELRqrhsqaLVEMAEQLEQ--------ARRGKGVWEKT 1246
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKYVFgdTLVVEDIEAARRL----MGKYR------MVTLEGELFEksgamtggSRAPRGGILFS 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1247 RlSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIR 1326
Cdd:TIGR02169 670 R-SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1327 LGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAglREQMEEevvarerAGRELQSTQAQLSEWRRRQEEeaa 1406
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPE-------IQAELSKLEEEVSRIEARLRE--- 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1407 vleageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVL 1486
Cdd:TIGR02169 817 ------------------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1487 RAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERArKAAEQAASDLR 1566
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQ 957
|
730
....*....|....*....
gi 1039779964 1567 TQVTELEDELTAAEDAKLR 1585
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNML 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
874-1220 |
1.20e-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: 93.20 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 874 VLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRaeaELCSEAEETRARLAARKQELElvvtELEARVG 953
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLA----RLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 954 EEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFS 1033
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1034 SQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEklkrrldGESSELQEQMVEQKQRAEELLAQLGRKEDEL 1113
Cdd:TIGR02168 824 ERLESLERRIAAT-------ERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1114 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEEL-EALRGELEDTLDSTNAQQELRSK 1192
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEE 969
|
330 340
....*....|....*....|....*...
gi 1039779964 1193 REQEVTELKKALEEESRAHEVSMQELRQ 1220
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEE 997
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
950-1832 |
1.21e-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: 90.13 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 950 ARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteAKMKKFEEDLLLLED-QNSKLSKERRLLEER 1028
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER----EKAERYQALLKEKREyEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1029 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgrqeleKLKRRLDGESSELQEQMveqkqraEELLAQLGR 1108
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEKI-------GELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1109 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAK-------AEKQRRDLGEELEALRGELedtld 1181
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyaeLKEELEDLRAELEEVDKEF----- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1182 stnaqQELRSKREQEVTELKKALEE--ESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKA 1259
Cdd:TIGR02169 381 -----AETRDELKDYREKLEKLKREinELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1260 ELSSLQTSRQEGEQKRRRLESQLQEVqgrssdsERARSEAAEKLQRAQAELESVSTalSEAESKAIRlgKELSSAESQLH 1339
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRV-------EKELSKLQRELAEAEAQARASEE--RVRGGRAVE--EVLKASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1340 DT-QELLQEETRAKLALGSrvraleaeAAGLREQ---MEEEVVA--------RERAGR-------ELQSTQAQLSEWRRR 1400
Cdd:TIGR02169 525 GTvAQLGSVGERYATAIEV--------AAGNRLNnvvVEDDAVAkeaiellkRRKAGRatflplnKMRDERRDLSILSED 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1401 -------------QEEEAAVL----------EAGEEARRRAAREAETLTQRLAEKTEAV-------ERLERARRRLQQEL 1450
Cdd:TIGR02169 597 gvigfavdlvefdPKYEPAFKyvfgdtlvveDIEAARRLMGKYRMVTLEGELFEKSGAMtggsrapRGGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1451 DDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARAlsltraleeeqeareeleRQNRAL 1530
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE------------------EKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1531 RAELEALLSskddvgknvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEvtvQALKAQHERDLQGRDDAGEE 1610
Cdd:TIGR02169 739 LEELEEDLS----------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKLEE 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1611 RRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVeetrssrd 1690
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------- 877
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1691 emftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQ 1770
Cdd:TIGR02169 878 ------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 1771 NnsellkdhYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQEL---RARLGEEDAGARAR 1832
Cdd:TIGR02169 952 S--------LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELkekRAKLEEERKAILER 1008
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
865-1396 |
3.96e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.20 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 865 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV 944
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 945 VtELEARVGEEEECSRQLQSEKKRLQQHIQELE---SHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1021
Cdd:PRK03918 296 I-KLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1022 RRlLEERLAEFSSQAAEE-----EEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRL--------DGESSEL 1088
Cdd:PRK03918 375 ER-LKKRLTGLTPEKLEKeleelEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKEL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1089 QEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKsLREAQAGLAEAQEDLEAERVARAKAE-KQRRDLGE 1167
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKaEEYEKLKE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1168 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHevsmQELRQRHSQALVEMAEQLEQARRGKGVWEKTR 1247
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL----KELEELGFESVEELEERLKELEPFYNEYLELK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1248 lSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEaaEKLQRAQAELESVSTALSEAESKAIRL 1327
Cdd:PRK03918 609 -DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEEL 685
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1328 GKELSSAESQLHDTQELLQEETRAKLALGSRVRALEaEAAGLREQMEE-EVVARERAGRELQSTQAQLSE 1396
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKyKALLKERALSKVGEIASEIFE 754
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
870-1202 |
4.13e-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: 88.20 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 870 RQDEVLQARAQELQKVQELQqqsaREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELE 949
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 950 ARVGEEEECSRQLqsEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERL 1029
Cdd:TIGR02169 772 EDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1030 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK 1109
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1110 EDELqAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRrdlgEELEALRGELEDTLDSTNAQQEL 1189
Cdd:TIGR02169 930 EEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEY----EEVLKRLDELKEKRAKLEEERKA 1004
|
330
....*....|...
gi 1039779964 1190 RSKREQEVTELKK 1202
Cdd:TIGR02169 1005 ILERIEEYEKKKR 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
927-1310 |
6.62e-17 |
|
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: 87.42 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 927 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKL---QLEKVTTEAKMKK 1003
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1004 FEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDG 1083
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1084 ESSELQEqmveqkqRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1163
Cdd:TIGR02168 818 EAANLRE-------RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1164 DLGEELEALRGELEDTLdstNAQQELRSKREQEVTELKKALEEESRAhEVSMQELRQR---HSQALVEMAEQLEQARrgk 1240
Cdd:TIGR02168 891 LLRSELEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGL-EVRIDNLQERlseEYSLTLEEAEALENKI--- 963
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1241 gvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARseaaEKLQRAQAEL 1310
Cdd:TIGR02168 964 ---EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAK----ETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
895-1727 |
5.88e-16 |
|
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: 84.35 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 895 EVGELQGRVAQLEEERTRLAEQLRAEAElcsEAEETRArLAARKQELElvVTELEARVGEEEECSRQLQSEKKRLQQHIQ 974
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRRERE---KAERYQA-LLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 975 ELESHLE--AEEGARQKLQLEKVTTEAkMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1052
Cdd:TIGR02169 255 KLTEEISelEKRLEEIEQLLEELNKKI-KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1053 YEATISDMEDRLKKEEKGR-----------QELEKLKRRLDGESSELQEQMVEQKQRAEEL------LAQLGRKEDELQA 1115
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRdklteeyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLeklkreINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1116 ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE-RVARAKAEKQRRDLG---EELEALRGELEDTldstnaqQELRS 1191
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSkyeQELYDLKEEYDRV-------EKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1192 KREQEVTELKKaleeesrahEVSMQELRQRHSQALVEMAEQLEQARRGK-----GVWEKTRLSLE-AEVSELKAELSSLQ 1265
Cdd:TIGR02169 487 KLQRELAEAEA---------QARASEERVRGGRAVEEVLKASIQGVHGTvaqlgSVGERYATAIEvAAGNRLNNVVVEDD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1266 TSRQEGEQ--KRRRLESQ----LQEVQGRSSDSERARSEA----AEKLQRAQAELESV------STALSEAESKAIRLGK 1329
Cdd:TIGR02169 558 AVAKEAIEllKRRKAGRAtflpLNKMRDERRDLSILSEDGvigfAVDLVEFDPKYEPAfkyvfgDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1330 E--LSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAV 1407
Cdd:TIGR02169 638 KyrMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1408 LEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLR 1487
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1488 AveDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRT 1567
Cdd:TIGR02169 798 A--ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1568 QVTELEDELTAAEDAKLRLEVTVQALkaqherdlqgrddagEERRRQLAKQLRDAEvERDEERKQRALAMAARKKLELEL 1647
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLREL---------------ERKIEELEAQIEKKR-KRLSELKAKLEALEEELSEIEDP 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1648 EELKAQTSAAGQGKEEAVKQLKKMQVQMKELW-------REVEETRSSRDEMftlsrenEKKLKGLEAEVLRLQEELAAS 1720
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDEL-------KEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 1039779964 1721 DRARRQA 1727
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1191-1965 |
6.46e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 6.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1191 SKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKgvwEKTRLSLEAEVSElkaelsslqtSRQE 1270
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA---EDARKAEEARKAE----------DARK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1271 GEQKRRRLESQLQEVQGRSSDSERAR-SEAAEKLQRAqaelESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEET 1349
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKA----EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1350 RaklalgsrvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQlsEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRL 1429
Cdd:PTZ00121 1218 R---------KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE--EIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1430 AEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLL--AEEK---AAVLRAVEDRERIEAEGREREA 1504
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkAEEAkkaAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1505 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDlrtqvtelEDELTAAEDAKL 1584
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--------AEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1585 RLEVTVQA----LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRAlamaarkkleLELEELKAQTSAAGQG 1660
Cdd:PTZ00121 1439 KAEEAKKAdeakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA----------EEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1661 KEEAVKQLKKMQVQMKELWREVEETRSSRDemftLSRENEKKlkglEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAS 1740
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADE----AKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1741 GNLSKAATLEEKRQLEgrlSQLEEELEEEQNNSELLKDHYRKLvlQVESLTTElSAERSFSAKAESGRQQLERQIQELRA 1820
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEE---VMKLYEEEKKMKAEEAKKAEEAKI--KAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1821 RlgEEDAGARARQKMLIAALESKlaQAEEQLEQESRERILSGKLVRRAE--KRLKEVVLQVDEERRVADQVRDQLEKSNL 1898
Cdd:PTZ00121 1655 A--EEENKIKAAEEAKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1899 RLKQLKR----------QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVF 1965
Cdd:PTZ00121 1731 KAEEAKKeaeedkkkaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
867-1172 |
7.00e-16 |
|
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: 84.34 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 867 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 946
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 947 ELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE 1026
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1027 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1106
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1107 grkedelqaallraeeeggarAQLLKSLREAQAGLAEAQEDLEAERVA-RAKAEKQRRDLGEELEAL 1172
Cdd:TIGR02168 939 ---------------------DNLQERLSEEYSLTLEEAEALENKIEDdEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1296-1951 |
1.42e-15 |
|
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: 83.18 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1296 RSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAEsqlhDTQELLQEETRAKLAL-GSRVRALEAEAAGLREQME 1374
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELALlVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1375 EEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDAT 1454
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1455 VDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1534
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1535 EALLSSKDDVGKNVHELERARKAA------------EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERdLQ 1602
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAelkelqaeleelEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-LQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1603 GRDDAGEERRRQ------------------------------------------LAKQLRDAEVERDEERKQ-------- 1632
Cdd:TIGR02168 489 ARLDSLERLQENlegfsegvkallknqsglsgilgvlselisvdegyeaaieaaLGGRLQAVVVENLNAAKKaiaflkqn 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1633 ---RALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKK---------------------------MQVQMKELWREV 1682
Cdd:TIGR02168 569 elgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsyllggvlvvddldnaleLAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1683 EET------------RSSRDEMFTLSRENEkkLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLE 1750
Cdd:TIGR02168 649 TLDgdlvrpggvitgGSAKTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1751 EKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGAR 1830
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1831 ARQKMLiAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEerrvadqVRDQLEKSNLRLKQLKRQLEEA 1910
Cdd:TIGR02168 807 ELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEAL 878
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1039779964 1911 EEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1951
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
949-1884 |
4.67e-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: 81.56 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 949 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1028
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA--KKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1029 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGR 1108
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1109 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1188
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1189 LRSKREQEVTELKKALEEEsrahevsMQELRQRHSQALVEMAEQleqarrgkgvwEKTRLSLEAEVSELKAELSSLQTSR 1268
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQL-------EDLLKEEKKEELEILEEE-----------EESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1269 QEGEQKRRRLESQLQEVQGRSSdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEe 1348
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKL-------QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1349 tRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR 1428
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1429 LAEKTEAVERLERARRRLQQELDDATVDLGqqKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1508
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESA--KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1509 LTRALEEEQEAREELErqnraLRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1588
Cdd:pfam02463 690 AKEEILRRQLEIKKKE-----QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1589 TVQALKAQHERDlqgrddagEERRRQLAKQLRDAEVERDEERKQRALAMAarkkleleleelkaqtsaagqgKEEAVKQL 1668
Cdd:pfam02463 765 EKSELSLKEKEL--------AEEREKTEKLKVEEEKEEKLKAQEEELRAL----------------------EEELKEEA 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1669 KKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAAT 1748
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1749 LEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAErsfsAKAESGRQQLERQIQELRARLGEEdag 1828
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE----EADEKEKEENNKEEEEERNKRLLL--- 967
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779964 1829 ararQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERR 1884
Cdd:pfam02463 968 ----AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1079-1858 |
8.55e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1079 RRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaraqllkslREAQAGLAEAQEDLEAERVARAKA 1158
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEA-----------RKAEEAKKKAEDARKAEEARKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1159 EKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRhsqalVEMAEQLEQARR 1238
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARK-----AEAARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1239 GkgvwEKTRLSLEAEVSElkaELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERArsEAAEKLQRAQAELESVSTALS 1318
Cdd:PTZ00121 1214 A----EEARKAEDAKKAE---AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA--HFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1319 EAESKaiRLGKELSSAEsQLHDTQELLQEETRAKLALGSRVRALEA--EAAGLREQMEEEVVARERAGRELQSTQAQLSe 1396
Cdd:PTZ00121 1285 KAEEK--KKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAkkKADAAKKKAEEAKKAAEAAKAEAEAAADEAE- 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1397 wRRRQEEEAAVLEAGEEARRRAAREAETLTQRlaeKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRkfdq 1476
Cdd:PTZ00121 1361 -AAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK---- 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1477 llAEEkaAVLRAVEDRERIEAEGREREAR-ALSLTRALEEEQEAREELERQNRALRAelEALLSSKDDVGKNVHELERAR 1555
Cdd:PTZ00121 1433 --ADE--AKKKAEEAKKADEAKKKAEEAKkAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAA 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1556 KAAEQAASDLRTQVTELEDELTAAEDAKLRLEvtvqALKAQHERDLQGRDDAGEERRRQLAKQLRDAevERDEERKQRAL 1635
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADE----AKKAEEKKKADELKKAEELKKAEEKKKAEEA--KKAEEDKNMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1636 AMA--ARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELwREVEETRSSRDEMFTLSRENEKKlkgleAEVLRL 1713
Cdd:PTZ00121 1581 RKAeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKKEAEEKKK-----AEELKK 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1714 QEElaasDRARRQAQQDRDEMAEEVASGNLSKAAtlEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKlvlqVESLTTE 1793
Cdd:PTZ00121 1655 AEE----ENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK----AEELKKA 1724
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 1794 LSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALE---SKLAQAEEQLEQESRER 1858
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEirkEKEAVIEEELDEEDEKR 1792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
898-1496 |
2.21e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 898 ELQGRVAQLEEERTRLaEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEEcsRQLQSEKKRLQQHIQELE 977
Cdd:COG4913 239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 978 SHLEAEEGARQKLQlekvttEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAeeeekvkslnKLRLKYEATI 1057
Cdd:COG4913 316 ARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA----------ALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1058 SDMEDRlkkeekgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRA----EEEGGARAQLLKS 1133
Cdd:COG4913 380 EEFAAL-------RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1134 LREAQAGL---AEAQEDLEAERVARAKAEK----QRRDL----GEELEALRgeledTLDSTNAQQELRSKR--EQEVTEL 1200
Cdd:COG4913 453 LGLDEAELpfvGELIEVRPEEERWRGAIERvlggFALTLlvppEHYAAALR-----WVNRLHLRGRLVYERvrTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1201 KKALEEESRAHEVS----------MQELRQRHSQALVEMAEQLEQARRG----------KGVWEK--------------- 1245
Cdd:COG4913 528 RPRLDPDSLAGKLDfkphpfrawlEAELGRRFDYVCVDSPEELRRHPRAitragqvkgnGTRHEKddrrrirsryvlgfd 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1246 --TRL-SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRS--SDSERARSEAAEKLQRAQAELESVSTALSEa 1320
Cdd:COG4913 608 nrAKLaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERLDASSDD- 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1321 eskairlgkeLSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1400
Cdd:COG4913 687 ----------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1401 QEEEAAVLEAGEEARRRAAREAETLTQRLAEK-TEAVERLERARRRLQQELDDATVDLGQQKQLLSTLE-----KKQRKF 1474
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALLDRLEedglpEYEERF 836
|
650 660 670
....*....|....*....|....*....|.
gi 1039779964 1475 DQLLAE----EKAAVLRAVED-----RERIE 1496
Cdd:COG4913 837 KELLNEnsieFVADLLSKLRRaireiKERID 867
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
932-1404 |
6.29e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 932 ARLAAR--KQELELVVTELEARVGEEEEcsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL 1009
Cdd:PRK02224 174 ARLGVErvLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1010 LLEDqnskLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQ 1089
Cdd:PRK02224 252 ELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1090 EQMVEQKQRAEELLAQLGRKEDELQAALLRAEEeggaraqllksLREAQaglAEAQEDLEAERVARAKAEKQRRDLGEEL 1169
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEE-----------LREEA---AELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1170 EALRGELEDTLDSTNAQQELRskreQEVTELKKALEEESRAHEVSMQELRQRhsqalVEMAEQLEQARR----GKGVWEK 1245
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFL----EELREERDELREREAELEATLRTARER-----VEEAEALLEAGKcpecGQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1246 TRLSL----EAEVSELKAELSSLQTSRQEGEQKRRRLESqLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAE 1321
Cdd:PRK02224 465 PHVETieedRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1322 SKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLrEQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1401
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELN 622
|
...
gi 1039779964 1402 EEE 1404
Cdd:PRK02224 623 DER 625
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1495-1938 |
1.16e-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: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1495 IEAEGREREARALSLTRALEEEQEAREELERQnrALRAELEALLSskddvgknvhELERARKAAEQAASDLRTQVTELED 1574
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELE--ELEAELEELEA----------ELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1575 ELTAAEDAKLRLEVTVQALKAQHER--DLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKA 1652
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1653 QTSAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRD 1732
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1733 EMAEEVAsgNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLE 1812
Cdd:COG1196 446 EAAEEEA--ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1813 RQIQELRARLGEEDAGAR----ARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQ 1888
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1889 VRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESM 1938
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1228-1945 |
1.28e-13 |
|
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: 76.65 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1228 EMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEqKRRRLESQLQEVQG-----RSSDSERARSEAAEK 1302
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1303 LQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLA-LGSRVRALEAEAAGLREQMEEEVVARE 1381
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGeLEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1382 RAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQK 1461
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1462 QLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSK 1541
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1542 DDVGKNVHELERARKAAEQAASDLRTQVTELEDEL-----TAAEDAKLRlEVTVQALKAQHERDLQG---RDDAGEERRR 1613
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgTVAQLGSVG-ERYATAIEVAAGNRLNNvvvEDDAVAKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1614 QLAKQLRDAEVE-------RDEERKQRALAM-----------------------------------AARKKLEL------ 1645
Cdd:TIGR02169 565 ELLKRRKAGRATflplnkmRDERRDLSILSEdgvigfavdlvefdpkyepafkyvfgdtlvvedieAARRLMGKyrmvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1646 ---------------ELEELKAQTSAAGQGKEEAVK-QLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAE 1709
Cdd:TIGR02169 645 egelfeksgamtggsRAPRGGILFSRSEPAELQRLReRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1710 VLRLQEELAAS--------------DRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSel 1775
Cdd:TIGR02169 725 IEQLEQEEEKLkerleeleedlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK-- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1776 LKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEdagaRARQKMLIAALESKLAQAEeqlEQES 1855
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI----EKEIENLNGKKEELEEELE---ELEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1856 RERILSGKLVRRAEKRlKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRE------LE 1929
Cdd:TIGR02169 876 ALRDLESRLGDLKKER-DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLE 954
|
810
....*....|....*.
gi 1039779964 1930 DVTESAESMNREVTTL 1945
Cdd:TIGR02169 955 DVQAELQRVEEEIRAL 970
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1070-1880 |
1.56e-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: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1070 GRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKslREAQAglaeaQEDLE 1149
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRR--RESQS-----QEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1150 aervarakaeKQRRDLGEELEALRGELEDTLDSTNAQQElrskreqevtELKKALeeesRAHEVSMQELRQrhsqALVEm 1229
Cdd:pfam15921 145 ----------NQLQNTVHELEAAKCLKEDMLEDSNTQIE----------QLRKMM----LSHEGVLQEIRS----ILVD- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1230 aeqLEQARrGKGVWEKTRLSlEAEVSELKAELSSLQtsrqegeqkrRRLESQLQEVQGR----SSDSERARSEAAEK--- 1302
Cdd:pfam15921 196 ---FEEAS-GKKIYEHDSMS-TMHFRSLGSAISKIL----------RELDTEISYLKGRifpvEDQLEALKSESQNKiel 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1303 -LQRAQAELESVstaLSEAESKAIRLGKELSSAESQLHDTQ---ELLQEETRAKLALGSR-VRALEAEAAGLREQMEEEV 1377
Cdd:pfam15921 261 lLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQNSMYMRqLSDLESTVSQLRSELREAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1378 VARERAGRELqstqaqlsewrrrqeEEAAVLEAGEearrraareaetLTQRLAEKTEAVERLERARRRLQQELddatVDL 1457
Cdd:pfam15921 338 RMYEDKIEEL---------------EKQLVLANSE------------LTEARTERDQFSQESGNLDDQLQKLL----ADL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1458 GQQKQLLStLEKKQRK--FDQLLAEEKAA--VLRAVEDR----ERIEAEGREREARALSLTRALEEEQEAREELERQNRA 1529
Cdd:pfam15921 387 HKREKELS-LEKEQNKrlWDRDTGNSITIdhLRRELDDRnmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1530 LRAELEallSSKDDVGKNVHELERAR---KAAEQAASDLRTQVTELED--ELTAAEDAKLRLEVTVQALKAQHerdLQGR 1604
Cdd:pfam15921 466 LTAQLE---STKEMLRKVVEELTAKKmtlESSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLKLQELQH---LKNE 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1605 DDageerrrqlakQLRDAEVERDEERKQRAlamAARKKLELELEELKAQTSAAGQGKEEAvkqlKKMQVQMKELWREVEE 1684
Cdd:pfam15921 540 GD-----------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQLVGQHGRTA----GAMQVEKAQLEKEIND 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1685 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEEL-----AASDRAR--RQAQQDRDEMAEEVASGNLSKAATLEEKRQLEG 1757
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvnAGSERLRavKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1758 RLSQLEEEleeeqnnselLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQ-------LERQIQELRARLG------- 1823
Cdd:pfam15921 682 NFRNKSEE----------METTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDalqskiq 751
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 1824 --EEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVD 1880
Cdd:pfam15921 752 flEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
933-1565 |
1.96e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 933 RLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQ---HIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdll 1009
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEVKELEELKEEIEE--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1010 lLEDQNSKLSKERRLLEERLAEFSSQAAEE-------EEKVKSLNKLRlKYEATISDMEDRLKKEEKGRQELEKLKRRLD 1082
Cdd:PRK03918 243 -LEKELESLEGSKRKLEEKIRELEERIEELkkeieelEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1083 GESSELQEQMVEQKQRAEELlAQLGRKEDELQAALLRAEEeggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKqr 1162
Cdd:PRK03918 321 EEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL-- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1163 rdlgEELEALRGELEDTLDSTNAQqelRSKREQEVTELKKALEEESRAHE---VSMQELRQRHSQALveMAEQLEQARRg 1239
Cdd:PRK03918 394 ----EELEKAKEEIEEEISKITAR---IGELKKEIKELKKAIEELKKAKGkcpVCGRELTEEHRKEL--LEEYTAELKR- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1240 kgvWEKTRLSLEAEVSELKAELSSLQTSRqEGEQKRRRLESQLQEVQgrsSDSERARSEAAEKLQRAQAELESVstalse 1319
Cdd:PRK03918 464 ---IEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKELAEQLK---ELEEKLKKYNLEELEKKAEEYEKL------ 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1320 aESKAIRLGKELSSAESQLHDTQELLQEetraKLALGSRVRALEAEAAGLREQMEEEVVARERagrELQSTQAQLSEWRR 1399
Cdd:PRK03918 531 -KEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELGFESVE---ELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1400 RQEEeaavleageearrraareAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLgqqKQLLSTLEKKQRKFDQlla 1479
Cdd:PRK03918 603 EYLE------------------LKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSE--- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1480 eekaavlravEDRERIEAEGREREaRALSltraleeeqeareelerqnrALRAELEALLSSKDDVGKNVHELERARKAAE 1559
Cdd:PRK03918 659 ----------EEYEELREEYLELS-RELA--------------------GLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
....*.
gi 1039779964 1560 QAASDL 1565
Cdd:PRK03918 708 KAKKEL 713
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
867-1480 |
2.79e-13 |
|
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: 75.78 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 867 QVTRQDEVLQARaqelQKVQELQQQSAREVGELQGRVAQLEEER---------TRLAEQLRAEAELCSEAEETRARLAAR 937
Cdd:TIGR00618 244 YLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEETQerinrarkaAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 938 KQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIqelESHLEAEEGARQKLQLEKVTTEAK-MKKFEEDLLLLEDQ-- 1014
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQhIHTLQQQKTTLTQKlq 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1015 --NSKLSKERRLLEERLAEFSSQAAEEEEKV--KSLNKLRLKYEATISDMEDRLKKEEKGRQ-ELEKLKRRLDGESSELQ 1089
Cdd:TIGR00618 397 slCKELDILQREQATIDTRTSAFRDLQGQLAhaKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1090 --EQMVEQKQRAEELLAQLGRKEDELQ----------AALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE------ 1151
Cdd:TIGR00618 477 tkEQIHLQETRKKAVVLARLLELQEEPcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQltserk 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1152 RVARAKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMA 1230
Cdd:TIGR00618 557 QRASLKEQMQEiQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1231 EQLEQARrgkgvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAEL 1310
Cdd:TIGR00618 637 CSQELAL------KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1311 ESVSTA---LSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLalgsrvraleAEAAGLREQMEEEVVARERAGREL 1387
Cdd:TIGR00618 711 THIEEYdreFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL----------KARTEAHFNNNEEVTAALQTGAEL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1388 QSTQAQLSEWRRRQEE---EAAVLEAGEEARRRAAREAETLTQ-RLAEKTEAVERLERARRRLQQELDDATVDLGQQKQL 1463
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEdthLLKTLEAEIGQEIPSDEDILNLQCeTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
650
....*....|....*..
gi 1039779964 1464 LSTLEKKQRKFDQLLAE 1480
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDK 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1146-1636 |
3.01e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1146 EDLEAERVARAKAEKQRRDLgEELEALRGELEDTLDSTNAQQELRSK-----REQEVTELKKALEEESRAHEVSMQELRQ 1220
Cdd:COG4913 235 DDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1221 RHSQ--ALVEMAEQLEQARRGKGVwektrlsleAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSE----R 1294
Cdd:COG4913 314 LEARldALREELDELEAQIRGNGG---------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1295 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHdtqellqeetraklALGSRVRALEAEAAGLREQME 1374
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--------------SLERRKSNIPARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1375 EEVVARERAGR---ELQSTQAQLSEWRR---------------RQEEEAAVL-----------------EAGEEARRRAA 1419
Cdd:COG4913 451 EALGLDEAELPfvgELIEVRPEEERWRGaiervlggfaltllvPPEHYAAALrwvnrlhlrgrlvyervRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1420 REAETLTQRLAEKTEAVERLERARRRLQ---------QELDDA----TVDlGQQKQLLSTLEKKQRK------------- 1473
Cdd:COG4913 531 LDPDSLAGKLDFKPHPFRAWLEAELGRRfdyvcvdspEELRRHpraiTRA-GQVKGNGTRHEKDDRRrirsryvlgfdnr 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1474 -----FDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNR--ALRAELEALLSSKDDVGk 1546
Cdd:COG4913 610 aklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERLDASSDDLA- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1547 nvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDlqgRDDAGEERRRQLAKQLRDAEVER 1626
Cdd:COG4913 689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLELRALLEERFAAALGDA 762
|
570
....*....|
gi 1039779964 1627 DEERKQRALA 1636
Cdd:COG4913 763 VERELRENLE 772
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1246-1941 |
3.16e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1246 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQ--GRSSDSERARSEAAEKLQRAQAELESVSTALSEAESK 1323
Cdd:PTZ00121 1058 GKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGkaEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1324 AIRLGKELSSAESQLHDTQELLQEETRaklalgsrvRALEAEAAGLREQMEEEVVARE--RAGRELQSTQAQLSEWRRRQ 1401
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEIARKAEDAR---------KAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1402 EEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEE 1481
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1482 --KAAVLRAVEDRERI-EAEGREREARalsltraleeeqeareelerqnralraeleallsskddvgknvhELERARKAA 1558
Cdd:PTZ00121 1289 kkKADEAKKAEEKKKAdEAKKKAEEAK--------------------------------------------KADEAKKKA 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1559 EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMA 1638
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1639 ARKKLELELEELKAQTSAAGQGKEEAVK--QLKKMQVQMK---ELWREVEETRSSRDemftLSRENEKKLKGLEAEvlRL 1713
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKkadEAKKKAEEAKKAEE----AKKKAEEAKKADEAK--KK 1478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1714 QEELAASDRARRQAQQDRDEmAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTE 1793
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1794 LSAERSfsAKAESGRQQLERQIQELRaRLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAE--KR 1871
Cdd:PTZ00121 1558 KKAEEK--KKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekKK 1634
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1872 LKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAqagrrrlQRELEDVTESAESMNRE 1941
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-------KKAEEDEKKAAEALKKE 1697
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
880-1396 |
5.96e-13 |
|
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: 74.37 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 880 QELQKVQELQQQSAREVGELQGRVAQL------------------EEERTR---LAEQLRAEAELCSEAEETRARLAark 938
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEINDKEKQVSLLliqitekenkmkdltfllEESRDKanqLEEKTKLQDENLKELIEKKDHLT--- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 939 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKL 1018
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1019 SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYE------ATISDMEDRLKKEEKGRQELEKLKRRLDG-------ES 1085
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKLLDEKKQFEKIAEELKGKEQELIFllqarekEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1086 SELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGG-------ARAQLLKSLREAQAGLAEAQEDLEAERVARAKA 1158
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklllENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1159 EKQRRDLGE-------ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQR--HSQALVEM 1229
Cdd:pfam05483 533 LKQIENLEEkemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQieNKNKNIEE 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1230 AEQLEQARRGKGVWEKTRLSL-EAEVSELKAELSS--------LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAA 1300
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAyEIKVNKLELELASakqkfeeiIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1301 EKLQRAQAELESVSTALSEAESKAIRLGKELSSaESQLHDTQEllQEETRAKLALGSRVRALEAEAAGLREQMEEEVVAR 1380
Cdd:pfam05483 693 EIDKRCQHKIAEMVALMEKHKHQYDKIIEERDS-ELGLYKNKE--QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
570
....*....|....*.
gi 1039779964 1381 ERAGRELQSTQAQLSE 1396
Cdd:pfam05483 770 EKLKMEAKENTAILKD 785
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
873-1395 |
2.37e-12 |
|
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: 72.55 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 873 EVLQARAQELQKVQELQQQSAR------EVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRArlaarkqeLELVVT 946
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRiaeaemQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKA--------LQTVIE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 947 ELEARVGEEEECSRQLQSEKKRL-----------QQHIQELE---SHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE 1012
Cdd:pfam10174 237 MKDTKISSLERNIRDLEDEVQMLktngllhtedrEEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLT 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1013 DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNkLRLKYEATIsdmedrLKKEEKGRQELEKLKRRLDGESSELQeQM 1092
Cdd:pfam10174 317 NQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALR-LRLEEKESF------LNKKTKQLQDLTEEKSTLAGEIRDLK-DM 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1093 VEQKQRA--------EELLAQLGRKE---DELQAALLRAEEEGGARAQLLKSLREAqagLAEAQEDLEAERVARAKAEKQ 1161
Cdd:pfam10174 389 LDVKERKinvlqkkiENLQEQLRDKDkqlAGLKERVKSLQTDSSNTDTALTTLEEA---LSEKERIIERLKEQREREDRE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1162 RRdlgEELEALRGELEDTLDSTNAQQELRSKREQEVTELKkaleEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKG 1241
Cdd:pfam10174 466 RL---EELESLKKENKDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1242 VWEKTRLSleAEVSELKAELSSlqtsrqegeqKRRRLEsqlQEVQGRSSDSERARSEAA---EKLQRAQAELESVSTALS 1318
Cdd:pfam10174 539 QLKKAHNA--EEAVRTNPEIND----------RIRLLE---QEVARYKEESGKAQAEVErllGILREVENEKNDKDKKIA 603
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1319 EAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLS 1395
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1286 |
2.78e-12 |
|
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: 71.98 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 861 KVKPLLQVTRQDEVLQARAQELQ-KVQELQQQSAREV-GELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 938
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 939 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL 1018
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1019 SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEkgrQELEKLKRRLDGESSELqEQMVEQKQR 1098
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKEL-KKLNEEKKE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1099 AEELLAQLGRKEDELQaallraeeeggaraqllkslreaqaglaEAQEDLEAERvarAKAEKQRRDLGEELEalrgELED 1178
Cdd:TIGR04523 508 LEEKVKDLTKKISSLK----------------------------EKIEKLESEK---KEKESKISDLEDELN----KDDF 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1179 TLDSTNAQQELRSKrEQEVTELKKALEEESRAHEvSMQELRQRHSQALVEMAEQLEQarrgkgvWEKTRLSLEAEVSELK 1258
Cdd:TIGR04523 553 ELKKENLEKEIDEK-NKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEE-------KEKKISSLEKELEKAK 623
|
410 420
....*....|....*....|....*...
gi 1039779964 1259 AELSSLQTSRQEGEQKRRRLESQLQEVQ 1286
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
875-1236 |
7.44e-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: 71.14 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 875 LQARAQELQKVQELQQQsarevgelQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE 954
Cdd:COG3096 329 YQAASDHLNLVQTALRQ--------QEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 955 EEECSRQLQSEKKRLQQHIQELEShleaeegARQKLQLEKVTTEAkmkkFEEDLLLLEDQNSKLSKERRLLEERLAEFSS 1034
Cdd:COG3096 401 YQQALDVQQTRAIQYQQAVQALEK-------ARALCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKLSVADA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1035 QAAEEEEKVKSLNKlrlkyeatISDMEDRLKKEEKGRQ------ELEKLKRRLDGESSELQE--QMVEQKQRAEELLAQL 1106
Cdd:COG3096 470 ARRQFEKAYELVCK--------IAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQLAEleQRLRQQQNAERLLEEF 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1107 GRK-------EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDT 1179
Cdd:COG3096 542 CQRigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEA 621
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1180 LDSTnaqqelrskreQEVTELKKALEEESRAHEVSMQELRQRhSQALVEMAEQLEQA 1236
Cdd:COG3096 622 LADS-----------QEVTAAMQQLLEREREATVERDELAAR-KQALESQIERLSQP 666
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
903-1937 |
7.53e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 71.01 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 903 VAQLEEERTRLAEQLRAEAELCSEAEEtraRLAARKQELELVVTELEARVGEE--------EECSRQLQSEKKRLQQHIQ 974
Cdd:NF041483 246 AAESDQARRQAAELSRAAEQRMQEAEE---ALREARAEAEKVVAEAKEAAAKQlasaesanEQRTRTAKEEIARLVGEAT 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 975 ELESHLEAEEG---ARQKLQLEKVTTEAKMKKfeeDLLLLEDQNSKLSKERRLLEERLAEFSSQA-------AEEEEKVK 1044
Cdd:NF041483 323 KEAEALKAEAEqalADARAEAEKLVAEAAEKA---RTVAAEDTAAQLAKAARTAEEVLTKASEDAkattraaAEEAERIR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1045 SLNKL---RLKYEAtiSDMEDRLK-------KEEKGRQ-ELEKLKRRLDGESSELQEQMVEQKQRaeellaqlgrkedel 1113
Cdd:NF041483 400 REAEAeadRLRGEA--ADQAEQLKgaakddtKEYRAKTvELQEEARRLRGEAEQLRAEAVAEGER--------------- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1114 qaalLRAEEEGGARAQLLKSLREAQAGLAEAQEDL-EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE-LRS 1191
Cdd:NF041483 463 ----IRGEARREAVQQIEEAARTAEELLTKAKADAdELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1192 KREQEVTELKKALEEESRahevsmqELRqrhsqalvEMAEQLEQARRGKGVWEKTRLSLEAEvSELKAELSSLQTSRQEG 1271
Cdd:NF041483 539 EAEEQAEEVRAAAERAAR-------ELR--------EETERAIAARQAEAAEELTRLHTEAE-ERLTAAEEALADARAEA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1272 EQKRRRlesqlqevqgRSSDSERARSEAAEKLQ--RAQAELES----------VSTALSEAESKAIRLGKELSSAESQLH 1339
Cdd:NF041483 603 ERIRRE----------AAEETERLRTEAAERIRtlQAQAEQEAerlrteaaadASAARAEGENVAVRLRSEAAAEAERLK 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1340 DTQELLQEETRAKLALGSRVRALEAEAAgLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAA 1419
Cdd:NF041483 673 SEAQESADRVRAEAAAAAERVGTEAAEA-LAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEA 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1420 ReaeTLTQRLAEKTEA-VERLERARRRLQQELDDATVDLGQQKQ-----LLSTLE--------KKQRKFDQLLAEEKAAV 1485
Cdd:NF041483 752 Q---AEAQRLVEEADRrATELVSAAEQTAQQVRDSVAGLQEQAEeeiagLRSAAEhaaertrtEAQEEADRVRSDAYAER 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1486 LRAVEDRERIEAEGREREARALSLtraleeeqeareelerqnralraeleallsSKDDVGKNVHELERARKAAEQAASDL 1565
Cdd:NF041483 829 ERASEDANRLRREAQEETEAAKAL------------------------------AERTVSEAIAEAERLRSDASEYAQRV 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1566 RTqvtELEDELTAAEDAKLRLEVtvqalkaqherdlQGRDDAgeERRRQLAKQLRDAEVERDEERKQRALAMAARKKLEL 1645
Cdd:NF041483 879 RT---EASDTLASAEQDAARTRA-------------DAREDA--NRIRSDAAAQADRLIGEATSEAERLTAEARAEAERL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1646 ELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSR-ENEKKLKGLEAEVLRLQEELAAS---- 1720
Cdd:NF041483 941 RDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRtEAERVKAEAAAEAERLRTEAREEadrt 1020
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1721 -DRARRQAQQDRDEMAEEV---ASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYR----------KLVLQ 1786
Cdd:NF041483 1021 lDEARKDANKRRSEAAEQAdtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERivaeatvegnSLVEK 1100
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1787 VESLTTEL--SAERSFSA---KAESGRQQLERQIQELRARLGEEDA----GARARQKMLIAALESKLAQAEEQLEQ---- 1853
Cdd:NF041483 1101 ARTDADELlvGARRDATAireRAEELRDRITGEIEELHERARRESAeqmkSAGERCDALVKAAEEQLAEAEAKAKElvsd 1180
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1854 ----ESRERILSgklVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRL-KQLKRQLEEAEEEASRAQAGRRRLQrel 1928
Cdd:NF041483 1181 anseASKVRIAA---VKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTvEEGKRELDVLVRRREDINAEISRVQ--- 1254
|
....*....
gi 1039779964 1929 eDVTESAES 1937
Cdd:NF041483 1255 -DVLEALES 1262
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
796-1284 |
7.63e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 7.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 796 LAQLEEERdlkvtdiivsfqaaargylarrafqrrqqqqsalrvmqrncaaylklrnwqwwrlfikvkpLLQVTRQDEVL 875
Cdd:COG1196 360 LAEAEEAL-------------------------------------------------------------LEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 876 QARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEE 955
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 956 EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQ 1035
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1036 AAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQE---LEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1112
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1113 LQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDtldstnAQQELRSK 1192
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE------LAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1193 REQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELsslqtSRQEGE 1272
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP-----DLEELE 766
|
490
....*....|..
gi 1039779964 1273 QKRRRLESQLQE 1284
Cdd:COG1196 767 RELERLEREIEA 778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
867-1283 |
1.24e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 867 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAeAELCSEAEETRARLA----------A 936
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-LPLYQELEALEAELAelperleeleE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 937 RKQELELVVTELEARVGEEEECSRQLQSEKKRL----QQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE 1012
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1013 DQNSKLSKERRLLEER--------LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEE----KGRQELEKLKRR 1080
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKaslgKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1081 LDGESSELQEQMVEQ---KQRAEELLAQLGRKEDELQAALLRAEEEgGARAQLLKSLREAQAGLAEAQEDLEAERVARAK 1157
Cdd:COG4717 314 EELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEEL-EEELQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1158 AEKQRRDLGEELEALRGELEdtldstnaqQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAE---QLE 1234
Cdd:COG4717 393 QAEEYQELKEELEELEEQLE---------ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEleaELE 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1235 QARRGKGVWEKT--RLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQ 1283
Cdd:COG4717 464 QLEEDGELAELLqeLEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1126-1338 |
3.11e-11 |
|
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: 67.48 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1126 ARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALE 1205
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1206 EESRA---HEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQL 1282
Cdd:COG4942 101 AQKEElaeLLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779964 1283 QEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQL 1338
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1269-1951 |
4.43e-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: 68.28 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1269 QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQrAQAELesvstaLSEAESKAIRLGKELSSAESQLHDTQELLQEE 1348
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-AETEL------CAEAEEMRARLAARKQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1349 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLsewrRRQEEEAAVLEageearrraareaetltqr 1428
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKI----KKLEEDILLLE------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1429 laektEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEekaavlraVEDRERIEAEGRErearals 1508
Cdd:pfam01576 145 -----DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD--------LEERLKKEEKGRQ------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1509 ltraleeeqeareelerqnralraeleallsskddvgknvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1588
Cdd:pfam01576 205 -----------------------------------------ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1589 TVQALKAQHErDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQ------TSAAGQ--- 1659
Cdd:pfam01576 244 ELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldTTAAQQelr 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1660 -GKEEAVKQLKKMQVqmkelwrevEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEV 1738
Cdd:pfam01576 323 sKREQEVTELKKALE---------EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1739 ASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQEL 1818
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1819 RARLGEEdagarARQKMLIA----ALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLE 1894
Cdd:pfam01576 474 QELLQEE-----TRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1895 KSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1951
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
915-1400 |
6.05e-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: 67.94 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 915 EQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEEcsrQLQSEKKRLQQHIQELESHLEAeegARQKLQLEK 994
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQE---ERQETSAELNQLLRTLDDQWKE---KRDELNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 995 VTTEAKMKKFEEDLLLLEDQNSKLSKER----RLLEERLAEFSSQAAEEEEKVKSL----NKLRLKYEATISDMEDRLKK 1066
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKALtgkhQDVTAKYNRRRSKIKEQNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1067 EEKG-RQELEKLK----RRLDGESSELQEQmvEQKQRaEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSlREAQAGL 1141
Cdd:pfam12128 391 DIAGiKDKLAKIReardRQLAVAEDDLQAL--ESELR-EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1142 AEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRA--HEVSMQELR 1219
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTllHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1220 QRHSQALVEMAEQLEQARRGKGVWEKT----------RLSLE--------AEVSELKAELSSLQTSRQEGEQKRRRLESQ 1281
Cdd:pfam12128 547 WEQSIGKVISPELLHRTDLDPEVWDGSvggelnlygvKLDLKridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1282 L-------QEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL-GKELSSAESQL----HDTQELLQEET 1349
Cdd:pfam12128 627 LvqangelEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEAQLkqldKKHQAWLEEQK 706
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1350 RAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRE-LQSTQAQLSEWRRR 1400
Cdd:pfam12128 707 EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSgAKAELKALETWYKR 758
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
865-1631 |
6.55e-11 |
|
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: 67.84 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 865 LLQVTRQDEVLQARAQELQKVQELQQQSARE-VGELQGRVAQLEEERTRLAEQLRAEaelcSEAEETRarlaarKQELEL 943
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsVIDLQTKLQEMQMERDAMADIRRRE----SQSQEDL------RNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 944 VVTELEArvgeeEECSRQLQSEKKRLQqhIQELESHLEAEEGARQKLQLEKVT-TEAKMKKFEE----DLLLLEDQNSKL 1018
Cdd:pfam15921 150 TVHELEA-----AKCLKEDMLEDSNTQ--IEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIYEhdsmSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1019 SKERRLLEERLAEFSSQAAEEEEKVKSL-----NKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV 1093
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALksesqNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1094 EQKQRAEELLAQLGRKEDELQAALlraeeeggarAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1173
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTV----------SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1174 GELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQrhsqalvEMAEQLEQARRgkgvwektrlsLEAE 1253
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRR-------ELDDRNMEVQR-----------LEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1254 VSELKAELSSlqtsrqegeqkrrRLESQLQEVQGRSsdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSS 1333
Cdd:pfam15921 435 LKAMKSECQG-------------QMERQMAAIQGKN--------ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1334 AESQLHDTQELLQEETRAklalgsrVRALEAEAAGLREQME---EEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLea 1410
Cdd:pfam15921 494 SERTVSDLTASLQEKERA-------IEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVI-- 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1411 geearRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAE---EKAAV-- 1485
Cdd:pfam15921 565 -----EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlelEKVKLvn 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1486 -----LRAVED---------------RERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSS-KDDV 1544
Cdd:pfam15921 640 agserLRAVKDikqerdqllnevktsRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlKSME 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1545 GKNVHELERARKAAEQAASDlRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRqLAKQLrdaEV 1624
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNK-MAGEL---EV 794
|
....*..
gi 1039779964 1625 ERDEERK 1631
Cdd:pfam15921 795 LRSQERR 801
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1066-1930 |
7.10e-11 |
|
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: 67.79 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1066 KEEKGRQELEKLKRRLD------GESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaraqLLKSLREAQA 1139
Cdd:TIGR02169 171 KKEKALEELEEVEENIErldliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1140 GLAEAQEDLEaervaraKAEKQRRDLGEELEALRGELEDtldstnAQQELRSKREQEVTELKKALeeesraHEVSMQELR 1219
Cdd:TIGR02169 245 QLASLEEELE-------KLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKI------GELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1220 QRHSQALVEMAEQLEQARRGKGVWEKTRL-----SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSER 1294
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLlaeieELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1295 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQME 1374
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1375 EEvvarERAGRELQSTQAQLSEWRRRQEEEAAVleageearrraareaetltqrlAEKTEAVERLERARRRLQQELDDAT 1454
Cdd:TIGR02169 466 KY----EQELYDLKEEYDRVEKELSKLQRELAE----------------------AEAQARASEERVRGGRAVEEVLKAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1455 VD--LGQQKQLLSTLEKKQrkfdqlLAEEKAAVLRA----VED----RERIEAEGREREARALSLTRALEEEQEAREELE 1524
Cdd:TIGR02169 520 IQgvHGTVAQLGSVGERYA------TAIEVAAGNRLnnvvVEDdavaKEAIELLKRRKAGRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1525 RQNRALRAELEalLSSKDDVGKN-----------VHELERARKAAEQA-ASDLRTQVTELEDELTAAEDAKLRLEVTVQA 1592
Cdd:TIGR02169 594 SEDGVIGFAVD--LVEFDPKYEPafkyvfgdtlvVEDIEAARRLMGKYrMVTLEGELFEKSGAMTGGSRAPRGGILFSRS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1593 LKAQHERdLQGRDDAGEERRRQLAKQLRDAEVERDEerkqralAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQ 1672
Cdd:TIGR02169 672 EPAELQR-LRERLEGLKRELSSLQSELRRIENRLDE-------LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1673 VQMKELWREVEETRSSRDEmftlsreNEKKLKGLEAEVLRLQEELAA-----SDRARRQAQQDRDEMAEEVASGNLSKAA 1747
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKE-------LEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1748 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHyrklvlqveslttelsaersfsakaesgRQQLERQIQELRARLGEEDA 1827
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ----------------------------IKSIEKEIENLNGKKEELEE 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1828 gararqkmLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQL 1907
Cdd:TIGR02169 869 --------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
890 900
....*....|....*....|....*....
gi 1039779964 1908 EEAEEEAS------RAQAGRRRLQRELED 1930
Cdd:TIGR02169 941 GEDEEIPEeelsleDVQAELQRVEEEIRA 969
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
878-1189 |
1.08e-10 |
|
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: 67.07 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 878 RAQELQKVQELQQQSAREVGElQGRVAQLEEERTRLAEQLRAEAElcSEAEETRARLAARKQELELVVTELEARVGEEEE 957
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAME--RERELERIRQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 958 CSRQLQSEKKRLQQHIQEleshlEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAA 1037
Cdd:pfam17380 379 ELERLQMERQQKNERVRQ-----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1038 EEEEKVKSLNKLRlKYEATISDMEDRLKKEEKGRQELEKLKRR-LDGESSELQEQMVEQKQRAEELLAQLgrkeDELQAA 1116
Cdd:pfam17380 454 EEQERQQQVERLR-QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLEKEM----EERQKA 528
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 1117 LLRAEEEggaraqllkslREAQAGLAEAQEDLEAERVARA--KAEKQRRDLgEELEALRGELEDTLDSTNAQQEL 1189
Cdd:pfam17380 529 IYEEERR-----------REAEEERRKQQEMEERRRIQEQmrKATEERSRL-EAMEREREMMRQIVESEKARAEY 591
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1249-1907 |
1.11e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1249 SLEAEVSELKAELSSLQTSRQEGEQKRRRLEsQLQEVQgrssdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLG 1328
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIE-LLEPIR-----------ELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1329 KELssAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMeeevvaRERAGRELQSTQAQLSEWRRRQEEeaavl 1408
Cdd:COG4913 290 LEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEE----- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1409 eageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDAtvdLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRA 1488
Cdd:COG4913 357 ----------------RERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1489 VEDRERIEAEGREREARALSLTRALEeeqeareelerqnrALRAELEALLSSKDD----VGK--NVHELERA-RKAAEQA 1561
Cdd:COG4913 418 RRELRELEAEIASLERRKSNIPARLL--------------ALRDALAEALGLDEAelpfVGEliEVRPEEERwRGAIERV 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1562 asdLRTQVTEL--EDELTAA-----EDAKLRLEVTVQALKAQHERDLQGRDDAG--------------EERRRQLAKQLR 1620
Cdd:COG4913 484 ---LGGFALTLlvPPEHYAAalrwvNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrAWLEAELGRRFD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1621 DAEVERDEERKQRALAMaarkkleleleelkaqtSAAGQGKEEAVKQLKKMQVQMKELWReveetrssrdemftLSRENE 1700
Cdd:COG4913 561 YVCVDSPEELRRHPRAI-----------------TRAGQVKGNGTRHEKDDRRRIRSRYV--------------LGFDNR 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1701 KKLKGLEAEVLRLQEELAASDRARRQAQQDRDemaeevasgnlskaaTLEEKRQLEGRLSQLEEELEEEQNnsellkdhy 1780
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDEIDVAS--------- 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1781 rkLVLQVESLTTELSAERSFSAKAEsgrqQLERQIQELRARLgEEDAGARARQKMLIAALESKLAQAEEQLEQ-----ES 1855
Cdd:COG4913 666 --AEREIAELEAELERLDASSDDLA----ALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDElqdrlEA 738
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1856 RERILSGKLVRRAEKRLKEVVLQvDEERRVADQVRDQLEKSNLRLKQLKRQL 1907
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
968-1506 |
1.30e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 968 RLQQHIQELES-HLEAEEGARQKLQLEKVTTEA-KMKKFEEDLLLLEDQNSKL-----SKERRLLEERLAEFSSQAAEEE 1040
Cdd:COG4913 229 ALVEHFDDLERaHEALEDAREQIELLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1041 EKVkslnklrlkyeatisdmeDRLKKEEKG-RQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1119
Cdd:COG4913 309 AEL------------------ERLEARLDAlREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1120 AEEEG-GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEdtldstnaqqELRSKR---EQ 1195
Cdd:COG4913 371 LGLPLpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA----------SLERRKsniPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1196 EVTELKKALEEESRAHEVSMQ------ELRQR------------HSQA---LVEmAEQLEQARR--------GKGVWEKT 1246
Cdd:COG4913 441 RLLALRDALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFAltlLVP-PEHYAAALRwvnrlhlrGRLVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1247 RLSLEAEVSE---------------------LKAELSSLQ-----TSRQEGEQKRRRLESQLQEVQGRSS----DSERAR 1296
Cdd:COG4913 520 RTGLPDPERPrldpdslagkldfkphpfrawLEAELGRRFdyvcvDSPEELRRHPRAITRAGQVKGNGTRhekdDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1297 SE------AAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKlalgsRVRALEAEAAGLR 1370
Cdd:COG4913 600 SRyvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1371 EQMEEEvvarERAGRELQSTQAQLSEWRRRQEEeaavleageearrraareaetLTQRLAEKTEAVERLerarrrlQQEL 1450
Cdd:COG4913 675 AELERL----DASSDDLAALEEQLEELEAELEE---------------------LEEELDELKGEIGRL-------EKEL 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 1451 DDATVDLGQQKQLLSTLEKKQRKFDQLLAEEK--AAVLRAVEDRERIEAEGREREARA 1506
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRA 780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1013-1221 |
1.31e-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: 65.56 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1013 DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQM 1092
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1093 VEQKQRAEELLAQLGRKEDELQAALLRAEEEGG--------------ARAQLLKSLREAQAGLAEAQEDLEAERVARAKA 1158
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLdavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779964 1159 EKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQR 1221
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
897-1755 |
1.37e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 897 GELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTelearvgeeeecSRQLQSEKKRLQQHIQEL 976
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT------------ALRQQEKIERYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 977 ESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFsSQAAEEEEKVKSLNKLRLKYEAT 1056
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQY-QQAVQALERAKQLCGLPDLTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1057 ISDMEDRLK-KEEKGRQELEKLKRRLDgesseLQEQMVEQKQRAEELLAQLGRKEDELQA-----ALLRAEEEGGARAQL 1130
Cdd:PRK04863 440 AEDWLEEFQaKEQEATEELLSLEQKLS-----VAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvarELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1131 LKSLReaqAGLAEAQEDLEAERVA-RAKAEKQRR-----DLGEELEALRGELEDTLDSTNAQQElrskreqEVTELKKAL 1204
Cdd:PRK04863 515 LQQLR---MRLSELEQRLRQQQRAeRLLAEFCKRlgknlDDEDELEQLQEELEARLESLSESVS-------EARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1205 EEESRAHEVSMQELRQRhSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQE 1284
Cdd:PRK04863 585 RQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1285 VQGRSSDSerarseaAEKLQRAQAELESVSTA-------LSEAESKAIRLG--------KELSSAESQL----------- 1338
Cdd:PRK04863 664 LSQPGGSE-------DPRLNALAERFGGVLLSeiyddvsLEDAPYFSALYGparhaivvPDLSDAAEQLagledcpedly 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1339 -------------HDTQEL-----LQEETRA-------KLALGSRvRALEAEAAGLREQMEEEVVARERAGRELQSTQ-- 1391
Cdd:PRK04863 737 liegdpdsfddsvFSVEELekavvVKIADRQwrysrfpEVPLFGR-AAREKRIEQLRAEREELAERYATLSFDVQKLQrl 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1392 ---------------------AQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR------------------LAEK 1432
Cdd:PRK04863 816 hqafsrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGlsalnrllprlnlladetLADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1433 TEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLlaeeKAAVLRAVEDRERIEAegrerEARALSltra 1512
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQ-----QAFALT---- 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1513 leeeqeareeLERQNRALRAELEA--LLSSKDDvgkNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTV 1590
Cdd:PRK04863 963 ----------EVVQRRAHFSYEDAaeMLAKNSD---LNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1591 QALKAQH---ERDLQG---RDDAGEE-----RRRQLAKQLRDAEVERDEERKQRALAMAARkkleleleelkaqtsaagq 1659
Cdd:PRK04863 1030 DAKRQMLqelKQELQDlgvPADSGAEeraraRRDELHARLSANRSRRNQLEKQLTFCEAEM------------------- 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1660 gkEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSREN--EKKLKGLEAEVLRLQEELAASDRAR---RQAQQDRDEM 1734
Cdd:PRK04863 1091 --DNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLHRRELAYLSADELRSMSDKALgalRLAVADNEHL 1168
|
970 980
....*....|....*....|.
gi 1039779964 1735 AEEVASgnLSKAATLEEKRQL 1755
Cdd:PRK04863 1169 RDVLRL--SEDPKRPERKVQF 1187
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
875-1346 |
2.78e-10 |
|
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: 65.53 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 875 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLA-EQLRAEAELCSEAEETRARLAARKQELELVVTELEARVG 953
Cdd:pfam05557 53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLnEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 954 EEEECSRQLQSEKKRLQQH---IQELESHLEAEEGARQKLQlekvTTEAKMKKFEEDLLLLEDQNSKLskerrlleERLA 1030
Cdd:pfam05557 133 ELEELQERLDLLKAKASEAeqlRQNLEKQQSSLAEAEQRIK----ELEFEIQSQEQDSEIVKNSKSEL--------ARIP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1031 EFSSQAAEEEEKVKSLNKLR---LKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQE-----QMVEQKQRAEEL 1102
Cdd:pfam05557 201 ELEKELERLREHNKHLNENIenkLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaQDTGLNLRSPED 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1103 LAqlGRKEDELQAALLRAEEEGGARAQLL---KSLREAQAGLAEAQEDLEAERVARAKAEKQRRDL-------GEELEAL 1172
Cdd:pfam05557 281 LS--RRIEQLQQREIVLKEENSSLTSSARqleKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvlllTKERDGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1173 RGELED-----TLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQaLVEMAEQLEQARRGKGVWEKTR 1247
Cdd:pfam05557 359 RAILESydkelTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQ-QAQTLERELQALRQQESLADPS 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1248 LSLEaEVSELKAELSSLQTSRQEGEQKRRRLESQL--QEVQGRS---------------SDSERARSEAAEKLQ------ 1304
Cdd:pfam05557 438 YSKE-EVDSLRRKLETLELERQRLREQKNELEMELerRCLQGDYdpkktkvlhlsmnpaAEAYQQRKNQLEKLQaeierl 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1305 -----RAQAELESV----STALSEAESKAIRLGKELSSAESQLHDTQELLQ 1346
Cdd:pfam05557 517 krllkKLEDDLEQVlrlpETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1020-1879 |
3.77e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1020 KERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRrLDGESSELQEQMVEQKQRA 1099
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDL-------EQDYQAASDHLNLVQTALRQQEKIER-YQADLEELEERLEEQNEVV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1100 EELLAQLgrkeDELQAALLRAEEEggaraqllksLREAQAGLAEAQEDLEAERvARAKAEKQRRDLGEELEALRGELEDT 1179
Cdd:PRK04863 372 EEADEQQ----EENEARAEAAEEE----------VDELKSQLADYQQALDVQQ-TRAIQYQQAVQALERAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1180 LDSTNAQQELRSKREQEVTELKKALEEESRAHevsmQELRQRHSQAL---------VEMAEQLEQARRGKGVWEKTRLsL 1250
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVA----QAAHSQFEQAYqlvrkiageVSRSEAWDVARELLRRLREQRH-L 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1251 EAEVSELKAELSSLQTSRQEgeqkRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAirlgke 1330
Cdd:PRK04863 512 AEQLQQLRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR------ 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1331 lssaeSQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQ---LSEWRRRQEEEAAV 1407
Cdd:PRK04863 582 -----MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERereLTVERDELAARKQA 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1408 LEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRlqqELDDA---------------TVDLGQQKQLLSTL----- 1467
Cdd:PRK04863 657 LDEEIERLSQPGGSEDPRLNALAERFGGVLLSEIYDDV---SLEDApyfsalygparhaivVPDLSDAAEQLAGLedcpe 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1468 -----EKKQRKFDQ--LLAEE-KAAVLRAVEDRE----RIEAE---GRE-REARALsltraleeeqeareelerqnrALR 1531
Cdd:PRK04863 734 dlyliEGDPDSFDDsvFSVEElEKAVVVKIADRQwrysRFPEVplfGRAaREKRIE---------------------QLR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1532 AELEALLSSKDDVGKNVHELERARKAA----------------EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKA 1595
Cdd:PRK04863 793 AEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1596 QHE--RDLQGR-----DDAGEERRRQLAKQLRDAEV-ERDEERKQRALAMAARKKleleleelkaqtsAAGQGKEEAVKQ 1667
Cdd:PRK04863 873 GLSalNRLLPRlnllaDETLADRVEEIREQLDEAEEaKRFVQQHGNALAQLEPIV-------------SVLQSDPEQFEQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1668 LKKMQVQMKELWREVeetrssRDEMFTLSRENEKKLK-GLEAEVLRLQEELAASDRAR---RQAQQDRDEMAEEVasgnl 1743
Cdd:PRK04863 940 LKQDYQQAQQTQRDA------KQQAFALTEVVQRRAHfSYEDAAEMLAKNSDLNEKLRqrlEQAEQERTRAREQL----- 1008
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1744 skaatleekRQLEGRLsqleeeleeeqnnsellkDHYRKLVLQVESlttelsaerSFSAKAESgRQQLERQIQEL--RAR 1821
Cdd:PRK04863 1009 ---------RQAQAQL------------------AQYNQVLASLKS---------SYDAKRQM-LQELKQELQDLgvPAD 1051
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1822 LGEEDAgARARQKMLIAAL---ESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQV 1879
Cdd:PRK04863 1052 SGAEER-ARARRDELHARLsanRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
898-1500 |
5.71e-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: 64.74 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 898 ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTE----------LEARVGEEEECSRQLQSEKK 967
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 968 RLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMK-KFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSL 1046
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1047 NKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSE----LQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEE 1122
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1123 EGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQ---------------- 1186
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKeveleelkkilaedek 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1187 ------------QELRSKrEQEVTELKKALEEESRAHEVSMQELR---QRHSQALVEMAEQLEQ---------ARRGKGV 1242
Cdd:pfam05483 420 lldekkqfekiaEELKGK-EQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELEKeklknieltAHCDKLL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1243 WEKTRLSLEAE--VSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEA 1320
Cdd:pfam05483 499 LENKELTQEASdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSI 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1321 ESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1400
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1401 QEEEAAVleageearrraareAETLTQRLAEKTEAVERLERARRRLQQELDDATvdlgQQK--QLLSTLEKKQRKFDQLL 1478
Cdd:pfam05483 659 YQKEIED--------------KKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC----QHKiaEMVALMEKHKHQYDKII 720
|
650 660
....*....|....*....|..
gi 1039779964 1479 aEEKAAVLRAVEDRERIEAEGR 1500
Cdd:pfam05483 721 -EERDSELGLYKNKEQEQSSAK 741
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
871-1263 |
6.57e-10 |
|
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: 63.76 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 871 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 950
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 951 RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLA 1030
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1031 EFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELqeqmveqkqraEELLAQLGRKE 1110
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL-----------SSMAAQRDRTQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1111 DELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDL------EAERVARAKAEKQRRD--LGEEL---EALRGELEDT 1179
Cdd:pfam07888 272 AELHQARLQAAQLTLQLADASLALREGRARWAQERETLqqsaeaDKDRIEKLSAELQRLEerLQEERmerEKLEVELGRE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1180 LDSTNAQqelRSKREQEVTELKKALEEESRAhevsmQELRQRHSQALVEMAEQLEQaRRGKGVWEKTRLSLEAEVSELKA 1259
Cdd:pfam07888 352 KDCNRVQ---LSESRRELQELKASLRVAQKE-----KEQLQAEKQELLEYIRQLEQ-RLETVADAKWSEAALTSTERPDS 422
|
....
gi 1039779964 1260 ELSS 1263
Cdd:pfam07888 423 PLSD 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1530-1951 |
1.21e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1530 LRAELEALLSSKDDVGKNVHELERAR-KAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAG 1608
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1609 EERRRQLAKQLRDAEVERDeERKQRALAMAarkkleleleelkAQTSAAGQGKEEAVKQLKKMQVQMKELwreVEETRSS 1688
Cdd:COG4913 337 GDRLEQLEREIERLERELE-ERERRRARLE-------------ALLAALGLPLPASAEEFAALRAEAAAL---LEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1689 RDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRAR----RQAQQDRDEMAEE--------------------------- 1737
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEAlgldeaelpfvgelievrpeeerwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1738 -------------VASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDH--YRKLVLQVESLTTELSAE--RSF 1800
Cdd:COG4913 480 iervlggfaltllVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAElgRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1801 S-AKAESGrQQLER---------QIQELRARlGEEDA----------GARARQKmlIAALESKLAQAEEQLEQ-ESRERI 1859
Cdd:COG4913 560 DyVCVDSP-EELRRhpraitragQVKGNGTR-HEKDDrrrirsryvlGFDNRAK--LAALEAELAELEEELAEaEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1860 LSGKL-----VRRAEKRLKEV------VLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQREL 1928
Cdd:COG4913 636 LEAELdalqeRREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500
....*....|....*....|...
gi 1039779964 1929 EDVTESAESMNREVTTLRNRLRR 1951
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEA 738
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1006-1842 |
2.47e-09 |
|
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: 62.66 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1006 EDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDgES 1085
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDL-------EQDYQAASDHLNLVQTALRQQEKIERYQE-DL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1086 SELQEQMVEQKQRAEELLAQLgrkeDELQAALLRAEEEggaraqllksLREAQAGLAEAQEDLEAERvARAKAEKQRRDL 1165
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQL----AEAEARLEAAEEE----------VDSLKSQLADYQQALDVQQ-TRAIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1166 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEeesraHEVSM-QELRQRHSQA---LVEMAEQLEQARrgkg 1241
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELE-----QKLSVaDAARRQFEKAyelVCKIAGEVERSQ---- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1242 VWEKTRLSLEaEVSELKAELSSLQTSRQEGEQKRRRLESQ------LQEVQGRSSDSERARSEAAEKLQRAQAELESVST 1315
Cdd:COG3096 493 AWQTARELLR-RYRSQQALAQRLQQLRAQLAELEQRLRQQqnaerlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1316 ALSEAESKAIRLGKELSSAESQ-------------LHDTQELLQEETRAKLAlgsrvraleaEAAGLREQMEEeVVARER 1382
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALERLREQSGEALA----------DSQEVTAAMQQ-LLERER 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1383 agrELQSTQAQLSEWRRRQEEEAAVLEAGEEARRraareaeTLTQRLAEKTEAVERLERARRRLqqeLDDATV------- 1455
Cdd:COG3096 641 ---EATVERDELAARKQALESQIERLSQPGGAED-------PRLLALAERLGGVLLSEIYDDVT---LEDAPYfsalygp 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1456 --------DLGQQKQLLSTL----------EKKQRKFDQLL---AEEKAAVLRAVEDRE----RIEAE---GRE-REARA 1506
Cdd:COG3096 708 arhaivvpDLSAVKEQLAGLedcpedlyliEGDPDSFDDSVfdaEELEDAVVVKLSDRQwrysRFPEVplfGRAaREKRL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1507 lsltraleeeqeareelerqnRALRAELEALLSSKDDVGKNVHELERARKAAEQ----------------AASDLRTQVT 1570
Cdd:COG3096 788 ---------------------EELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRS 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1571 ELEDELTAAEDAKLRLEVTVQALKAQHE--RDLQGR-----DDAGEERRRQLAKQLRDAEVERDEERKQRAlAMAARKKL 1643
Cdd:COG3096 847 ELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPQanllaDETLADRLEELREELDAAQEAQAFIQQHGK-ALAQLEPL 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1644 ELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELwREVEETR-----SSRDEMFTLSRE-NEKklkgLEAEVLRLQEEL 1717
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL-SEVVQRRphfsyEDAVGLLGENSDlNEK----LRARLEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1718 AASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKdhyrklvlqVESLTTELSAE 1797
Cdd:COG3096 1001 REAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIR---------RDELHEELSQN 1071
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1039779964 1798 RSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALES 1842
Cdd:COG3096 1072 RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1094-1334 |
3.66e-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: 60.93 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1094 EQKQRAEELLAQLGRKEDELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1173
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1174 GELEDTLDSTnAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQarrgkgvwekTRLSLEAE 1253
Cdd:COG4942 97 AELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA----------DLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1254 VSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSS 1333
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 1039779964 1334 A 1334
Cdd:COG4942 246 A 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1162-1964 |
4.53e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1162 RRDLGEELEALRGELeDTLDStnAQQELRSKREQevtelKKALEEESRAHEvSMQELRQRHS--QALVEMAeQLEQARRG 1239
Cdd:COG4913 220 EPDTFEAADALVEHF-DDLER--AHEALEDAREQ-----IELLEPIRELAE-RYAAARERLAelEYLRAAL-RLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1240 KGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRssdserARSEAAEKLQRAQAELESVSTALSE 1319
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1320 AESKAIRLGKELSSAESQLHDTQELLQEetraklalgsRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRR 1399
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAA----------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1400 RQ----EEEAAVLEAgeearrraareaetLTQRLAEKTEAVERLErarrrlqqELDDatVDLGQQK------QLLSTLek 1469
Cdd:COG4913 434 RKsnipARLLALRDA--------------LAEALGLDEAELPFVG--------ELIE--VRPEEERwrgaieRVLGGF-- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1470 kqrKFDqLLAEEK--AAVLRAVEDR--------ERIEAEGREREARAL---SLTRALEEEQEareelerqnrALRAELEA 1536
Cdd:COG4913 488 ---ALT-LLVPPEhyAAALRWVNRLhlrgrlvyERVRTGLPDPERPRLdpdSLAGKLDFKPH----------PFRAWLEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1537 LLSSKDDVGK--NVHELERARKAaeqaasdlrtqvteledeltaaedaklrleVTVQALkAQHERDLQGRDDAGEERRRQ 1614
Cdd:COG4913 554 ELGRRFDYVCvdSPEELRRHPRA------------------------------ITRAGQ-VKGNGTRHEKDDRRRIRSRY 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1615 L-----AKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAgqgkeEAVKQLKKMQVQMKELWREVEETRSSR 1689
Cdd:COG4913 603 VlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-----QRLAEYSWDEIDVASAEREIAELEAEL 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1690 DEMftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEE 1769
Cdd:COG4913 678 ERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1770 QNNSELLKDHYRKLvlqVESLTTELSAERsfsAKAESGRQQLERQIQELRAR-------LGEEDAGARARQKMLIAALES 1842
Cdd:COG4913 754 RFAAALGDAVEREL---RENLEERIDALR---ARLNRAEEELERAMRAFNREwpaetadLDADLESLPEYLALLDRLEED 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1843 KLAQAEEQLEQEsrerilsgkLVRRAEKRLKEVVLQVDEERRvadQVRDQLEKSNLRLKQLK----RQLEEAEEEASRAQ 1918
Cdd:COG4913 828 GLPEYEERFKEL---------LNENSIEFVADLLSKLRRAIR---EIKERIDPLNDSLKRIPfgpgRYLRLEARPRPDPE 895
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1919 AgrRRLQRELEDVTESAESMNRE--------VTTLRNRLRRGPLTFTTRTVRQV 1964
Cdd:COG4913 896 V--REFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEEEESDRRWRARV 947
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
904-1133 |
5.40e-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: 60.55 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 904 AQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEae 983
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 984 egaRQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRL--LEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDME 1061
Cdd:COG4942 101 ---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1062 DRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRaeelLAQLGRKEDELQAALLRAEEEGGARAQLLKS 1133
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
973-1351 |
6.19e-09 |
|
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: 61.13 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 973 IQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1052
Cdd:COG5185 161 IKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1053 YEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK--EDELQAALLRAEEEG------ 1124
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKiaEYTKSIDIKKATESLeeqlaa 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1125 -GARAQLLKSLREAQAGLAEAQEDLeaervarakaEKQRRDLGEELEALRGELE---DTLDSTNAQQELRSKrEQEVTEL 1200
Cdd:COG5185 321 aEAEQELEESKRETETGIQNLTAEI----------EQGQESLTENLEAIKEEIEnivGEVELSKSSEELDSF-KDTIEST 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1201 KKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGkgvWEKTRLSLEAEVSELKAELSSLQTSRQEGEQkrrrlES 1280
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQ---IEQATSSNEEVSKLLNELISELNKVMREADE-----ES 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1281 QLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRA 1351
Cdd:COG5185 462 QSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
871-1099 |
6.73e-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: 60.16 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 871 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 950
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 951 RVGE-EEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERL 1029
Cdd:COG4942 98 ELEAqKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1030 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRA 1099
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1111-1511 |
1.07e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1111 DELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA--ERVARAKAEKQRRDLGEELEALRGELEDT---LDSTNA 1185
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1186 QQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQ 1265
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1266 TSRQEGEQKRR--------RLESQLQEVQGRSSDSERARSEAAE--------------KLQRAQAELESVSTALSEAESK 1323
Cdd:COG4717 234 NELEAAALEERlkearlllLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1324 AIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAgRELQSTQAQlsewrrrQEE 1403
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVE-------DEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1404 EAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQ--QELDDATVDL----GQQKQLLSTLEKKQRKFDQL 1477
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELeeleEELEELREELAELEAELEQL 465
|
410 420 430
....*....|....*....|....*....|....
gi 1039779964 1478 LAEEKAAVLRAVEDRERIEAEGREREARALSLTR 1511
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
866-1347 |
1.24e-08 |
|
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: 60.52 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 866 LQVTRQDEVLQARAQELQKVQELQ-------QQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 938
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 939 QELELVVtelearvgeeEECSRQLQSEKKRLQQHIQELEsHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL 1018
Cdd:pfam15921 506 QEKERAI----------EATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1019 SKerrLLEERLAEFSSQAAEEEEKVKSLNKLRLKYE--ATISDMEDRLKKEEKGR-QELEKLKRRLDGESSELQEQMVEQ 1095
Cdd:pfam15921 575 TQ---LVGQHGRTAGAMQVEKAQLEKEINDRRLELQefKILKDKKDAKIRELEARvSDLELEKVKLVNAGSERLRAVKDI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1096 KQRAEELLAQLGRKEDELQA------ALLR-----AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRD 1164
Cdd:pfam15921 652 KQERDQLLNEVKTSRNELNSlsedyeVLKRnfrnkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1165 LGEELEALRGELEDTLDSTNAQQELRSKREQEvtelKKALEEESrahevsmQELRQRHSQALVE---MAEQLEQARRGKG 1241
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKE----KHFLKEEK-------NKLSQELSTVATEknkMAGELEVLRSQER 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1242 VWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQ----LQEVQG---RSSDSERARSEAAEKLQRAQAEL---E 1311
Cdd:pfam15921 801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQhtldVKELQGpgyTSNSSMKPRLLQPASFTRTHSNVpssQ 880
|
490 500 510
....*....|....*....|....*....|....*.
gi 1039779964 1312 SVSTALSEAESKAIRLgkelssAESQLHDTQELLQE 1347
Cdd:pfam15921 881 STASFLSHHSRKTNAL------KEDPTRDLKQLLQE 910
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
960-1404 |
1.50e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 960 RQLQSEKKRLQQhIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLED--QNSKLSKERRLLEERLAEFSSQAA 1037
Cdd:COG4717 71 KELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1038 EEEEKVKSLNKLRlkyeatiSDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAL 1117
Cdd:COG4717 150 ELEERLEELRELE-------EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1118 LRAEEE------GGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLG-------------EELEALRGELED 1178
Cdd:COG4717 223 EELEEEleqlenELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallfLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1179 TLDSTNAQQELRSKREQEVTELKKA--LEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSE 1256
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1257 LKAELSSLQTSRQEGEQKRRRLESQLQEVqgRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAES 1336
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQL--EELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 1337 QLHDtqellqeetrakLALGSRVRALEAEAAGLREQMEEEvvarERAGRELQSTQAQLSEWRRRQEEE 1404
Cdd:COG4717 461 ELEQ------------LEEDGELAELLQELEELKAELREL----AEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1029-1238 |
1.64e-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: 59.01 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1029 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQrAEELLAQLGR 1108
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1109 KEDELQAALLRAEEEGGARAQLL--KSLREAQAGLAEAQEDLEAERVAR--AKAEKQRRDLGEELEALRGELEDTLDSTN 1184
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1185 AQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARR 1238
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
868-1406 |
3.04e-08 |
|
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: 58.98 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 868 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRvaQLEEERTRLAeQLRaeaelcSEAEETRARLAARKQELELVVTE 947
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR--QLSDLESTVS-QLR------SELREAKRMYEDKIEELEKQLVL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 948 LEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEgarQKLQLEKvttEAKMKKFEEDL----------LLLEDQNSK 1017
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE---KELSLEK---EQNKRLWDRDTgnsitidhlrRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1018 LSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgESSElqeqmveqkQ 1097
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL--ESSE---------R 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1098 RAEELLAQLGRKEDELQAA---LLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRG 1174
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATnaeITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1175 ELEDTLDSTNAQQELRSKREQEVTELKKALEE---ESRAHEVSMQELRQRHSQALVEMAEQL----EQARRGKGVwEKTR 1247
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLELEKVKLVnagsERLRAVKDI-KQER 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1248 LSLEAEVSELKAELSSLQtsrQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL 1327
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLS---EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 1328 GKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQlsewRRRQEEEAA 1406
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ----ERRLKEKVA 807
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1061-1313 |
4.43e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1061 EDRLKKEEKGRQELEKLKRRLDGESSELQEQ-----MVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLR 1135
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERrealqRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1136 EAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSM 1215
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1216 QELRQRHSQALVEMAEQLEQARRgkgVWEKTRLSLEAEVSEL---KAELSSLQTS---RQEGEQKRRRLESQLQEVQGRS 1289
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNR---EWPAETADLDADLESLpeyLALLDRLEEDglpEYEERFKELLNENSIEFVADLL 852
|
250 260
....*....|....*....|....
gi 1039779964 1290 SDSERARSEAAEKLQRAQAELESV 1313
Cdd:COG4913 853 SKLRRAIREIKERIDPLNDSLKRI 876
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
872-1236 |
7.43e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 872 DEVLQARAQ------ELQKVQELQQQSAREVGELQGRVAQLEEER-------------TRLAEQL-RAEAELcseaEETR 931
Cdd:PRK04863 286 EEALELRRElytsrrQLAAEQYRLVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIeRYQADL----EELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 932 ARLAARKQELELV---VTELEARVGEEEECSRQLQSEKKRLQQHIQELESH-------LEAEEGARQKLQLEKVTTEakm 1001
Cdd:PRK04863 362 ERLEEQNEVVEEAdeqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaVQALERAKQLCGLPDLTAD--- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1002 kKFEEDLLLLEDQNSKLSKERRLLEERLAeFSSQAAEEEEKVKSLNKlrlkyeaTISDMEDRLKKEEKGRQELEKLK--R 1079
Cdd:PRK04863 439 -NAEDWLEEFQAKEQEATEELLSLEQKLS-VAQAAHSQFEQAYQLVR-------KIAGEVSRSEAWDVARELLRRLReqR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1080 RLDGESSELQ------EQMVEQKQRAEELLAQLGRK-------EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQE 1146
Cdd:PRK04863 510 HLAEQLQQLRmrlselEQRLRQQQRAERLLAEFCKRlgknlddEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1147 DLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTnaqqelrskreQEVTELKKALEEESRAHEVSMQELRQRhSQAL 1226
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-----------QDVTEYMQQLLERERELTVERDELAAR-KQAL 657
|
410
....*....|
gi 1039779964 1227 VEMAEQLEQA 1236
Cdd:PRK04863 658 DEEIERLSQP 667
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
914-1633 |
8.39e-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: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 914 AEQLRAEAELCSE-AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQhiqeleshleaeegaRQKLQL 992
Cdd:TIGR00618 196 AELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE---------------QLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 993 EKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLeerlaefssQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQ 1072
Cdd:TIGR00618 261 LLKQLRARIEELRAQEAVLEETQERINRARKAA---------PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1073 ELEKlkrrlDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGG---ARAQLLKSLREAQAGLAEAQEDLE 1149
Cdd:TIGR00618 332 AHVK-----QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihTLQQQKTTLTQKLQSLCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1150 AERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEM 1229
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1230 AEQLEQARRGKGVWEKTRL----SLEAEVSELKAELSSLQTSR-QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQ 1304
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPlcgsCIHPNPARQDIDNPGPLTRRmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1305 RAQAELESVSTALSEAESKAIRLGKELssaESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAG 1384
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNIT---VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1385 RELQSTQAQLSEWRRRQEEEAAvleageearrraareaeTLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLL 1464
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHAL-----------------SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1465 STLEKKQRKFDQLLAEEKAAVLRAVEDRErieaegREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDV 1544
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLA------AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1545 GKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLakqlrdaev 1624
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL--------- 851
|
....*....
gi 1039779964 1625 ERDEERKQR 1633
Cdd:TIGR00618 852 LKYEECSKQ 860
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
927-1285 |
1.07e-07 |
|
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: 56.83 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 927 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLeaeegarQKLQLEKVTTEAKMKKFEE 1006
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV-------AELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1007 DLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGE-- 1084
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlq 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1085 ---------SSELQEQMVEQKQRAEELLaQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1155
Cdd:pfam07888 182 qteeelrslSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1156 AKAEKQRRDLGEELEALRGELEDT----LDSTNAQQELRSKREQEVTELKKALE----------EESRAHEVSMQELRQR 1221
Cdd:pfam07888 261 SSMAAQRDRTQAELHQARLQAAQLtlqlADASLALREGRARWAQERETLQQSAEadkdrieklsAELQRLEERLQEERME 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1222 HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEV 1285
Cdd:pfam07888 341 REKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
882-1221 |
1.14e-07 |
|
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: 57.29 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 882 LQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQ 961
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 962 --LQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NSKLSKERRLLEERLAEFSSQAA 1037
Cdd:pfam02463 725 drVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEreKTEKLKVEEEKEEKLKAQEEELR 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1038 EEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAL 1117
Cdd:pfam02463 805 ALEEELKEEAELLEEEQLLIEQEEKIKEEELE-ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1118 LRAEEEG----GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSK 1192
Cdd:pfam02463 884 LKDELESkeekEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
330 340
....*....|....*....|....*....
gi 1039779964 1193 REQEVTELKKALEEESRAHEVSMQELRQR 1221
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1185-1599 |
1.70e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1185 AQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELK------ 1258
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEeleerl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1259 AELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERAR-SEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQ 1337
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1338 LHDTQELLQ-EETRAKLALGSRVRALEAEAAGLREQMEE--------------EVVARERAGRELQSTQAQLSEWRRRQE 1402
Cdd:COG4717 236 LEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1403 EEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELddatvdlgQQKQLLSTLEKKQRKFDQLLAEEK 1482
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--------QLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1483 AAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRA--LRAELEALLSSKDDVGKNVHELERARKAAE- 1559
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEELEELREELAELEAELEQLEe 467
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1039779964 1560 -QAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHER 1599
Cdd:COG4717 468 dGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1052 |
1.84e-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: 55.54 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 867 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEE----RTRLAEQLRAEAELCSEAE-------ETRARLA 935
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPlalllspEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 936 ARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQN 1015
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039779964 1016 SKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1052
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1060-1790 |
2.31e-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: 56.39 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1060 MEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAllraeeeggaRAQLLKSLREAQA 1139
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK----------RDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1140 GLAEAQEDLEA----------ERVARAKAEKQRRDL-GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEES 1208
Cdd:pfam12128 316 AVAKDRSELEAledqhgafldADIETAAADQEQLPSwQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1209 RAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAE-----VSELKAELSSLQTSRQEGEQKRrrlesQLQ 1283
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksrLGELKLRLNQATATPELLLQLE-----NFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1284 EVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHdtqellqeeTRAKLALGSRVRALE 1363
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE---------LQLFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1364 AEAAGLREQMEEeVVARERAGRelqsTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERAR 1443
Cdd:pfam12128 542 KEAPDWEQSIGK-VISPELLHR----TDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1444 RRLQQELDDAtvdlgqqkqlLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGR-EREARALSLTRALEEEQEAREE 1522
Cdd:pfam12128 617 REKQAAAEEQ----------LVQANGELEKASREETFARTALKNARLDLRRLFDEKQsEKDKKNKALAERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1523 LERQNRALRAELEALLSS-KDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRlevtvqALKAQHERDL 1601
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEqKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK------ALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1602 QGRDdAGEERRRQLAKQLRD--AEVERDEERKQRALAMAA--RKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE 1677
Cdd:pfam12128 761 ASLG-VDPDVIAKLKREIRTleRKIERIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1678 LWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQE----ELAASDRARRQAQQDRDEMAEEVASGNLSK------AA 1747
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEdansEQAQGSIGERLAQLEDLKLKRDYLSESVKKyvehfkNV 919
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1039779964 1748 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESL 1790
Cdd:pfam12128 920 IADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQW 962
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
867-1263 |
2.37e-07 |
|
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: 55.90 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 867 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRA----EAELCSEaEETRARLAARKQELe 942
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRikelEFEIQSQ-EQDSEIVKNSKSEL- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 943 LVVTELEA---RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQK---LQLEKVTTEAKMK---KFEEDLLLLED 1013
Cdd:pfam05557 197 ARIPELEKeleRLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaatLELEKEKLEQELQswvKLAQDTGLNLR 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1014 QNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRL------------ 1081
Cdd:pfam05557 277 SPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvllltkerd 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1082 -----------DGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLrEAQAGLAEAQEDLEA 1150
Cdd:pfam05557 357 gyrailesydkELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL-ERELQALRQQESLAD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1151 ERVARAKAEKQRRDLgEELEALRGELE---DTLDSTNAQQELRSKREQ---EVTELKKALEEESRAHEVSMQELRQRHSQ 1224
Cdd:pfam05557 436 PSYSKEEVDSLRRKL-ETLELERQRLReqkNELEMELERRCLQGDYDPkktKVLHLSMNPAAEAYQQRKNQLEKLQAEIE 514
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1039779964 1225 ALVEMAEQLEQARRGKGVWEKTRLSL-EAEVSELKAELSS 1263
Cdd:pfam05557 515 RLKRLLKKLEDDLEQVLRLPETTSTMnFKEVLDLRKELES 554
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
963-1403 |
4.76e-07 |
|
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: 55.13 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 963 QSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEk 1042
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIE---LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1043 vksLNKLRLKYEATISdmeDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEEL---LAQLGRKEDELQAALLR 1119
Cdd:pfam05557 77 ---LNRLKKKYLEALN---KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTnseLEELQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1120 AEEEGGARAQLLKSLREAQAGLAEAQEDLE-----AERVARAKAEKQR-RDLGEELEALRGELEdTLDSTNAQQELrskR 1193
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQsqeqdSEIVKNSKSELARiPELEKELERLREHNK-HLNENIENKLL---L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1194 EQEVTELKKALE--EESRAHEVSMqELRQRHSQALVEMAEQLEQ-----------ARRGKGVWEKTRLSLEAEVSELKAE 1260
Cdd:pfam05557 227 KEEVEDLKRKLEreEKYREEAATL-ELEKEKLEQELQSWVKLAQdtglnlrspedLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1261 LSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSErarsEAAEKLQRA-----------QAELESVSTALSEAESkAIRLGK 1329
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHK----ALVRRLQRRvllltkerdgyRAILESYDKELTMSNY-SPQLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1330 ELSSAESQLHDTQeLLQEETRAKL--------ALGSRVRALEAEAAGLREQMEEEVVARERAG-----RELQSTQAQLSE 1396
Cdd:pfam05557 381 RIEEAEDMTQKMQ-AHNEEMEAQLsvaeeelgGYKQQAQTLERELQALRQQESLADPSYSKEEvdslrRKLETLELERQR 459
|
....*..
gi 1039779964 1397 WRRRQEE 1403
Cdd:pfam05557 460 LREQKNE 466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1252-1487 |
4.91e-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: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1252 AEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvstalsEAESKAIRLGKEL 1331
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1332 SSAESQLHDTQELLQEETRAKLALGSR------VRALEAEAAGLREQMEEEVV-ARERAGRELQSTQAQLSEWRRRQEEE 1404
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLApARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1405 AAVLEAGEEARRRAAReaeTLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAA 1484
Cdd:COG4942 173 RAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1039779964 1485 VLR 1487
Cdd:COG4942 250 ALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
869-1127 |
5.73e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 869 TRQDEVLQARAQELQkvqelqqqsaREVGELQGRVAQLEEERTRLAEQLRAEAELCS---------EAEETRARLAARKQ 939
Cdd:COG4913 609 RAKLAALEAELAELE----------EELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 940 ELEL---VVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQklQLEKVTTEAKMKKFEEDLLLLEDQNS 1016
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD--ELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1017 KLSKE------RRLLEERLAEFSSQAAEEEEK-VKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRrldgesselq 1089
Cdd:COG4913 757 AALGDaverelRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE---------- 826
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039779964 1090 EQMVEQKQRAEELLAQL-GRKEDELQAALLRAEEEGGAR 1127
Cdd:COG4913 827 DGLPEYEERFKELLNENsIEFVADLLSKLRRAIREIKER 865
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1035-1311 |
6.40e-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: 54.74 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1035 QAAEEEEKVKSlNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSelQEQMVEQKQRAEELLAQLGRKEDELQ 1114
Cdd:pfam17380 288 QQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMERERELERIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1115 AALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGE---ELEALRGELEDTldstnAQQELRS 1191
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-----RQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1192 KREQEVTELKKA-LEEESRAHEvsMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSslqtsrqE 1270
Cdd:pfam17380 440 LEEERAREMERVrLEEQERQQQ--VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI-------E 510
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039779964 1271 GEQKRRRLESQLQEVQGRSSDSERARSeaAEKLQRAQAELE 1311
Cdd:pfam17380 511 EERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEME 549
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1006-1707 |
7.24e-07 |
|
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: 54.59 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1006 EDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEeeKVKSLNKLRLKYEATISDMEDRLKK----EEKGRQELEKLKRRL 1081
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC--MPDTYHERKQVLEKELKHLREALQQtqqsHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1082 DGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQ 1161
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1162 RRDLGEE---LEALRGELEDTLDSTNAQQELRSKREQEVTELK--KALEEESRAHEVSMQELRQ-----RHSQALVEMAE 1231
Cdd:TIGR00618 337 QSSIEEQrrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKeldilQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1232 QLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTS--------RQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKL 1303
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1304 QRAQAELESVSTALSEAESKAIRLGkelssaesQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEvvaRERA 1383
Cdd:TIGR00618 497 LELQEEPCPLCGSCIHPNPARQDID--------NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL---KEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1384 GRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQkQL 1463
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA-LK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1464 LSTLEKKQRKFDQLLAEEKAAVLRAVEDR--ERIEAEGREREARALSLTraleeeqEAREELERQNRALRAELEALLSSK 1541
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLT-------YWKEMLAQCQTLLRELETHIEEYD 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1542 ddvgKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRd 1621
Cdd:TIGR00618 718 ----REFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR- 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1622 aevERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQL----KKMQVQMKELWREVEETRSSRDEMFTLSR 1697
Cdd:TIGR00618 793 ---LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRleekSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
730
....*....|
gi 1039779964 1698 ENEKKLKGLE 1707
Cdd:TIGR00618 870 KIIQLSDKLN 879
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1181-1402 |
7.79e-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: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1181 DSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSqaLVEMAEQLEQarrgkgvwektrlsLEAEVSELKAE 1260
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKL--------------LLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1261 LSSLQTSRQEGEQKRRRLESQLQEVQGRSSD--SERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQl 1338
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ- 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1339 hdtqeLLQEETRAKLALGSRVRALEAEAAGLREQMEEevvARERAgRELQSTQAQLSEWRRRQE 1402
Cdd:COG3206 307 -----LQQEAQRILASLEAELEALQAREASLQAQLAQ---LEARL-AELPELEAELRRLEREVE 361
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
872-1123 |
8.06e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.16 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 872 DEVLQArAQELQKVQ--ELQQQSAREVGelqGRVAQLEEERTRLAEQLRAEAELCSEAEETR-----ARLAARKQELELV 944
Cdd:PRK05771 19 DEVLEA-LHELGVVHieDLKEELSNERL---RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvKSLEELIKDVEEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 945 VTELEARVGEEEECSRQLQSEKKRLQQHIQELE---------------SHLEAEEGARQKLQLEKVTTEAKMKKFEE--- 1006
Cdd:PRK05771 95 LEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYist 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1007 ----DLLLLEDQNSKLSKERRLLEErlAEFSSQAAEEEEKVKSLnklrlkyeatISDMEDRLKKEEKGRQ----ELEKLK 1078
Cdd:PRK05771 175 dkgyVYVVVVVLKELSDEVEEELKK--LGFERLELEEEGTPSEL----------IREIKEELEEIEKEREslleELKELA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 1079 RRLDGESSELQEQMVEQKQRAEELLAQLG-------------RKEDELQAALLRAEEE 1123
Cdd:PRK05771 243 KKYLEELLALYEYLEIELERAEALSKFLKtdktfaiegwvpeDRVKKLKELIDKATGG 300
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1167-1878 |
8.83e-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: 54.46 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1167 EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWE-K 1245
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1246 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAeskAI 1325
Cdd:pfam12128 331 HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREA---RD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1326 RLGKELSSA----ESQLHDTQ-----ELLQEETRAKLALGS-RVRALEAEAAG-LREQMEEEVVARERAGRELQSTQAQL 1394
Cdd:pfam12128 408 RQLAVAEDDlqalESELREQLeagklEFNEEEYRLKSRLGElKLRLNQATATPeLLLQLENFDERIERAREEQEAANAEV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1395 SewrRRQEEEAAvleageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDATVDL-GQQKQLLSTLEKKQRK 1473
Cdd:pfam12128 488 E---RLQSELRQ------------------ARKRRDQASEALRQASRRLEERQSALDELELQLfPQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1474 FDQLLAE--EKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVgknvheL 1551
Cdd:pfam12128 547 WEQSIGKviSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREK------Q 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1552 ERARKAAEQAASDLRTQVTELEDELTAAEDAKL---RLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEverde 1628
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD----- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1629 eRKQRALamaarkkleleleelkaqtsaagqgKEEAVKQLKKMQVQMKELWREVEETRSSrdemftlsrenekKLKGLEA 1708
Cdd:pfam12128 696 -KKHQAW-------------------------LEEQKEQKREARTEKQAYWQVVEGALDA-------------QLALLKA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1709 EVLRLQEELAASDRARRQaQQDRDEMAEEVASGNLSKAATleEKRQLEGRLSQLEEELEEEQNNSELLKDHYR----KLV 1784
Cdd:pfam12128 737 AIAARRSGAKAELKALET-WYKRDLASLGVDPDVIAKLKR--EIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1785 LQVESLTTELSAER----SFSAKAESGRQQLERQIQELRA---RLGEEDAGARARQKMLIaalESKLAQAEEQLEQESRE 1857
Cdd:pfam12128 814 TQLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASEKqqvRLSENLRGLRCEMSKLA---TLKEDANSEQAQGSIGE 890
|
730 740
....*....|....*....|.
gi 1039779964 1858 RILSGKLVRRAEKRLKEVVLQ 1878
Cdd:pfam12128 891 RLAQLEDLKLKRDYLSESVKK 911
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
870-1400 |
1.30e-06 |
|
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: 53.80 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 870 RQDEVLQARAQELQKvqELQQQSAREVG---ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL--- 943
Cdd:COG3096 525 EQRLRQQQNAERLLE--EFCQRIGQQLDaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArap 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 944 -------VVTELEARVGEEEECSRQLQSEKKRLQQHIQELEshLEAEEGARQKLQLEKVTTEAKMKKFEED--LLLLEDq 1014
Cdd:COG3096 603 awlaaqdALERLREQSGEALADSQEVTAAMQQLLEREREAT--VERDELAARKQALESQIERLSQPGGAEDprLLALAE- 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1015 nsklskerRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEdRLKKEEKGRQE-------LEKLKRRLDGESSE 1087
Cdd:COG3096 680 --------RLGGVLLSEIYDDVTLEDAPYFSALYGPARHAIVVPDLS-AVKEQLAGLEDcpedlylIEGDPDSFDDSVFD 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1088 LQEQ----MVEQKQRAEEL-----LAQLGRKEDELQAALLRAEEEGGAR--AQLLKSLREAQAgLAEAQEDLEAERVARA 1156
Cdd:COG3096 751 AEELedavVVKLSDRQWRYsrfpeVPLFGRAAREKRLEELRAERDELAEqyAKASFDVQKLQR-LHQAFSQFVGGHLAVA 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1157 KAEkqrrDLGEELEAL---RGELEDTLDSTNAQ-QELRSKREQ---EVTELKKALeeeSRAHEVSMQELRQRhSQALVEM 1229
Cdd:COG3096 830 FAP----DPEAELAALrqrRSELERELAQHRAQeQQLRQQLDQlkeQLQLLNKLL---PQANLLADETLADR-LEELREE 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1230 AEQLEQARRGKGVWEKTRLSLEAEVSELK---AELSSLQTSRQEGEQKRRRLESQ---LQEVQGRS-----SDSERARSE 1298
Cdd:COG3096 902 LDAAQEAQAFIQQHGKALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQifaLSEVVQRRphfsyEDAVGLLGE 981
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1299 AA-------EKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEAAGLR 1370
Cdd:COG3096 982 NSdlneklrARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAeAEERARIRR 1061
|
570 580 590
....*....|....*....|....*....|....
gi 1039779964 1371 EQMEEEVVA----RERAGRELQSTQAQLSEWRRR 1400
Cdd:COG3096 1062 DELHEELSQnrsrRSQLEKQLTRCEAEMDSLQKR 1095
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1661-1951 |
1.40e-06 |
|
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: 53.53 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1661 KEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAasdrarRQAQQDRDEMAEEVAS 1740
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ------LRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1741 GNLSKAATLEEKRQLEGRLSQleeeleeeqnnselLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRA 1820
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAK--------------LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1821 RLGEEDAGARArqkmliaaLESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRL 1900
Cdd:TIGR02169 372 ELEEVDKEFAE--------TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1901 KQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1951
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
865-1243 |
1.87e-06 |
|
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: 52.84 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 865 LLQVTRQDEVLQARAQELQKVQELQQQSARE------VGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 938
Cdd:pfam09731 72 VSAVTGESKEPKEEKKQVKIPRQSGVSSEVAeeekeaTKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 939 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NS 1016
Cdd:pfam09731 152 KDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHldNV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1017 KLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQK 1096
Cdd:pfam09731 232 EEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1097 QRAEELLAQlgrkedelqaallRAEEEGGARAQLLKSLREAQAgLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1176
Cdd:pfam09731 312 KHIERALEK-------------QKEELDKLAEELSARLEEVRA-ADEAQLRLEFEREREEIRESYEEKLRTELERQAEAH 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1177 EDTLDSTNAQQELRSKREQEvTELKKALEEESRAHEVSMQELRQR---HSQALVEMAEQLEQARRGKGVW 1243
Cdd:pfam09731 378 EEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENRKAQQLW 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1290-1508 |
2.45e-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: 52.07 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1290 SDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGL 1369
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1370 REQMEEEVVARERAGR----ELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRR 1445
Cdd:COG4942 103 KEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779964 1446 LQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1508
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1024-1313 |
2.45e-06 |
|
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: 52.72 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1024 LLEERLAEFSSQAAEEEEkvksLNKLRLKyeATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1103
Cdd:pfam05667 208 LLERNAAELAAAQEWEEE----WNSQGLA--SRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1104 AQLGRKEDELQA-----------ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA--ERVARAKAEKQRrdLGEELE 1170
Cdd:pfam05667 282 SSFSGSSTTDTGltkgsrfthteKLQFTNEAPAATSSPPTKVETEEELQQQREEELEElqEQLEDLESSIQE--LEKEIK 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1171 ALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAhEVSMQELR---QRHSQALVEMAEQleqarrgkgvWEKTR 1247
Cdd:pfam05667 360 KLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDA-EENIAKLQalvDASAQRLVELAGQ----------WEKHR 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779964 1248 LSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVqgrssdSERARSeAAEKLQRAQAELESV 1313
Cdd:pfam05667 429 VPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEV------AEEAKQ-KEELYKQLVAEYERL 487
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
863-1175 |
2.46e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 863 KPLLQVTRQDEVLQARAQElqKVQELQQQSAREVGELQG---RVAQLEEERT-RLAEQLRAEAELCSEAEETRARLAARK 938
Cdd:pfam02029 27 EPSGQVTESVEPNEHNSYE--EDSELKPSGQGGLDEEEAfldRTAKREERRQkRLQEALERQKEFDPTIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 939 QELELV----------VTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLE----KVTTEAKMKKF 1004
Cdd:pfam02029 105 ENNEEEensswekeekRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVptenFAKEEVKDEKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1005 EEDLLLLEDQNSKLSKERRLLEERlaefSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGE 1084
Cdd:pfam02029 185 KKEKKVKYESKVFLDQKRGHPEVK----SQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1085 SSELQEQMVEQKQRAEELLAQLGRKEDELQAalLRAEEEggaraqllkslreaqaglaeaQEDLEAERVARAKAEKQRRD 1164
Cdd:pfam02029 261 ESEEFEKLRQKQQEAELELEELKKKREERRK--LLEEEE---------------------QRRKQEEAERKLREEEEKRR 317
|
330
....*....|.
gi 1039779964 1165 LGEELEALRGE 1175
Cdd:pfam02029 318 MKEEIERRRAE 328
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
866-1401 |
2.65e-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: 52.74 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 866 LQVTRQDEVLQARAQELQKVQELQQQSAREVGELQ------GRVAQLEEER-TRLAEQLRAEAELCSEAEETRARLAarK 938
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRdekkglGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRIL--E 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 939 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVT-------TEAKMKKFEE----- 1006
Cdd:TIGR00606 476 LDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmemlTKDKMDKDEQirkik 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1007 ----DLLL-----------LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKK---EE 1068
Cdd:TIGR00606 556 srhsDELTsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgSQ 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1069 KGRQELEKLKRRLDGES---------SELQEQMVEQK-----------QRAEELLAQLGRKEDELQAALLRAEEEGGARA 1128
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSkqramlagaTAVYSQFITQLtdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTE 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1129 QLLKSL---REAQAGLAEAQEDLEAERVARAKAEKQR-RDLGEELEALRGELEDT---LDSTNAQQELRSKREQEVT--- 1198
Cdd:TIGR00606 716 SELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEEQetlLGTIMPEEESAKVCLTDVTime 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1199 ELKKALEEESRAHE------------VSMQELRQR---HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1263
Cdd:TIGR00606 796 RFQMELKDVERKIAqqaaklqgsdldRTVQQVNQEkqeKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1264 LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE------AAEKLQRAQAEL-ESVSTALSEAESKAIRLGKELSSAES 1336
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHG 955
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 1337 QLHDTQELLQEETRAKLalgsrvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1401
Cdd:TIGR00606 956 YMKDIENKIQDGKDDYL------KQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
860-1101 |
2.90e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 860 IKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERtrlaeqlraeaelcSEAEETRARLAARKQ 939
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL--------------DELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 940 ELEL-VVTELEARVGEEEECSRQ---LQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteakmKKFEEDLLLLEDQN 1015
Cdd:PRK03918 581 ELGFeSVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETE-------KRLEELRKELEELE 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1016 SKLSKER-RLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDgESSELQEQMVE 1094
Cdd:PRK03918 654 KKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKK 732
|
....*..
gi 1039779964 1095 QKQRAEE 1101
Cdd:PRK03918 733 YKALLKE 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1022-1204 |
3.77e-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: 50.31 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1022 RRLLEerLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMveqkQRAEE 1101
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----KKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1102 LLAQlGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLD 1181
Cdd:COG1579 81 QLGN-VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|...
gi 1039779964 1182 stnaqqELRSKREQEVTELKKAL 1204
Cdd:COG1579 160 ------ELEAEREELAAKIPPEL 176
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
935-1363 |
3.80e-06 |
|
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: 51.95 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 935 AARKQELE---LVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGArqKLQLEKVTTEAKMKKfeedllll 1011
Cdd:pfam05701 28 AHRIQTVErrkLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEEL--KLNLERAQTEEAQAK-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1012 edQNSKLSKER-RLLEERLAEFSSQAAEEEEKVkslnkLRLKYEATISDMedRLKKEEKG--RQELEKLKRRLDGESSEL 1088
Cdd:pfam05701 98 --QDSELAKLRvEEMEQGIADEASVAAKAQLEV-----AKARHAAAVAEL--KSVKEELEslRKEYASLVSERDIAIKRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1089 QEQMVEQKQ---RAEELLAQLGRKEDEL---QAALLRAEEE--GGARA------QLLKSLREAQAGLAEAQEDLEAERVA 1154
Cdd:pfam05701 169 EEAVSASKEiekTVEELTIELIATKESLesaHAAHLEAEEHriGAALAreqdklNWEKELKQAEEELQRLNQQLLSAKDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1155 RAKAEKQRR---DLGEELEA---------LRGELEDTLDSTNAQQELRSKREqEVTELKKALEEES------RAHEVSMQ 1216
Cdd:pfam05701 249 KSKLETASAlllDLKAELAAymesklkeeADGEGNEKKTSTSIQAALASAKK-ELEEVKANIEKAKdevnclRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1217 ELRQRHSQALVEMaeqleqaRRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEvqgrssdserAR 1296
Cdd:pfam05701 328 SELEKEKAELASL-------RQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQ----------AA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 1297 SEAAEKLQRAQAELESVSTALSEAE-SKAirlgkELSSAESQLHDTQ-ELLQEETRAKLALGSrVRALE 1363
Cdd:pfam05701 391 QEAEEAKSLAQAAREELRKAKEEAEqAKA-----AASTVESRLEAVLkEIEAAKASEKLALAA-IKALQ 453
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1041-1317 |
4.23e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.07 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1041 EKVKSLnklrlkyEATISDMEDRLK-KEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1119
Cdd:pfam00038 18 DKVRFL-------EQQNKLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1120 AEEEGGARaqllkslREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELED--------------------- 1178
Cdd:pfam00038 91 YEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevrelqaqvsdtqvnvemdaa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1179 -TLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRgkgvwekTRLSLEAEVSEL 1257
Cdd:pfam00038 164 rKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRR-------TIQSLEIELQSL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779964 1258 KAELSSLQTSRQEGEQkrrRLESQLQEVQGRSSDSERARSEAAEKLQRAQAE---LESVSTAL 1317
Cdd:pfam00038 237 KKQKASLERQLAETEE---RYELQLADYQELISELEAELQETRQEMARQLREyqeLLNVKLAL 296
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
873-1396 |
4.24e-06 |
|
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: 52.26 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 873 EVLQARA-------QELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVV 945
Cdd:COG3096 406 DVQQTRAiqyqqavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 946 TELEArvGEEEECSRQL---QSEKKRLQQHIQELESHL-EAEEGARQKLQLEKVTTE--AKMKKFEEDLLLLEDQNSKLs 1019
Cdd:COG3096 486 GEVER--SQAWQTARELlrrYRSQQALAQRLQQLRAQLaELEQRLRQQQNAERLLEEfcQRIGQQLDAAEELEELLAEL- 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1020 kerrllEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLkRRLDGESSELQEQMVEQKQRA 1099
Cdd:COG3096 563 ------EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL-REQSGEALADSQEVTAAMQQL 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1100 EELLAQLGRKEDELQAALLRAEEE-------GGARAQLLKSLREAQAG--LAEAQEDLEAE-------RVARAKAEKQRR 1163
Cdd:COG3096 636 LEREREATVERDELAARKQALESQierlsqpGGAEDPRLLALAERLGGvlLSEIYDDVTLEdapyfsaLYGPARHAIVVP 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1164 DLGEELEALRGeLEDTL--------------DSTNAQQEL-------------------------RSKREQEVTELKKAL 1204
Cdd:COG3096 716 DLSAVKEQLAG-LEDCPedlyliegdpdsfdDSVFDAEELedavvvklsdrqwrysrfpevplfgRAAREKRLEELRAER 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1205 EEESRAHEVSMQELR--QRHSQALVE-MAEQLEQARRGKGvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQ 1281
Cdd:COG3096 795 DELAEQYAKASFDVQklQRLHQAFSQfVGGHLAVAFAPDP--EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQ 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1282 LQEVQGRSS-------DSERARSEAAE----KLQRAQAELESVSTALSEAESKAIRL------GKELSSAESQLHDTQEL 1344
Cdd:COG3096 873 LQLLNKLLPqanlladETLADRLEELReeldAAQEAQAFIQQHGKALAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRR 952
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1345 LQEETRAKLALGSRVRALE-AEAAG-----------LREQMEEEVVARERAGRELQSTQAQLSE 1396
Cdd:COG3096 953 LKQQIFALSEVVQRRPHFSyEDAVGllgensdlnekLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1072-1408 |
4.25e-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: 51.22 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1072 QELEKLKRRLDGESSELQEQMVE-QKQRAE--ELLAQLGRKEDELQAALLRAeeeggarAQLLKSLREAQAGLAEAQEDL 1148
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAyGKLRRElaGLTRRLSAAEGELEELVARL-------AKLEAALREAEAAKEELRIEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1149 EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKA---LEEESRAHEVSMQELRQRHSQA 1225
Cdd:pfam19220 114 RDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERlalLEQENRRLQALSEEQAAELAEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1226 LVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQR 1305
Cdd:pfam19220 194 TRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1306 AQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALeAEAAGLREqmeeevVARERAGR 1385
Cdd:pfam19220 274 RDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML-TKALAAKD------AALERAEE 346
|
330 340
....*....|....*....|...
gi 1039779964 1386 ELQSTQAQLSEWRRRQEEEAAVL 1408
Cdd:pfam19220 347 RIASLSDRIAELTKRFEVERAAL 369
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
871-1598 |
4.86e-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: 51.97 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 871 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 950
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 951 RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKfeedlllledqnSKLSKERRLLEERLA 1030
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI------------ERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1031 EFSSQaaeEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgesselqeqmveqkQRAEELLAQLGRKE 1110
Cdd:TIGR00606 416 DLQSK---ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL---------------QQLEGSSDRILELD 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1111 DELQAALlrAEEEGGARAQLLKSLREAQAGLAEAQEDLeaERVARAKAEKQrRDLGEELEALRGELEDTLDSTNAQQELR 1190
Cdd:TIGR00606 478 QELRKAE--RELSKAEKNSLTETLKKEVKSLQNEKADL--DRKLRKLDQEM-EQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1191 SKREQEVTEL---------KKALEEESRAHEVSMQELRQRhsqaLVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAEL 1261
Cdd:TIGR00606 553 KIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDR----LAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1262 SSLQTSRQEgEQKRRRLESQLqevqgrssdsERARSEAAeKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDT 1341
Cdd:TIGR00606 629 FDVCGSQDE-ESDLERLKEEI----------EKSSKQRA-MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1342 QELLQEETRaklALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEeaavleageearrraare 1421
Cdd:TIGR00606 697 ISDLQSKLR---LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK------------------ 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1422 AETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGRE 1501
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1502 REARalSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNvheLERARKAAEQAAsDLRTQVTELEDELTAAED 1581
Cdd:TIGR00606 836 HELD--TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN---LQRRQQFEEQLV-ELSTEVQSLIREIKDAKE 909
|
730
....*....|....*..
gi 1039779964 1582 AKLRLEVTVQALKAQHE 1598
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKE 926
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
905-1348 |
6.19e-06 |
|
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: 51.56 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 905 QLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 984
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 985 gaRQKLQLEKVTTEAKMKKFEEDLLLLEDQnsKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRL 1064
Cdd:TIGR04523 180 --KEKLNIQKNIDKIKNKLLKLELLLSNLK--KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1065 KKEekgRQELEKLKRRLdgesSELQEQMVEQKQRAEELLAQLGRKEDELQAalLRAEEEggarAQLLKSLREAqagLAEA 1144
Cdd:TIGR04523 256 NQL---KDEQNKIKKQL----SEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKE----QDWNKELKSE---LKNQ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1145 QEDLEAERVARAKAEKQRRDLGEELEALRGELEDtLDSTNA--QQELRSKrEQEVTELKKALE---EESRAHEVSMQELR 1219
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTN-SESENSekQRELEEK-QNEIEKLKKENQsykQEIKNLESQINDLE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1220 QRHSQALV---EMAEQLEQARRGKGVWEK-------TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQgRS 1289
Cdd:TIGR04523 398 SKIQNQEKlnqQKDEQIKKLQQEKELLEKeierlkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS-RS 476
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1290 SDSERARSEAAEK-LQRAQAELESVSTALSEAESKAirlgKELSSAESQLHDTQELLQEE 1348
Cdd:TIGR04523 477 INKIKQNLEQKQKeLKSKEKELKKLNEEKKELEEKV----KDLTKKISSLKEKIEKLESE 532
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
902-1173 |
1.08e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.46 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 902 RVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV---VTELEA---RVGEEEEcsrqLQSEKKRLQqHIQE 975
Cdd:COG0497 149 AFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLrfqLEELEAaalQPGEEEE----LEEERRRLS-NAEK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 976 LeshLEAEEGARQklqlekvtteakmkkfeedlLLLEDQNS---KLSKERRLLEeRLAEFSSQAAEEEEKVKSLnklrlk 1052
Cdd:COG0497 224 L---REALQEALE--------------------ALSGGEGGaldLLGQALRALE-RLAEYDPSLAELAERLESA------ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1053 yEATISDMedrlkkeekgRQELEKLKRRLDGESSELQEqmVEQKQraeELLAQLGRK----EDELqaallraeeeggarA 1128
Cdd:COG0497 274 -LIELEEA----------ASELRRYLDSLEFDPERLEE--VEERL---ALLRRLARKygvtVEEL--------------L 323
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039779964 1129 QLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1173
Cdd:COG0497 324 AYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAAR 368
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
949-1175 |
1.11e-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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 949 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLlllEDQNSKLSKERRLLEER 1028
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1029 LAefssQAAEEEEKVKSLNKL-----------RLKYEATISDMEDRLKKE-EKGRQELEKLKRRLDGESSELQEQMVEQK 1096
Cdd:COG3883 92 AR----ALYRSGGSVSYLDVLlgsesfsdfldRLSALSKIADADADLLEElKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 1097 QRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGE 1175
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
962-1753 |
1.28e-05 |
|
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: 50.49 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 962 LQSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtTEAKMKKFEEDLllleDQNSKLSKERRLLEERLAEFSSQAAEEEE 1041
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFE---NEKVSLKLEEEI----QENKDLIKENNATRHLCNLLKETCARSAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1042 KVKSLNKLRLKYEATISDMEDRLKKEEKGRQELeklkrRLDGESS------ELQEQMVEQKQRAEELLAQLGRKEDELQA 1115
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-----RVQAENArlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1116 ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDStnaqqelrskreq 1195
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST------------- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1196 evtelKKALEEESRAHEVSMQELRQrhsqalvEMAEQLEQARRGKGVWEKTRLSLEAEVSELKaELssLQTSRQEGEQKR 1275
Cdd:pfam05483 312 -----QKALEEDLQIATKTICQLTE-------EKEAQMEELNKAKAAHSFVVTEFEATTCSLE-EL--LRTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1276 RRLESQLQEVQGRSSDSErarsEAAEKLQRAQAELESVSTALSEAESkairlgkeLSSAESQLHDTQELLQEETRAKLAL 1355
Cdd:pfam05483 377 DQLKIITMELQKKSSELE----EMTKFKNNKEVELEELKKILAEDEK--------LLDEKKQFEKIAEELKGKEQELIFL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1356 gsrVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAvleageearrraareaeTLTQRLAEKTEA 1435
Cdd:pfam05483 445 ---LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA-----------------HCDKLLLENKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1436 VERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEE 1515
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1516 EQEAREELERQNRALRAELEallsskdDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEdakLRLEVTVQALka 1595
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIE-------NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE---LELASAKQKF-- 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1596 qherdlqgrddagEERRRQLAKQLRDAEVERDE--ERKQRALAMAARKKLELELEELKAQTSAAgqgkeEAVKQLKKMQV 1673
Cdd:pfam05483 653 -------------EEIIDNYQKEIEDKKISEEKllEEVEKAKAIADEAVKLQKEIDKRCQHKIA-----EMVALMEKHKH 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1674 QmkelWREVEETRSSRDEMFTLSRENEKKLK-GLEAEVLRLQEELAAsdrARRQAQQDRDEmAEEVASGNLSKAATLEEK 1752
Cdd:pfam05483 715 Q----YDKIIEERDSELGLYKNKEQEQSSAKaALEIELSNIKAELLS---LKKQLEIEKEE-KEKLKMEAKENTAILKDK 786
|
.
gi 1039779964 1753 R 1753
Cdd:pfam05483 787 K 787
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
901-1214 |
1.44e-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: 50.34 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 901 GRVAQleEERtrlAEQLRAEAElcsEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEK--KRLQQHIQELES 978
Cdd:COG3096 779 GRAAR--EKR---LEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAelAALRQRRSELER 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 979 HLEAEEGA--RQKLQLEKVTTEAKM-KKFEEDLLLLEDQNskLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA 1055
Cdd:COG3096 851 ELAQHRAQeqQLRQQLDQLKEQLQLlNKLLPQANLLADET--LADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAV 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1056 TISDME--DRLKKE-EKGRQELEKLKRRLD---------------------GESSELQEQMVEQKQRAEELLAQLGrkeD 1111
Cdd:COG3096 929 LQSDPEqfEQLQADyLQAKEQQRRLKQQIFalsevvqrrphfsyedavgllGENSDLNEKLRARLEQAEEARREAR---E 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1112 ELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV-----ARAKAEKQRRDLGEELEALRG---ELEDTLDST 1183
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVqadaeAEERARIRRDELHEELSQNRSrrsQLEKQLTRC 1085
|
330 340 350
....*....|....*....|....*....|.
gi 1039779964 1184 NAQQELRSKREQEVTELKKALEEESRAHEVS 1214
Cdd:COG3096 1086 EAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1057-1241 |
1.69e-05 |
|
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: 48.38 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1057 ISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEeggARAQL--LKSL 1134
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLgnVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1135 REAQAglaeAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALEEESRAHEVS 1214
Cdd:COG1579 89 KEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190
....*....|....*....|....*....|.
gi 1039779964 1215 MQELRQRHSQALVEMAEQL----EQARRGKG 1241
Cdd:COG1579 158 LEELEAEREELAAKIPPELlalyERIRKRKN 188
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
861-1111 |
1.77e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.93 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 861 KVKPLLQVTRQDEVLQAraQELQKVQELQQQSAREvgelqgrvaQLEEERTRLAEqlrAEAELCSEAEETRA-----RLA 935
Cdd:PLN03188 1015 KRNSLLKLTYSCEPSQA--PPLNTIPESTDESPEK---------KLEQERLRWTE---AESKWISLAEELRTeldasRAL 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 936 ARKQELELvvtELEARVGEEEECSRQL--QSEKKRLQQ-------HIQELESHLEAEEGARQklqLEKVTTEAKMKKFEE 1006
Cdd:PLN03188 1081 AEKQKHEL---DTEKRCAEELKEAMQMamEGHARMLEQyadleekHIQLLARHRRIQEGIDD---VKKAAARAGVRGAES 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1007 DLL-LLEDQNSKL----SKERRLLEERLAEFSSQAAEEEEKVKSLNKL--RLK-YEATISDMEDRLKKEE----KGRQEL 1074
Cdd:PLN03188 1155 KFInALAAEISALkverEKERRYLRDENKSLQAQLRDTAEAVQAAGELlvRLKeAEEALTVAQKRAMDAEqeaaEAYKQI 1234
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039779964 1075 EKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKED 1111
Cdd:PLN03188 1235 DKLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCM 1271
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1295-1511 |
1.94e-05 |
|
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: 48.99 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1295 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQME 1374
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1375 EEvvaRERAGRELQSTQAQlsewRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDAT 1454
Cdd:COG4942 101 AQ---KEELAELLRALYRL----GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1455 VDLgqqKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTR 1511
Cdd:COG4942 174 AEL---EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1220-1941 |
1.94e-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: 49.97 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1220 QRHSQALVEMAEQLEQARRgkgvweKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARS-E 1298
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKK------KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1299 AAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEAAGLREQMEEEV 1377
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1378 VARERAGRELQSTQAQLsewrrrQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDL 1457
Cdd:pfam02463 307 RRKVDDEEKLKESEKEK------KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1458 GQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEAL 1537
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1538 LSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAK 1617
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1618 QLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE-LWREVEETRSSRDEMFTLS 1696
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1697 RENEKKLKGLEAEVLRLQE-ELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSEL 1775
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKEsAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1776 LKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKlaqaEEQLEQ-- 1853
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKel 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1854 -ESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVT 1932
Cdd:pfam02463 777 aEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
....*....
gi 1039779964 1933 ESAESMNRE 1941
Cdd:pfam02463 857 ERLEEEITK 865
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1355-1871 |
2.13e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1355 LGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEeaavleageearrraareaetltqrLAEKTE 1434
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE-------------------------LETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1435 AVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQrkfDQLLAEekAAVLRAveDRERIEAEGREREARALSLTRALE 1514
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEER---DDLLAE--AGLDDA--DAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1515 EEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALK 1594
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1595 AQHERDLQGRDDAGE------------ERRRQLAKQLRDA----EVERDEERKQRALAMAARKKLELELEELKAQTSAAG 1658
Cdd:PRK02224 412 DFLEELREERDELREreaeleatlrtaRERVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1659 QGKEEAVKQLKkmqvQMKELWREVEETRSSRDEMFTLSRENEKKL--KGLEAEVLRLQ-EELAASDRARRQAQQDRDEMA 1735
Cdd:PRK02224 492 EEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIeeKRERAEELRERaAELEAEAEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1736 EEVAsgnlSKAATLEEKRQ-LEGRLSQLeeeleeeqnnsellkDHYRKLVLQVESLTTELSAERS-FSAKAESGRQQLER 1813
Cdd:PRK02224 568 EEAR----EEVAELNSKLAeLKERIESL---------------ERIRTLLAAIADAEDEIERLREkREALAELNDERRER 628
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1814 qIQELRAR---LGEEDAGARarqkmlIAALESKLAQAEEQLEQesreriLSGKLVRRAEKR 1871
Cdd:PRK02224 629 -LAEKRERkreLEAEFDEAR------IEEAREDKERAEEYLEQ------VEEKLDELREER 676
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1077-1907 |
2.14e-05 |
|
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: 49.97 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1077 LKRRLDGESSELQEQM-VEQKQRAEELLAQLGRKEDELQAALLRAEEE---------GGARAQLLKSLREAQAGLAEAQE 1146
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLyLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtftrvvllpQGEFAQFLKAKSKEKKELLMNLF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1147 DLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEEsrahevsMQELRQRHSQaL 1226
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA-------LQQTQQSHAY-L 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1227 VEMAEQLEQARRgkgvWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLesqlqevqgRSSDSERARSEAAEKLQRA 1306
Cdd:TIGR00618 246 TQKREAQEEQLK----KQQLLKQLRARIEELRAQEAVLEETQERINRARKAA---------PLAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1307 QAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEEtraklalgSRVRALEAEAAGLREQMEEEVVARERAgRE 1386
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE--------IHIRDAHEVATSIREISCQQHTLTQHI-HT 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1387 LQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLST 1466
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1467 LEKKQRKFDQLLAEEKAAVLRavedreriEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGK 1546
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1547 NVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKA------QHERDLQGRDDAGEERRRQLAKQLR 1620
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdipnlqNITVRLQDLTEKLSEAEDMLACEQH 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1621 DAEVERDEERKQRALAMAARKKLeleleelkaqtsaagqgKEEAVKQLKKMQVQMKELWREVEET-RSSRDEMFTLSREN 1699
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCS-----------------QELALKLTALHALQLTLTQERVREHaLSIRVLPKELLASR 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1700 EKKLKGLEAEVLRL---QEELAASDRARRQAQQDRDEMAEEVasgNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSell 1776
Cdd:TIGR00618 679 QLALQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDREF---NEIENASSSLGSDLAAREDALNQSLKELMHQA--- 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1777 KDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEedagararqkmliaaleskLAQAEEQLEQESR 1856
Cdd:TIGR00618 753 RTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------------------LKTLEAEIGQEIP 813
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1857 ERILsgklvrraEKRLKEVVLQVDEErrvadQVRDQLEKSNLRLKQLKRQL 1907
Cdd:TIGR00618 814 SDED--------ILNLQCETLVQEEE-----QFLSRLEEKSATLGEITHQL 851
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1011-1238 |
2.33e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1011 LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKvksLNKLRLKYEatISDMEDRLKKEEkgrQELEKLKRRLdgesSELQE 1090
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNG--LVDLSEEAKLLL---QQLSELESQL----AEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1091 QMVEQKQRAEELLAQLGRKEDELQAALlraeeEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELE 1170
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1171 AlrgELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELR--QRHSQALVEMAEQLEQARR 1238
Cdd:COG3206 309 Q---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1527-1951 |
2.41e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1527 NRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHE-RDLQGRD 1605
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1606 DAGEERRRQLAKQLRD-AEVERDEERKQRALAMAARKKLELELeelkAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEE 1684
Cdd:COG4717 149 EELEERLEELRELEEElEELEAELAELQEELEELLEQLSLATE----EELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1685 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEE 1764
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1765 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKaesgrqQLERQIQELRARLgeEDAGARARQKMLIAALESKL 1844
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELL------DRIEELQELLREA--EELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1845 AQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNL--RLKQLKRQLEEAEEEASRAQAGRR 1922
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeeELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|.
gi 1039779964 1923 RLQRELEDVTESAE--SMNREVTTLRNRLRR 1951
Cdd:COG4717 457 ELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1011-1171 |
2.63e-05 |
|
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: 47.61 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1011 LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgRQELEKLKRRLDGESSELQE 1090
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1091 QMVEQKQRAEELLAQLGRKEdELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAErvaRAKAEKQRRDLGEELE 1170
Cdd:COG1579 101 LKRRISDLEDEILELMERIE-ELEEELAELEAE---LAELEAELEEKKAELDEELAELEAE---LEELEAEREELAAKIP 173
|
.
gi 1039779964 1171 A 1171
Cdd:COG1579 174 P 174
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
873-1284 |
2.88e-05 |
|
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: 49.36 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 873 EVLQARAQELQKVQELQQQS-AREVGELQgrvaQLEEERTRLAEQLraeaeLCSEAEETRA---RLAARKQELELVVTEL 948
Cdd:pfam07111 266 ELLQVRVQSLTHMLALQEEElTRKIQPSD----SLEPEFPKKCRSL-----LNRWREKVFAlmvQLKAQDLEHRDSVKQL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 949 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1028
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIW 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1029 LAEFSSQAAEEEEKVKSLNKlRLKYEA----TISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLA 1104
Cdd:pfam07111 417 LETTMTRVEQAVARIPSLSN-RLSYAVrkvhTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1105 QLGRKEDELQAALLRAEEEGGA-RAQLLKSLREAQAGLAEAQEDLEAervarakaekqrrdLGEELE-ALRGELEDTLDS 1182
Cdd:pfam07111 496 ELQLSAHLIQQEVGRAREQGEAeRQQLSEVAQQLEQELQRAQESLAS--------------VGQQLEvARQGQQESTEEA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1183 TNAQQELRSKRE-------QEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAE-QLEQARRGKGVWEKTRLSLEAEv 1254
Cdd:pfam07111 562 ASLRQELTQQQEiygqalqEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQiQHRATQEKERNQELRRLQDEAR- 640
|
410 420 430
....*....|....*....|....*....|
gi 1039779964 1255 selKAELSSLQTSRQEGEQKRRRLESQLQE 1284
Cdd:pfam07111 641 ---KEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1185-1406 |
2.90e-05 |
|
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: 48.61 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1185 AQQELRSKREQEVTELKKALEEESRAHEvSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSL 1264
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1265 QTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQEL 1344
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1345 LQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAA 1406
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
912-1237 |
2.91e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.55 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 912 RLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVgEEEECSrqLQSEKKRLQQhiqELESHLEAeegARQKLQ 991
Cdd:PLN03188 898 RLVQQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFL-EEELAS--LMHEHKLLKE---KYENHPEV---LRTKIE 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 992 LEKVTTEAK-MKKF----EEDLLLLEDQNSKLS-------------KERRLLEERLAEFSSQA--------AEEEEKVKS 1045
Cdd:PLN03188 969 LKRVQDELEhYRNFydmgEREVLLEEIQDLRSQlqyyidsslpsarKRNSLLKLTYSCEPSQApplntipeSTDESPEKK 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1046 LNKLRLKYEATISD---MEDRLKKE-EKGRQELEKLKRRLDGE---SSELQEQM---VEQKQRAEELLAQLGRKEDELQA 1115
Cdd:PLN03188 1049 LEQERLRWTEAESKwisLAEELRTElDASRALAEKQKHELDTEkrcAEELKEAMqmaMEGHARMLEQYADLEEKHIQLLA 1128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1116 ALLRAEE------EGGARAqllkSLREAQAGLAEAqedLEAERVA-RAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1188
Cdd:PLN03188 1129 RHRRIQEgiddvkKAAARA----GVRGAESKFINA---LAAEISAlKVEREKERRYLRDENKSLQAQLRDTAEAVQAAGE 1201
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 1189 L--RSKREQE--VTELKKALEEESRAHEV--SMQELRQRHSQALVEMAEQLEQAR 1237
Cdd:PLN03188 1202 LlvRLKEAEEalTVAQKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESR 1256
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
960-1106 |
3.10e-05 |
|
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: 47.61 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 960 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL---------SKERRLLEERLA 1030
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779964 1031 EFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgrqELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1106
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-984 |
3.48e-05 |
|
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: 48.22 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 864 PLLQVTRQDEVLQArAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL 943
Cdd:COG4942 121 PLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1039779964 944 VVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 984
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1051-1172 |
3.80e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1051 LKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLgrkEDELQAALLRAEEEGgarAQL 1130
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEA---DEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039779964 1131 LKSLREAQAGLAEAQedleaervARAKAEKQRRDLGEELEAL 1172
Cdd:PRK00409 590 IKELRQLQKGGYASV--------KAHELIEARKRLNKANEKK 623
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1080-1237 |
3.85e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1080 RLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAE 1159
Cdd:PRK09039 57 RLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1160 KQRRDLGEELEALR---GELEDTLDstnaqqelrskreqevtelkkALEEESRAHEVSMQELRQRHSQALVEMAEQLEQA 1236
Cdd:PRK09039 137 AQVELLNQQIAALRrqlAALEAALD---------------------ASEKRDRESQAKIADLGRRLNVALAQRVQELNRY 195
|
.
gi 1039779964 1237 R 1237
Cdd:PRK09039 196 R 196
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
871-1162 |
4.15e-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: 48.81 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 871 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAAR-----KQELELVV 945
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEErekteKLKVEEEK 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 946 TELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEA--EEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERR 1023
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1024 LLEERLAEFSSQAAEEEEKVKSLNKLRlkyeatisdmEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1103
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEK----------KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 1104 AQlgRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQR 1162
Cdd:pfam02463 943 EE--ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
955-1105 |
4.23e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 955 EEECSRQLQSEKKRLQQHIQELEshLEA-EEGARQKLQLEKVTTE--AKMKKFEEDLLLLEDQnskLSKERRLLEERLAE 1031
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEAL--LEAkEEIHKLRNEFEKELRErrNELQKLEKRLLQKEEN---LDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1032 FSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLK------KEEKGRQELEKLKRRLDGESSELQEQMVEQ-----KQRAE 1100
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQELErisgltAEEAKEILLEKVEEEARHEAAVLIKEIEEEakeeaDKKAK 191
|
....*
gi 1039779964 1101 ELLAQ 1105
Cdd:PRK12704 192 EILAQ 196
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
868-1321 |
4.46e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 48.67 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 868 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAElcSEAEETRARLAArkqELELVVTE 947
Cdd:NF041483 436 VELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAK--ADADELRSTATA---ESERVRTE 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 948 LEARVG----EEEECSRQLQSEKKRLQQHIQEL--ESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQnsklske 1021
Cdd:NF041483 511 AIERATtlrrQAEETLERTRAEAERLRAEAEEQaeEVRAAAERAARELREETERAIAARQAEAAEELTRLHTE------- 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1022 rrlLEERLAefssqAAEEEEKVKSLNKLRLKYEATisdmedrlkkEEKGRQELEKLKRRldgesSELQEQMVEQKQR-AE 1100
Cdd:NF041483 584 ---AEERLT-----AAEEALADARAEAERIRREAA----------EETERLRTEAAERI-----RTLQAQAEQEAERlRT 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1101 ELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVArAKAEKQRRDLGEELEALRGELEDTL 1180
Cdd:NF041483 641 EAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVG-TEAAEALAAAQEEAARRRREAEETL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1181 DS--TNAQQELRSKREQEVTELKKALE--EESRAHEVSMQELRQRHSQALVEMAEQLEQARRGK--GVWEKTrlslEAEV 1254
Cdd:NF041483 720 GSarAEADQERERAREQSEELLASARKrvEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSvaGLQEQA----EEEI 795
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1255 SELK--AELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELE-SVSTALSEAE 1321
Cdd:NF041483 796 AGLRsaAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAErTVSEAIAEAE 865
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
905-1303 |
4.78e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 48.79 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 905 QLEEERTRLAEQL-----RAEAElcSEAEETRARLAARKQELELvvtELEARVGEEEECSRQLQSEKKRLQQHIQELESH 979
Cdd:pfam15818 1 QLLDFKTSLLEALeelrmRREAE--TQYEEQIGKIIVETQELKW---QKETLQNQKETLAKQHKEAMAVFKKQLQMKMCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 980 LEAEEGarqKLQLEKVTTEAKMKKFEEDLLLLedQNSKLSKERRLLE-ERLAEFSSQAAEEEEKvkSLNKLRlKYEATIS 1058
Cdd:pfam15818 76 LEEEKG---KYQLATEIKEKEIEGLKETLKAL--QVSKYSLQKKVSEmEQKLQLHLLAKEDHHK--QLNEIE-KYYATIT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1059 DMEDRLK----KEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQaalLRAEEEggaraQLLKSL 1134
Cdd:pfam15818 148 GQFGLVKenhgKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQ---YKMGEE-----NINLTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1135 REAQagLAEAQEDLEAERVARAKaekqrrdLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELK---KALEEESRAH 1211
Cdd:pfam15818 220 KEQK--FQELQERLNMELELNKK-------INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEaelKALKENNQTL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1212 EVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSR--------QEGEQKRRRLESQLQ 1283
Cdd:pfam15818 291 ERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHiklqehynKLCNQKKFEEDKKFQ 370
|
410 420
....*....|....*....|
gi 1039779964 1284 EVQGRSSDSERARSEAAEKL 1303
Cdd:pfam15818 371 NVPEVNNENSEMSTEKSENL 390
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
870-1209 |
4.85e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 870 RQDEVLQARAQELQKVQELQQQSAREVGELQGRVaQLEEERTRLAEQLRAEAElcseaeETRARLAARKQELELVVTELE 949
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMI-QNAEKNILLLNQARLQAL------EDLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 950 ARVGEEEECSRQLQSEKKrlqqHIQELESHLEAeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERL 1029
Cdd:PLN02939 177 MRLSETDARIKLAAQEKI----HVEILEEQLEK---LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1030 AEFssqaAEEEEKVKSLNKLRLKYEATISDMEDRLkkeekgrqeleklkrrldgesSELQEQMVEQKQRAEELLAQlgrK 1109
Cdd:PLN02939 250 IEV----AETEERVFKLEKERSLLDASLRELESKF---------------------IVAQEDVSKLSPLQYDCWWE---K 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1110 EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRdLGEELEALRGELEDTLDSTNAQQEL 1189
Cdd:PLN02939 302 VENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQL 380
|
330 340
....*....|....*....|
gi 1039779964 1190 RSKREQEVTELKKALEEESR 1209
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESK 400
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1038-1151 |
4.94e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1038 EEEEKV----KSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDgesSELQEQMVEQKQRAEELLAQLgRKEDEL 1113
Cdd:PRK00409 513 EDKEKLneliASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEA-KKEADE 588
|
90 100 110
....*....|....*....|....*....|....*...
gi 1039779964 1114 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE 1151
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
857-1051 |
5.34e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 857 RLFIKVKPLLQVTRQD----EVLQARAQELQKVQELQQQSAREVGE--------------------------LQGRVAQL 906
Cdd:PRK04863 918 NALAQLEPIVSVLQSDpeqfEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfsyedaaemlaknsdlnekLRQRLEQA 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 907 EEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE-----EEECSRQLQSEKKRLQQHIQELESHLE 981
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpaDSGAEERARARRDELHARLSANRSRRN 1077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 982 AEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NSKLSK------------ERRLLEERLAEFSSQAAEEEEKvKSLN 1047
Cdd:PRK04863 1078 QLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQvvNAKAGWcavlrlvkdngvERRLHRRELAYLSADELRSMSD-KALG 1156
|
....
gi 1039779964 1048 KLRL 1051
Cdd:PRK04863 1157 ALRL 1160
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1119-1460 |
6.51e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1119 RAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVT 1198
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1199 ELKKALEEESRAHEVSMQELRQRhSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRL 1278
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESL-QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1279 ESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSR 1358
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1359 VRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVER 1438
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340
....*....|....*....|..
gi 1039779964 1439 LERARRRLQQELDDATVDLGQQ 1460
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQ 344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1021-1214 |
7.38e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1021 ERRLLEERLAEFSSQAAEEEEKVKSLNKlrlKYEATISDMEDRLKKEEKGRQELEKLKRRLDgessELQEQMVEQKQRAE 1100
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIA----EAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1101 ELLAQLGRKEDELQ--AALLRAEEEG-------------GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDL 1165
Cdd:COG3883 90 ERARALYRSGGSVSylDVLLGSESFSdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039779964 1166 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVS 1214
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1262-1472 |
8.41e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1262 SSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE---------AAEKLQRAQAELESVSTALSEAESKAIRLGKELS 1332
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1333 SAESQLHDTQELLQE--ETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLsewrrrQEEEAAVLEA 1410
Cdd:COG3206 244 ALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1411 GEEARRRAAREAETLTQRLAEKTEAVerleRARRRLQQELDDATVDLGQQKQLLSTLEKKQR 1472
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
865-1144 |
8.48e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 865 LLQVTRQDEVLQARAQELQKVQELQ------QQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaeetrarlaark 938
Cdd:COG0497 137 LLDPDAQRELLDAFAGLEELLEEYReayrawRALKKELEELRADEAERARELDLLRFQL--------------------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 939 QELElvvtELEARVGEEEEcsrqLQSEKKRLQ------QHIQELESHLEAEEG--------ARQKLQlEKVTTEAKMKKF 1004
Cdd:COG0497 196 EELE----AAALQPGEEEE----LEEERRRLSnaeklrEALQEALEALSGGEGgaldllgqALRALE-RLAEYDPSLAEL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1005 EEDL----LLLEDQNSKLSKERRLLE---ERLAEFssqaaeeEEKVKSLNKLRLKYEATISDMedrLKKEEKGRQELEKL 1077
Cdd:COG0497 267 AERLesalIELEEAASELRRYLDSLEfdpERLEEV-------EERLALLRRLARKYGVTVEEL---LAYAEELRAELAEL 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 1078 krrldgesselqeqmveqkQRAEELLAQLGRKEDELQAALLRAeeeggarAQLLKSLREAQAG-LAEA 1144
Cdd:COG0497 337 -------------------ENSDERLEELEAELAEAEAELLEA-------AEKLSAARKKAAKkLEKA 378
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1055-1372 |
8.70e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1055 ATISDME---DRLKKEEKGRQELEKLKRRLDGESSELQEqmveqkqrAEELLAQLGRKEDELQAALLRAEEeggaRAQLL 1131
Cdd:PRK11281 60 LVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQ--------AQAELEALKDDNDEETRETLSTLS----LRQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1132 KSLREAQAGLAEAQEDLEaervarakaekqrrDLGEELEALRGELEdtldstNAQQEL--RSKREQEVTELKKALEEESR 1209
Cdd:PRK11281 128 SRLAQTLDQLQNAQNDLA--------------EYNSQLVSLQTQPE------RAQAALyaNSQRLQQIRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1210 AHEVSMQELRQRHsQALVEMaeQLEQARRgkgvwektrlslEAEVSELKAELssLQTSRQEGEQKRRRLESQLQEVQGRS 1289
Cdd:PRK11281 188 ALRPSQRVLLQAE-QALLNA--QNDLQRK------------SLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQEAI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1290 SDSERARSEA-AEKLQRAQAELESVSTALSEAESKA-IRLGKELSSAESQLHdtqELLQEETRAKLALGsrvRALEAEAA 1367
Cdd:PRK11281 251 NSKRLTLSEKtVQEAQSQDEAARIQANPLVAQELEInLQLSQRLLKATEKLN---TLTQQNLRVKNWLD---RLTQSERN 324
|
....*
gi 1039779964 1368 gLREQ 1372
Cdd:PRK11281 325 -IKEQ 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1506-1746 |
1.44e-04 |
|
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: 46.30 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1506 ALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLR 1585
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1586 LEVTVQALKAQHerdlqgrddagEERRRQLAKQLR---------------DAEVERDEERKQRALAMAARKKLELELEEL 1650
Cdd:COG4942 88 LEKEIAELRAEL-----------EAQKEELAELLRalyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1651 KAQTSAAGQgKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQD 1730
Cdd:COG4942 157 ADLAELAAL-RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*.
gi 1039779964 1731 RDEMAEEVASGNLSKA 1746
Cdd:COG4942 236 AAAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1714-1956 |
1.56e-04 |
|
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: 46.30 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1714 QEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTE 1793
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1794 LSAERSFSAKAESGRQQLERQiQELRARLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLK 1873
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1874 EVVLQVDEERRVADQVRDQLEKsnlRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGP 1953
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 1039779964 1954 LTF 1956
Cdd:COG4942 255 LPW 257
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1668-1974 |
1.85e-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: 46.43 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1668 LKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAA 1747
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1748 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDA 1827
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1828 GARARQKMlIAALESKLAQAE------EQLEQE---SRERI-LSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSN 1897
Cdd:pfam07888 207 QVLQLQDT-ITTLTQKLTTAHrkeaenEALLEElrsLQERLnASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLT 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1898 LRLKQLKRQLeeaEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRgpltftTRTVRQVFRLEEGVASD 1974
Cdd:pfam07888 286 LQLADASLAL---REGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE------ERMEREKLEVELGREKD 353
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
948-1202 |
1.90e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 948 LEARVGEEEECSRQLQSEKKRLQQHI---QELESHLEAEEGAR-QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERR 1023
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIktyNKNIEEQRKKNGENiARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1024 LLEERLAEFSSQAAEEEEKVKSLNKLRLKYE---------ATISDMEDRLkkeEKGRQELEKLKRRLDgessELQEQMVE 1094
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRI---TKIKDKLKELQHSLE----KLDTAIDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1095 QKQRAEElLAQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAglaeAQEDLEAERVARAkaekqrrdlgEELEALRG 1174
Cdd:PHA02562 325 LEEIMDE-FNEQSKKLLELKNKI---STNKQSLITLVDKAKKVKA----AIEELQAEFVDNA----------EELAKLQD 386
|
250 260
....*....|....*....|....*...
gi 1039779964 1175 ELEDtLDSTNAQQELRSKREQEVTELKK 1202
Cdd:PHA02562 387 ELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
865-1090 |
2.05e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.57 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 865 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEER---TRLAEQLRAEAE----------LCSEAEETR 931
Cdd:pfam15905 86 VQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLlelTRVNELLKAKFSedgtqkkmssLSMELMKLR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 932 ARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKL-----QLEKVTTEAKMKKFEE 1006
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLleyitELSCVSEQVEKYKLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1007 DLL--LLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKeekgrqELEKLKRRLDGE 1084
Cdd:pfam15905 246 AQLeeLLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNA------ELEELKEKLTLE 319
|
....*.
gi 1039779964 1085 SSELQE 1090
Cdd:pfam15905 320 EQEHQK 325
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
988-1587 |
2.13e-04 |
|
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: 46.55 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 988 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKlrlkyEATISDMEDRLKKE 1067
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS-----DLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1068 EKGR--QELEKLKRRLDgESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQ 1145
Cdd:TIGR04523 118 QKNKleVELNKLEKQKK-ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE---LNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1146 EDLEAER----VARAKAEKQRRDLGE--ELEALRGELEDTLdstnaqQELRSKREQEVTELKKALEEESRAHEVSMQELR 1219
Cdd:TIGR04523 194 NKLLKLElllsNLKKKIQKNKSLESQisELKKQNNQLKDNI------EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1220 QrhsqaLVEMAEQLEQArrgkgvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKrrRLESQLQEVQGRSSDSERARSEA 1299
Cdd:TIGR04523 268 Q-----LSEKQKELEQN-------NKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1300 AEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAE---AAGLREQMEEE 1376
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnQEKLNQQKDEQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1377 VVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL----ERARRRLQQELDD 1452
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1453 ATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNR--AL 1530
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieEL 573
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1531 RAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLE 1587
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
898-1202 |
2.27e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 898 ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELE 977
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 978 SHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERrllEERLAEFSSQAAEEEEKVKSLNKLRLKyeatI 1057
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKELEKAKKALEKNEK----L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1058 SDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELlaqlgRKEdelqaallraeeeggaraqllksLREA 1137
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADEL-----RKE-----------------------ADEL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 1138 QAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLdSTNAQQELRSKREQEVTELKK 1202
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK-REKEKEELEEKAEEIFEKLKK 278
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1715-1951 |
2.32e-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: 46.60 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1715 EELAASDRARRQAQQDRDEMaeEVASGNLSKA-ATLEEKRQLEGRLSQLEEELEEEQNNSELLKD-HYRKLVLQVESLTT 1792
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEEL--EEVEENIERLdLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1793 ELSAERSFSAKAESGRQQLERQIQELRARLGE----------------EDAGARARQKML-----IAALESKLAQAEEQL 1851
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEieqlleelnkkikdlgEEEQLRVKEKIGeleaeIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1852 EQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDV 1931
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260
....*....|....*....|
gi 1039779964 1932 TESAESMNREVTTLRNRLRR 1951
Cdd:TIGR02169 398 KREINELKRELDRLQEELQR 417
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
678-702 |
2.32e-04 |
|
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: 43.87 E-value: 2.32e-04
10 20
....*....|....*....|....*
gi 1039779964 678 YKESLSRLMATLSNTNPSFVRCIVP 702
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
931-1202 |
2.35e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 931 RARLAARKQELELVVTEL-EARVGEEEECSRQLQSEKKR--------LQQHIQELESHLEAEEGarqklqLEKVTTEAKM 1001
Cdd:PRK05771 8 KVLIVTLKSYKDEVLEALhELGVVHIEDLKEELSNERLRklrslltkLSEALDKLRSYLPKLNP------LREEKKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1002 KKFEEdllLLEDQNSKLSK-ERRL--LEERLAEFssqaaEEEEKVKSLNKLRLKYEATIsDMEDRLKKEEK------GRQ 1072
Cdd:PRK05771 82 KSLEE---LIKDVEEELEKiEKEIkeLEEEISEL-----ENEIKELEQEIERLEPWGNF-DLDLSLLLGFKyvsvfvGTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1073 ELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAE------EEGGARAQLLKSLREAQAGLaeaqe 1146
Cdd:PRK05771 153 PEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGferlelEEEGTPSELIREIKEELEEI----- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779964 1147 dleaervarakaEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKK 1202
Cdd:PRK05771 228 ------------EKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1746-1951 |
2.45e-04 |
|
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: 45.53 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1746 AATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEe 1825
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1826 dagARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKR 1905
Cdd:COG4942 95 ---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039779964 1906 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1951
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
876-1404 |
2.57e-04 |
|
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: 46.28 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 876 QARAQELQKVQELQQQS------------AREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL 943
Cdd:pfam07111 136 EGSQRELEEIQRLHQEQlssltqaheealSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 944 VVTELEA---RVGEE---EECSRQLQSEKKRLQQHIQELESHleaeegaRQKLQLEKVTTEAKMKKFEEDLLLLEDQnsk 1017
Cdd:pfam07111 216 QVTLVESlrkYVGEQvppEVHSQTWELERQELLDTMQHLQED-------RADLQATVELLQVRVQSLTHMLALQEEE--- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1018 lskerrlLEERLAEFSSQAAEEEEKVKSLnkLRLKYEATISDMEDRLKKEEKGRQELEKLKrrldGESSELQEQMVEQKQ 1097
Cdd:pfam07111 286 -------LTRKIQPSDSLEPEFPKKCRSL--LNRWREKVFALMVQLKAQDLEHRDSVKQLR----GQVAELQEQVTSQSQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1098 RaeellaqlgrkedelQAALLRAEEEGGARAQLLK-SLREAQAGLAEAQEdleaervARAKAEKQRRDLGEELEALRGEL 1176
Cdd:pfam07111 353 E---------------QAILQRALQDKAAEVEVERmSAKGLQMELSRAQE-------ARRRQQQQTASAEEQLKFVVNAM 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1177 EDTLDSTNAQQELRSKREQEVTELKKALEEESR---------AHEVSMQELRQRHS-------QALVEMAEQLEQARRgk 1240
Cdd:pfam07111 411 SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRkvhtikglmARKVALAQLRQESCpppppapPVDADLSLELEQLRE-- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1241 gvwEKTRLSLEAEVSELKAElSSLQTSRQEGEQKRRRLESQLQEVQgrssdserarseaaEKLQRAQAELESVSTALSEA 1320
Cdd:pfam07111 489 ---ERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLE--------------QELQRAQESLASVGQQLEVA 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1321 eskaiRLGKELSSAESQlHDTQELLQEETRAKLALGSRVRALEAEaagLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1400
Cdd:pfam07111 551 -----RQGQQESTEEAA-SLRQELTQQQEIYGQALQEKVAEVETR---LREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
|
....
gi 1039779964 1401 QEEE 1404
Cdd:pfam07111 622 ATQE 625
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
964-1738 |
2.58e-04 |
|
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: 46.19 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 964 SEKKRLQQHIQELES---HLEAEEGARQKLQlekvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEE 1040
Cdd:TIGR00606 166 SEGKALKQKFDEIFSatrYIKALETLRQVRQ----TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1041 EKVKSLNKLRLKYE------ATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQ 1114
Cdd:TIGR00606 242 SYENELDPLKNRLKeiehnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1115 AALLRAEEEGGARAQLLkSLREAQAGLAEAQEDLEAERVaraKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKre 1194
Cdd:TIGR00606 322 VDCQRELEKLNKERRLL-NQEKTELLVEQGRLQLQADRH---QEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1195 qeVTELKKALEEESRAHEVSMQELRQRHSQALvEMAEQLEQARRGKG-VWEKTRLSLEAEVSELKAELSSLQTSRQ---- 1269
Cdd:TIGR00606 396 --HTLVIERQEDEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKGLGrTIELKKEILEKKQEELKFVIKELQQLEGssdr 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1270 --EGEQKRRRLESQLQEVQGRSSDSERARSEAAekLQRAQAELESVSTALSE----------AESKAIRLGKELSSAESQ 1337
Cdd:TIGR00606 473 ilELDQELRKAERELSKAEKNSLTETLKKEVKS--LQNEKADLDRKLRKLDQemeqlnhhttTRTQMEMLTKDKMDKDEQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1338 LHDTQELLQEETRAKLALGSRVRALEAEAAGLRE---QMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEA 1414
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1415 RRRAAREAETLtQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQ----LLSTLEKKQRKFDQLLAEEKAAVLRAVE 1490
Cdd:TIGR00606 631 VCGSQDEESDL-ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1491 DRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSS----KDDVGKNVHELERArKAAEQAASDLR 1566
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDiqrlKNDIEEQETLLGTI-MPEEESAKVCL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1567 TQVTELEDELTAAEDAKLRLEVTVQALKAQH-ERDLQGRDDAGEERRRQLAKQLRDAEVERD--EERKQRALAMAARKKL 1643
Cdd:TIGR00606 789 TDVTIMERFQMELKDVERKIAQQAAKLQGSDlDRTVQQVNQEKQEKQHELDTVVSKIELNRKliQDQQEQIQHLKSKTNE 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1644 ELELEELKAQTSAAGQGKEEavkQLKKMQVQMKELWREVEEtrsSRDEMFTLSRENEKKLKGLEAEVLRLQEElaasdra 1723
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEE---QLVELSTEVQSLIREIKD---AKEQDSPLETFLEKDQQEKEELISSKETS------- 935
|
810
....*....|....*
gi 1039779964 1724 RRQAQQDRDEMAEEV 1738
Cdd:TIGR00606 936 NKKAQDKVNDIKEKV 950
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
900-1067 |
3.27e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 900 QGRVAQLEEERTRLAEQLRAEAELCSEAEETRArlaarKQELELVVTELEARVGEEEecsRQLQSEKKRLQQHIQELESH 979
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEA-----KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 980 LEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKLSKERRLLeERLAEFSSQAAEEE--EKVKSlnklRLKYEA-- 1055
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEK---KEEELEELIEEQLQEL-ERISGLTAEEAKEIllEKVEE----EARHEAav 173
|
170
....*....|..
gi 1039779964 1056 TISDMEDRLKKE 1067
Cdd:PRK12704 174 LIKEIEEEAKEE 185
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
873-1400 |
3.30e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 873 EVLQARAQEL-QKVQELQQQ--SAREVGELQGRVAQL------EEERTRLAEQLRaeaELCSEAEETRArLAARKQELEL 943
Cdd:PRK04863 445 EEFQAKEQEAtEELLSLEQKlsVAQAAHSQFEQAYQLvrkiagEVSRSEAWDVAR---ELLRRLREQRH-LAEQLQQLRM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 944 VVTELEARVGEEEECSRQLQSEKKRLQQHIQ---ELESHLEAEEGARQKLQLEKVTTEAK---MKKFEEDLLLLEDQNSK 1017
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAEFCKRLGKNLDdedELEQLQEELEARLESLSESVSEARERrmaLRQQLEQLQARIQRLAA 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1018 LSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQeqmveqkQ 1097
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDV-------TEYMQQLLERERELTVERDELAARKQALDEEIERLS-------Q 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1098 RAEELLAQLGRKEDELQAALLrAE-------EE--------GGARAQL----LKSLREAQAGLAEAQEDL---------- 1148
Cdd:PRK04863 667 PGGSEDPRLNALAERFGGVLL-SEiyddvslEDapyfsalyGPARHAIvvpdLSDAAEQLAGLEDCPEDLyliegdpdsf 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1149 -----EAERVARAKAEKQ-----------------RRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALEE 1206
Cdd:PRK04863 746 ddsvfSVEELEKAVVVKIadrqwrysrfpevplfgRAAREKRIEQLRAEREEL-------AERYATLSFDVQKLQRLHQA 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1207 ESR---AH---------EVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSL------------------------ 1250
Cdd:PRK04863 819 FSRfigSHlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnlladetladrvee 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1251 ------EAEV------------SELKAELSSLQTSRQEGEQKRRR---LESQLQEVQGRS---------------SDSER 1294
Cdd:PRK04863 899 ireqldEAEEakrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDyqqAQQTQRDAKQQAfaltevvqrrahfsyEDAAE 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1295 ARSEAAE-------KLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEA 1366
Cdd:PRK04863 979 MLAKNSDlneklrqRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgAEERA 1058
|
650 660 670
....*....|....*....|....*....|....*...
gi 1039779964 1367 AGLREQMEEEVVA----RERAGRELQSTQAQLSEWRRR 1400
Cdd:PRK04863 1059 RARRDELHARLSAnrsrRNQLEKQLTFCEAEMDNLTKK 1096
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
925-1156 |
4.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 925 SEAEETRARLAARKQELELVVTELEArvgeeeecsrqLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKF 1004
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDA-----------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1005 EEDL----LLLEDQNSKLSKERRLLE--------ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQ 1072
Cdd:COG3883 85 REELgeraRALYRSGGSVSYLDVLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1073 ELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAER 1152
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
....
gi 1039779964 1153 VARA 1156
Cdd:COG3883 245 SAAG 248
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1144-1355 |
4.54e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.31 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1144 AQEDLEAERVARAKAEKQRRDLGEELealRGELEdtldstnAQQELRSKREQEVTELKKALEEESRAHEVSMQ------- 1216
Cdd:PLN03188 1045 PEKKLEQERLRWTEAESKWISLAEEL---RTELD-------ASRALAEKQKHELDTEKRCAEELKEAMQMAMEgharmle 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1217 ---ELRQRHSQALVEMAEQLE--------QARRG-KGVWEKTRLSLEAEVSELKAElsslqtsrqeGEQKRRRLESQLQE 1284
Cdd:PLN03188 1115 qyaDLEEKHIQLLARHRRIQEgiddvkkaAARAGvRGAESKFINALAAEISALKVE----------REKERRYLRDENKS 1184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 1285 VQGRSSDSERARSEAAEKLQRAQAELESVSTALS---EAESKAIRLGKELSSA----ESQLHDTQELLQEETRAKLAL 1355
Cdd:PLN03188 1185 LQAQLRDTAEAVQAAGELLVRLKEAEEALTVAQKramDAEQEAAEAYKQIDKLkrkhENEISTLNQLVAESRLPKEAI 1262
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
873-1174 |
5.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 873 EVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARV 952
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 953 GEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEF 1032
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1033 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1112
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1113 LQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRG 1174
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
875-1374 |
6.05e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 875 LQARAQELQKVQELQQQSAREVGELQGRVAQLEE-ERTRLAEQLRAEAELCSEAEEtrarlaarKQELELVVTELEArvg 953
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKsHSITLKEIERLSIEYNNAMDD--------YNNLKSALNELSS--- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 954 eeeecsrqLQSEKKRLQQHIQELESHLEAEEGARQKL-----QLEKVTTEAKMKKFEE---------DLL----LLEDQN 1015
Cdd:PRK01156 247 --------LEDMKNRYESEIKTAESDLSMELEKNNYYkeleeRHMKIINDPVYKNRNYindyfkyknDIEnkkqILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1016 SKLSKERRLLE--ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV 1093
Cdd:PRK01156 319 AEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1094 EQKQRAEELLAQLgrkeDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV--------ARAKAEKQRRDL 1165
Cdd:PRK01156 399 IQEIDPDAIKKEL----NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlGEEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1166 GEELEALRGEL--------------------------EDTLDSTNAQQELRSKREQ------EVTELK----KALEEESR 1209
Cdd:PRK01156 475 NEKKSRLEEKIreieievkdidekivdlkkrkeylesEEINKSINEYNKIESARADledikiKINELKdkhdKYEEIKNR 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1210 AHEVSMQELRQRHSQALVEMAE----QLEQARRGKGVWEKTRLSLEAEVSELKAEL----SSLQTSRQEGEQKRRRLESQ 1281
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddkSYIDKSIREIENEANNLNNK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1282 LQEVQGRSSDSERARsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA 1361
Cdd:PRK01156 635 YNEIQENKILIEKLR-GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
570
....*....|...
gi 1039779964 1362 LEAEAAGLREQME 1374
Cdd:PRK01156 714 LSDRINDINETLE 726
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1137-1393 |
6.11e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1137 AQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEesrahevsmq 1216
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1217 eLRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAE-VSELkaeLSSLQTSRQEGEQKRRRLESQLQEVQgrssDSERA 1295
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsFSDF---LDRLSALSKIADADADLLEELKADKA----ELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1296 RSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEE 1375
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*...
gi 1039779964 1376 EVVARERAGRELQSTQAQ 1393
Cdd:COG3883 229 AAAAAAAAAAAAAAAASA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1610-1933 |
6.48e-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: 44.94 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1610 ERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMkelwREVEETRSSR 1689
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL----RQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1690 DEMftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAsgNLSKAATLEEKR-----QLEGRLSQLEE 1764
Cdd:COG3096 354 EDL----EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA--DYQQALDVQQTRaiqyqQAVQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1765 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGE---EDAGARARQKMLIAALE 1841
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEverSQAWQTARELLRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1842 SKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEksnlrlkQLKRQLEEAEEEASRAQAGR 1921
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQAAEAVEQR 580
|
330
....*....|..
gi 1039779964 1922 RRLQRELEDVTE 1933
Cdd:COG3096 581 SELRQQLEQLRA 592
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
904-1263 |
6.78e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 904 AQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAE 983
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 984 EGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDR 1063
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1064 LKKEEKGRQELEKLKRRldgesSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAE 1143
Cdd:COG4372 166 LAALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1144 AQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHS 1223
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039779964 1224 QALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1263
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
880-1163 |
7.75e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 880 QELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRaeaELCSEAEETRARlaaRKQELELVvtelearvgeeeecs 959
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK---ELREEAQELREK---RDELNEKV--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 960 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERrllEERLAEFSSQAAEE 1039
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1040 EEKVKSLNKLRLKyeatISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1119
Cdd:COG1340 149 LEKAKKALEKNEK----LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039779964 1120 AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1163
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1112-1284 |
8.03e-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: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1112 ELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEdtlDSTNAQQELRS 1191
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1192 KREQEvtelkkALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEG 1271
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 1039779964 1272 EQKRRRLESQLQE 1284
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1020-1235 |
8.35e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1020 KERRLLEERLAEFSSQAAEEEEK-------VKSLNKLRLKyeatiSDMEDRLKKE-------EKGRQELEKLKRRLDGES 1085
Cdd:COG0497 165 RAWRALKKELEELRADEAERAREldllrfqLEELEAAALQ-----PGEEEELEEErrrlsnaEKLREALQEALEALSGGE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1086 SELQEQMveqkQRAEELLAQLGRKEDELQAALLRAEEeggARAQLlkslREAQAGLAEAQEDLEA---------ERVARA 1156
Cdd:COG0497 240 GGALDLL----GQALRALERLAEYDPSLAELAERLES---ALIEL----EEAASELRRYLDSLEFdperleeveERLALL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1157 KAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEEsrAHEVSmqELRQRHSQALVE-MAEQLE 1234
Cdd:COG0497 309 RRLARKyGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEA--AEKLS--AARKKAAKKLEKaVTAELA 384
|
.
gi 1039779964 1235 Q 1235
Cdd:COG0497 385 D 385
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1246-1630 |
8.37e-04 |
|
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: 44.18 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1246 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQgrssDSERARSEAAEKLQRAQAELESVStALSEAESKAI 1325
Cdd:COG5185 185 TLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKA----KEIINIEEALKGFQDPESELEDLA-QTSDKLEKLV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1326 RLGKELSsaESQLHDTQELLQeetraklalgsRVRALEAEAAGLREQMEEEVVARERAG---RELQSTQAQLSEWRRRQE 1402
Cdd:COG5185 260 EQNTDLR--LEKLGENAESSK-----------RLNENANNLIKQFENTKEKIAEYTKSIdikKATESLEEQLAAAEAEQE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1403 EEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDlgqqkQLLSTLEKKQRKFDQLLAEEK 1482
Cdd:COG5185 327 LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELD-----SFKDTIESTKESLDEIPQNQR 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1483 AA---VLRAVEDRERIEAEGREREARALsltraleeeqearEELERQNRALRAELEALLSSKDDVGKNVHELERAR--KA 1557
Cdd:COG5185 402 GYaqeILATLEDTLKAADRQIEELQRQI-------------EQATSSNEEVSKLLNELISELNKVMREADEESQSRleEA 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039779964 1558 AEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEER 1630
Cdd:COG5185 469 YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
883-1163 |
8.79e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 883 QKVQELQQqsarEVGELQGRVAQLEEERTRLAEQLRAEAELCSEA----EETRARLAARKQELELV---VTELEARVGEE 955
Cdd:PRK11637 47 DQLKSIQQ----DIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrklRETQNTLNQLNKQIDELnasIAKLEQQQAAQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 956 EE-CSRQLQSeKKRLQQHiQELESHLEAEEGARQK--LQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERLAEF 1032
Cdd:PRK11637 123 ERlLAAQLDA-AFRQGEH-TGLQLILSGEESQRGEriLAYFGYLNQARQETIAE----LKQTREELAAQKAELEEKQSQQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1033 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEekgrqeleklkrrldgesselQEQMVEQKQraeellaqlgrKEDE 1112
Cdd:PRK11637 197 KTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD---------------------QQQLSELRA-----------NESR 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039779964 1113 LQAALLRAEEEGGARAQllkslREAQaglaeaqedlEAERVARAKAEKQRR 1163
Cdd:PRK11637 245 LRDSIARAEREAKARAE-----REAR----------EAARVRDKQKQAKRK 280
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
908-1305 |
1.04e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 908 EERTRLAEQLRAEAELCSEAEETRARLAARKQELelvvTELEARVGEEEEC-SRQLQSEKKRLQQHIQEleshleAEEGA 986
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSEL----KPSGQGGLDEEEAfLDRTAKREERRQKRLQE------ALERQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 987 RQklqLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLlEERLAEfssqAAEEEEKVKSLNKLRLKYEATISDMEDRLKK 1066
Cdd:pfam02029 87 KE---FDPTIADEKESVAERKENNEEEENSSWEKEEKR-DSRLGR----YKEEETEIREKEYQENKWSTEVRQAEEEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1067 EEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQE 1146
Cdd:pfam02029 159 EEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1147 DLEAERVARAKAEKQRRDLGEelealrgeledtldstnaqqelrsKREQEvtelkkaleeesrahevsMQELRQRHSQAL 1226
Cdd:pfam02029 239 EAEVFLEAEQKLEELRRRRQE------------------------KESEE------------------FEKLRQKQQEAE 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 1227 VEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAelsslqtsrQEGEQKRRRLEsqlqevqgrssDSERARSEAAEKLQR 1305
Cdd:pfam02029 277 LELEELKKKREERRKLLEEEEQRRKQEEAERKL---------REEEEKRRMKE-----------EIERRRAEAAEKRQK 335
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1425-1634 |
1.04e-03 |
|
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: 43.60 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1425 LTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREA 1504
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1505 RALSLTRALEEEQEAREELERQ----NRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAE 1580
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1581 DAKLRLEVTVQALKAQhERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRA 1634
Cdd:COG4942 192 ALKAERQKLLARLEKE-LAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1224-1358 |
1.08e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1224 QALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLqtsrqegEQKRRRLESQLQEVQGrssdserARSEAAEKL 1303
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAA-------EAERSRLQALLAELAG-------AGAAAEGRA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1304 QRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ------EETRAKLA-LGSR 1358
Cdd:PRK09039 119 GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDasekrdRESQAKIAdLGRR 180
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
881-1059 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 881 ELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcSEAEETRARLAARKQELELVVTELEARVGEEEECSR 960
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARL-------EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 961 QLQSEKKrLQQHIQELESHleaeegARQKLQLEKVTTEAkMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEE 1040
Cdd:COG1579 84 NVRNNKE-YEALQKEIESL------KRRISDLEDEILEL-MERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*....
gi 1039779964 1041 EKVKSLNKLRLKYEATISD 1059
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
890-1178 |
1.16e-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: 44.17 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 890 QQSAREVGELQGRVAQLEEERTRLAEQLRAeaelcseaeeTRARLAARKQELELVV----TELEARVGEEEECSRQLQSE 965
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQ----------LKEQLQLLNKLLPQANlladETLADRLEELREELDAAQEA 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 966 KKRLQQH---IQELESHLEA--------EEGARQKLQLEKVTTEAKMKKFE-------------EDLLLLEDQNSKLSKE 1021
Cdd:COG3096 909 QAFIQQHgkaLAQLEPLVAVlqsdpeqfEQLQADYLQAKEQQRRLKQQIFAlsevvqrrphfsyEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1022 rrlLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLkkeEKGRQELEKLKRRLD---------------GESS 1086
Cdd:COG3096 989 ---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELEelgvqadaeaeerarIRRD 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1087 ELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAE-----AQEDLEAERVARA----K 1157
Cdd:COG3096 1063 ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAvlrlaRDNDVERRLHRRElaylS 1142
|
330 340
....*....|....*....|.
gi 1039779964 1158 AEKQRRDLGEELEALRGELED 1178
Cdd:COG3096 1143 ADELRSMSDKALGALRLAVAD 1163
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1661-1949 |
1.18e-03 |
|
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: 43.96 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1661 KEEAVKQLKKMQVQMKELWREVEETRSSR----DEMFTLSRENEKKLKGLEAEVLRLQEElaasDRARRQAQQDRDEMAE 1736
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1737 EVasgnlSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQ 1816
Cdd:pfam17380 373 EI-----SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1817 ELRARLGEEDagaRARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRA-EKRLKEVVLQVDEERRVADQVRDQLEK 1895
Cdd:pfam17380 448 MERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1896 snlrlkqlkRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMnREVTTLRNRL 1949
Cdd:pfam17380 525 ---------RQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1264-1895 |
1.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1264 LQTSRQEGEQKRRRLESQLQevqgrssdserARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQE 1343
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIK-----------RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1344 LLQEETRAKLALGSR---VRALEAEAAGLREQMEEevvaRERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAR 1420
Cdd:PRK03918 236 LKEEIEELEKELESLegsKRKLEEKIRELEERIEE----LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1421 EAETLTqRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFdqllaeEKAAVLRAVEDRERIEAEGR 1500
Cdd:PRK03918 312 IEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY------EEAKAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1501 EREAralsltraleeeqeareelerqnraLRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDeltaae 1580
Cdd:PRK03918 385 TPEK-------------------------LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK------ 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1581 dAKLRLEVTVQALKAQHERDLQGRDDAG-----------EERRRQLAKQLRDAEVERDEERKQRALAMAARKKlelelee 1649
Cdd:PRK03918 434 -AKGKCPVCGRELTEEHRKELLEEYTAElkriekelkeiEEKERKLRKELRELEKVLKKESELIKLKELAEQL------- 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1650 lkaqtsaagqgkEEAVKQLKKMQVQ-MKELWREVEETRSsrdemftLSRENEKKLKGLEAEVLRLQE---ELAASDRARR 1725
Cdd:PRK03918 506 ------------KELEEKLKKYNLEeLEKKAEEYEKLKE-------KLIKLKGEIKSLKKELEKLEElkkKLAELEKKLD 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1726 QAQQDRDEMAEEVASGNLSKAATLEEK-RQLEGRLSQLEEELEEEQNNSELLKdhyrklvlQVESLTTELSAERSFSAKA 1804
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEK--------ELKKLEEELDKAFEELAET 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1805 ESGRQQLERQIQELRARLGEEDAgARARQKMLiaALESKLAqaeeqleqesrerilsgklvrRAEKRLKEVVLQVDEERR 1884
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEY-EELREEYL--ELSRELA---------------------GLRAELEELEKRREEIKK 694
|
650
....*....|.
gi 1039779964 1885 VADQVRDQLEK 1895
Cdd:PRK03918 695 TLEKLKEELEE 705
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1084-1538 |
1.25e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.08 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1084 ESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV--ARAKAEKQ 1161
Cdd:COG3899 763 EAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARAlfNLGFILHW 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1162 RRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKG 1241
Cdd:COG3899 843 LGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLA 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1242 VWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvsTALSEAE 1321
Cdd:COG3899 923 AAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALE---AAAAALL 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1322 SKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1401
Cdd:COG3899 1000 ALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAA 1079
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1402 EEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEE 1481
Cdd:COG3899 1080 AAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLAL 1159
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1482 KAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL 1538
Cdd:COG3899 1160 ALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
865-1133 |
1.28e-03 |
|
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: 43.81 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 865 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV 944
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 945 VTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLL-LEDQNSKLSKERR 1023
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLkYEEEPEELLLEEA 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1024 LLEERLAEFSSQaaEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1103
Cdd:pfam02463 946 DEKEKEENNKEE--EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
250 260 270
....*....|....*....|....*....|
gi 1039779964 1104 AQLGRKEDELQAalLRAEEEGGARAQLLKS 1133
Cdd:pfam02463 1024 ELFVSINKGWNK--VFFYLELGGSAELRLE 1051
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1065-1321 |
1.32e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.26 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1065 KKEEKGRQELEKLKRrLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREaqagLAEA 1144
Cdd:pfam15905 63 KKSQKNLKESKDQKE-LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE----LTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1145 QEDLEAeRVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEV-TELKKALEEESRAHE--VSMQELRQR 1221
Cdd:pfam15905 138 NELLKA-KFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTqKNLEHSKGKVAQLEEklVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1222 ---HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQK-RRRLESQLQEVQGRSSDSERARS 1297
Cdd:pfam15905 217 eksETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQElSKQIKDLNEKCKLLESEKEELLR 296
|
250 260
....*....|....*....|....
gi 1039779964 1298 EAAEKLQRAQAELESVSTALSEAE 1321
Cdd:pfam15905 297 EYEEKEQTLNAELEELKEKLTLEE 320
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1110-1385 |
1.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1110 EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQEL 1189
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1190 RSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRgkgvwektrlSLEAEVSELKAELSSLQTSRQ 1269
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA----------ELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1270 EGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEET 1349
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 1039779964 1350 RAKLALGSRVRALEAEAAGLREQMEEEVVARERAGR 1385
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
867-1147 |
1.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 867 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 946
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 947 ELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE 1026
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1027 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1106
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039779964 1107 GRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQED 1147
Cdd:COG4372 300 LLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1216-1388 |
1.45e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.85 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1216 QELRQRHSqalvemAEQLEQARRGkgvwektRLSLEAEVSELKAElsslqtsrqegEQKRRRLESQLQEVQGRSSDSERA 1295
Cdd:PTZ00491 664 QEAAARHQ------AELLEQEARG-------RLERQKMHDKAKAE-----------EQRTKLLELQAESAAVESSGQSRA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1296 RSEAaeklqRAQAELESVSTALSEAE--SKAIRLGKELSSAESQLHDTQELLQEETRAKLALgSRVRAL-EAEAAGLREQ 1372
Cdd:PTZ00491 720 EALA-----EAEARLIEAEAEVEQAElrAKALRIEAEAELEKLRKRQELELEYEQAQNELEI-AKAKELaDIEATKFERI 793
|
170 180
....*....|....*....|
gi 1039779964 1373 ME----EEVVARERAGRELQ 1388
Cdd:PTZ00491 794 VEalgrETLIAIARAGPELQ 813
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1447-1708 |
1.60e-03 |
|
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: 43.57 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1447 QQELDDATVDLGQQKQLLSTLEKKQRKFDQ---LLAEEKAAVLRAVEDRERIEAEGREREAR-------ALSLTRALEEE 1516
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEERKRELErirqeeiAMEISRMRELE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1517 QEAREELErQNRALRAELEALLSSK-------DDVGKNVHELERARKAAEQAAS-DLRTQVTELEDELTAAEDAKLRLEV 1588
Cdd:pfam17380 382 RLQMERQQ-KNERVRQELEAARKVKileeerqRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQQ 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1589 TVQALKAQH-ERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQ 1667
Cdd:pfam17380 461 QVERLRQQEeERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1039779964 1668 LKKMQVQMKE------LWREVEETRSSRD------EMFTLSRENEKKLKGLEA 1708
Cdd:pfam17380 541 ERRKQQEMEErrriqeQMRKATEERSRLEamererEMMRQIVESEKARAEYEA 593
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1786-1929 |
1.64e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1786 QVESLTTELSAERSFSAKAESGRQQLERQIQelrarlGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLV 1865
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLG------SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 1866 RRAEKRLKEVVLQVDEE-RRVADQVRDQLEKSNLRLKQLKRQLEE---AEEEASRAQAGRRRLQRELE 1929
Cdd:COG3206 294 IALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVE 361
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
871-1115 |
1.69e-03 |
|
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: 43.51 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 871 QDEVLQARAQELQKV--QELQQQSARevgeLQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVvtel 948
Cdd:pfam13166 262 GQPLPAERKAALEAHfdDEFTEFQNR----LQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVL---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 949 earvgeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAK--MKKFEEDLLLLEDQNSKLSKERRLLE 1026
Cdd:pfam13166 334 ----------NSQLDGLRRALEAKRKDPFKSIELDSVDAKIESINDLVASINelIAKHNEITDNFEEEKNKAKKKLRLHL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1027 erLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKgrqELEKLkrrlDGESSELQEQMVEQKQRAEE---LL 1103
Cdd:pfam13166 404 --VEEFKSEIDEYKDKYAGL-------EKAINSLEKEIKNLEA---EIKKL----REEIKELEAQLRDHKPGADEinkLL 467
|
250
....*....|..
gi 1039779964 1104 AQLGRKEDELQA 1115
Cdd:pfam13166 468 KAFGFGELELSF 479
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1137-1408 |
1.91e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1137 AQAGLAEAQEDL--EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQevtelkkaleeesrahevs 1214
Cdd:PRK11281 24 SAFARAASNGDLptEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQ------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1215 mqeLRQRHSQAlvemAEQLEQARRgkgvwEKTRLSlEAEVSELKAELSSLQTsrqegeqkrRRLESQLQEVQgrssdser 1294
Cdd:PRK11281 85 ---LKQQLAQA----PAKLRQAQA-----ELEALK-DDNDEETRETLSTLSL---------RQLESRLAQTL-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1295 arseaaEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLAL-GSRVRALEAEAAGLREQM 1373
Cdd:PRK11281 135 ------DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALrPSQRVLLQAEQALLNAQN 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1039779964 1374 EEEvvARERAGRE-LQST-QAQ---LSEWRRRQEEEAAVL 1408
Cdd:PRK11281 209 DLQ--RKSLEGNTqLQDLlQKQrdyLTARIQRLEHQLQLL 246
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
889-1076 |
1.95e-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: 41.83 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 889 QQQSAREVGELQGRVAQLEEERTRLAEQLraeAELCSEAEETRARLAARKQELElvvtelearvgeeeecsrQLQSEKKR 968
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAEL---AELEDELAALEARLEAAKTELE------------------DLEKEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 969 LQQHIQELESHLEaeegaRQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKS--- 1045
Cdd:COG1579 64 LELEIEEVEARIK-----KYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAElea 138
|
170 180 190
....*....|....*....|....*....|..
gi 1039779964 1046 -LNKLRLKYEATISDMEDRLKKEEKGRQELEK 1076
Cdd:COG1579 139 eLEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1079-1703 |
2.14e-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: 43.20 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1079 RRLDGESSELQEQMVEQKQRAEELLAQLgrkedelqAALLRAEEEGGARAQllkSLREAQAGlaeaqedleAERVARAKA 1158
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMEL--------DALAVAEKAGQAEAE---GLRAALAG---------AEMVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1159 EKQRRDLgEELEALrgeledtldstnaQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARR 1238
Cdd:pfam07111 136 EGSQREL-EEIQRL-------------HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1239 GKGVWEKTRLSLEAEVSELKA------ELSSLQTSRQEGEQKRRRLESQLQEVQgrssdSERARSEAAEKLqrAQAELES 1312
Cdd:pfam07111 202 LRKQLSKTQEELEAQVTLVESlrkyvgEQVPPEVHSQTWELERQELLDTMQHLQ-----EDRADLQATVEL--LQVRVQS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1313 VSTALSEAESKAIRLGKELSSAESQL-HDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVvareragrelqstq 1391
Cdd:pfam07111 275 LTHMLALQEEELTRKIQPSDSLEPEFpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQV-------------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1392 AQLSEWRRRQEEEAAVLEageearrraareaetltQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKK- 1470
Cdd:pfam07111 341 AELQEQVTSQSQEQAILQ-----------------RALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQl 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1471 ----------QRKFDQLLAEEKAAVLRAVEDRERIEAEGRERE------ARALSLTRALEEEQEAREELERQNRALRAEL 1534
Cdd:pfam07111 404 kfvvnamsstQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglmARKVALAQLRQESCPPPPPAPPVDADLSLEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1535 EALLSSKDDVGKNV--------HELERARKAAEQAASDLRTQVTELEDELTAAEDA----KLRLEVTVQA---------- 1592
Cdd:pfam07111 484 EQLREERNRLDAELqlsahliqQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlasvGQQLEVARQGqqesteeaas 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1593 ----LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVK-Q 1667
Cdd:pfam07111 564 lrqeLTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKeE 643
|
650 660 670
....*....|....*....|....*....|....*.
gi 1039779964 1668 LKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKL 1703
Cdd:pfam07111 644 GQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRL 679
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1117-1593 |
2.29e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.08 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1117 LLRAEEEGGARAQLLKSLRE-AQAGLAEAQEDLEAER---------VARAKAEKQRRDLGEELEALRGELEDTLDstnAQ 1186
Cdd:COG3903 456 LEVEGGGGGPRYRLLETVREyAAERLAEAGERAAARRrhadyylalAERAAAELRGPDQLAWLARLDAEHDNLRA---AL 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1187 QELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQT 1266
Cdd:COG3903 533 RWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1267 SRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ 1346
Cdd:COG3903 613 AAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAA 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1347 EETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLT 1426
Cdd:COG3903 693 ALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAAL 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1427 QRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEkkqrkfDQLLAEEKAAVLRAVEDRERIEAEGREREARA 1506
Cdd:COG3903 773 AALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAA------ALAAAAAAAAAAAAALAAALAAAAAAAAAAAA 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1507 LSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRL 1586
Cdd:COG3903 847 AAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAA 926
|
....*..
gi 1039779964 1587 EVTVQAL 1593
Cdd:COG3903 927 AAAAAAA 933
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
928-1094 |
3.19e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 928 EETRARLAARKQELELVVTELEARvgeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKF--- 1004
Cdd:PHA02562 205 EEQRKKNGENIARKQNKYDELVEE-------AKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqkv 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1005 -------------------EEDLLL-LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA---TISDME 1061
Cdd:PHA02562 278 ikmyekggvcptctqqiseGPDRITkIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTnkqSLITLV 357
|
170 180 190
....*....|....*....|....*....|...
gi 1039779964 1062 DRLKKEEKGRQELEKLKRRLDGESSELQEQMVE 1094
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
873-992 |
3.25e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 873 EVLQARAQELQKVQElqqQSAREVGELQGRVAQLEEERTRLAEQLRA-EAELCSEAEET-RARLAARKQELELVVTELEA 950
Cdd:PRK00409 519 NELIASLEELERELE---QKAEEAEALLKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039779964 951 RVGEEEEC--SRQLQSEKKRLQQHIQELESHLEAEEGARQKLQL 992
Cdd:PRK00409 596 LQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
923-1263 |
3.41e-03 |
|
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: 42.36 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 923 LCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELE--SHLEAEEGARQKLQLEKVTTEAK 1000
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIkrKKNSALSEALNGFKYEANFKSRL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1001 MKKFEEDLlllEDQNSKLSKERRllEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEekgrQELEKLKRR 1080
Cdd:pfam13166 167 LREIEKDN---FNAGVLLSDEDR--KAALATVFSDNKPEIAPLTFNVIDFDALEKAEILIQKVIGKS----SAIEELIKN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1081 LD-----GESSELQEQMVEQ---------KQRAEELLAQLGRKEDELQAALLR-AEEEGGARAQLLKSLreaQAGLAEAQ 1145
Cdd:pfam13166 238 PDladwvEQGLELHKAHLDTcpfcgqplpAERKAALEAHFDDEFTEFQNRLQKlIEKVESAISSLLAQL---PAVSDLAS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1146 EDLEAERvARAKAEKQRRDLGEELEALRGELE-----------------------DTLDSTNAQQELRSKREQEVTELKK 1202
Cdd:pfam13166 315 LLSAFEL-DVEDIESEAEVLNSQLDGLRRALEakrkdpfksieldsvdakiesinDLVASINELIAKHNEITDNFEEEKN 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1203 ALEEESRAHEVS-MQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1263
Cdd:pfam13166 394 KAKKKLRLHLVEeFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1033-1158 |
3.58e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1033 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1112
Cdd:COG2433 377 SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1039779964 1113 LQAAlLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEaERVARAKA 1158
Cdd:COG2433 457 ERRE-IRKDREISRLDREIERLERELEEERERIEELK-RKLERLKE 500
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
894-1079 |
3.77e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 894 REVGELQGRVAQLEEERTRLAEQ---LRAE-AELCSEAEETRARLAARKQELELVVTELEARVGEEEECSR------QLQ 963
Cdd:COG2433 399 REKEHEERELTEEEEEIRRLEEQverLEAEvEELEAELEEKDERIERLERELSEARSEERREIRKDREISRldreieRLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 964 SEKKRLQQHIQELESHLEAEEGARQKLQ---------LEKVTTEA------KMKKFEEDLLLLEDQNSKLSKERRLLEE- 1027
Cdd:COG2433 479 RELEEERERIEELKRKLERLKELWKLEHsgelvpvkvVEKFTKEAirrleeEYGLKEGDVVYLRDASGAGRSTAELLAEa 558
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1028 ------RLAEFSSQAAE------------EEEKVKSLNKL----RLKYEATISDMEDRLKKEEKgRQELEKLKR 1079
Cdd:COG2433 559 gpraviVPGELSEAADEvlfeegipvlpaEDVTIQEVDDLavvdEEELEAAIEDWEERAEERRR-EKKAEMLER 631
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
877-1162 |
3.99e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 877 ARAQELQKVQELQQQsarevgelqgrvAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELElvvtELEARVGEEE 956
Cdd:pfam15558 15 ARHKEEQRMRELQQQ------------AALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKE----QRKARLGREE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 957 EcsRQLQSEKKRLQQHIQELESHLEAEEGARQKlQLEKVTTEAKMKKFEEDLLLLED---QNSKLSKERRLLEERLAEFS 1033
Cdd:pfam15558 79 R--RRADRREKQVIEKESRWREQAEDQENQRQE-KLERARQEAEQRKQCQEQRLKEKeeeLQALREQNSLQLQERLEEAC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1034 S----QAAEEEEKVKSLN-KLRLKYEATISDMEDRLKKEEKGRQ-ELEKLKRRldgeSSELQEQMVEQkqRAEELLAQLG 1107
Cdd:pfam15558 156 HkrqlKEREEQKKVQENNlSELLNHQARKVLVDCQAKAEELLRRlSLEQSLQR----SQENYEQLVEE--RHRELREKAQ 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1039779964 1108 RKEDELQAALLRAEEEGGARAQLLKSLREAqAGLAEAQEDLEAERVARAKAEKQR 1162
Cdd:pfam15558 230 KEEEQFQRAKWRAEEKEEERQEHKEALAEL-ADRKIQQARQVAHKTVQDKAQRAR 283
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
881-1324 |
4.02e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 881 ELQKVQELQQQSAREVGELQGRVAQLEEERTRLA---EQLRAEAELCSEAEETRARLAARKQELELVVTELearvgeeEE 957
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQqenKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQL-------QE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 958 CSRQLQSEKKRLQQHIQELESHLeAEEGARQKlQLEKVTTEAKMKKFEEDllLLEDQNSKLSKERRLLE------ERLAE 1031
Cdd:pfam05622 74 ENFRLETARDDYRIKCEELEKEV-LELQHRNE-ELTSLAEEAQALKDEMD--ILRESSDKVKKLEATVEtykkklEDLGD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1032 FSSQaaeeeekVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgesSELQEQMVEQKQRAEELLAQLGRKED 1111
Cdd:pfam05622 150 LRRQ-------VKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1112 ELqAALLRAEEeggaraqllkSLREAQAGLAEAQEDLEAervarakAEKQRRDLGEElEALRGELEDTLDSTNAqqelrs 1191
Cdd:pfam05622 219 KL-EALQKEKE----------RLIIERDTLRETNEELRC-------AQLQQAELSQA-DALLSPSSDPGDNLAA------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1192 krEQEVTELKKALEEesRAHEVSMQELRQRHS--QALVEMAEQLEQARRGK-GVWEKTRLSLEaEVSELKAELSSLQTSR 1268
Cdd:pfam05622 274 --EIMPAEIREKLIR--LQHENKMLRLGQEGSyrERLTELQQLLEDANRRKnELETQNRLANQ-RILELQQQVEELQKAL 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779964 1269 QEGEQKRRrlesqlqevqgRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKA 1324
Cdd:pfam05622 349 QEQGSKAE-----------DSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ 393
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1112-1403 |
4.26e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1112 ELQAALLRAEEE---GGARAQLLKSLREAQAGLAEAQEDLEAERVARakaekqRRDLGEELEALRGELEDTLDSTNAQQE 1188
Cdd:NF041483 82 QIQADQLRADAErelRDARAQTQRILQEHAEHQARLQAELHTEAVQR------RQQLDQELAERRQTVESHVNENVAWAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1189 -LRSKREQEVtelkKALEEESRAhevsmqELRQRHSQALVEMAEQLEQARRgkgvwektRLSLEAEVSELKAElSSLQTS 1267
Cdd:NF041483 156 qLRARTESQA----RRLLDESRA------EAEQALAAARAEAERLAEEARQ--------RLGSEAESARAEAE-AILRRA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1268 RQEGEQKRRRLESQLQEV-----QGRSS---DSERAR--------------SEAAEKLQRAQAELESVstaLSEAESKAi 1325
Cdd:NF041483 217 RKDAERLLNAASTQAQEAtdhaeQLRSStaaESDQARrqaaelsraaeqrmQEAEEALREARAEAEKV---VAEAKEAA- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1326 rlGKELSSAESQ--------LHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAgRELQSTQAQLSEW 1397
Cdd:NF041483 293 --AKQLASAESAneqrtrtaKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKART-VAAEDTAAQLAKA 369
|
....*.
gi 1039779964 1398 RRRQEE 1403
Cdd:NF041483 370 ARTAEE 375
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
910-1068 |
4.61e-03 |
|
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: 41.86 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 910 RTRLAEQLRAEAELCSEAEETRARLAARKQELElvvteleARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQK 989
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQEQLERA-------EKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 990 LQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----------RRLLEERLAEFSSQAAE--EEEKVKSLNKLRLKYEATI 1057
Cdd:pfam15709 412 LQLQAAQERARQQQEEFRRKLQELQRKKQQEEaeraeaekqrQKELEMQLAEEQKRLMEmaEEERLEYQRQKQEAEEKAR 491
|
170
....*....|.
gi 1039779964 1058 SDMEDRLKKEE 1068
Cdd:pfam15709 492 LEAEERRQKEE 502
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1136-1346 |
4.96e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 40.96 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1136 EAQAGLAEAQEDLEAERVARAKAEKQRRDLgeELEALRGELEDTLdstNAQQELRSKREQEVTELKKALEEESRAHE-VS 1214
Cdd:pfam17045 27 EGQTRALETRLDIREEELLSARNTLERKHK--EIGLLRQQLEELE---KGKQELVAKYEQQLQKLQEELSKLKRSYEkLQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1215 MQELRQRHSQA---------LVEMAEQLEQARRGKGVWEKTRL-------SLEAEVSELKAELSSLQTS--RQEGEQKRR 1276
Cdd:pfam17045 102 RKQLKEAREEAksreedrseLSRLNGKLEEFRQKSLEWEQQRLqyqqqvaSLEAQRKALAEQSSLIQSAayQVQLEGRKQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1277 RLESQLQEVQGRSSDSERARseaaEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ 1346
Cdd:pfam17045 182 CLEASQSEIQRLRSKLERAQ----DSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQ 247
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1245-1396 |
5.19e-03 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 41.13 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1245 KTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQevqgrssdSERARSEAA----EKLQRAQAELESvstALSEA 1320
Cdd:pfam14915 56 KTVFQYNGQLNVLKAENTMLNSKLENEKQNKERLETEVE--------SYRSRLAAAiqdhEQSQTSKRDLEL---AFQRE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779964 1321 ESKAIRLGKELSSAESQLHDTQELL-QEETRAKlalgSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSE 1396
Cdd:pfam14915 125 RDEWLRLQDKMNFDVSNLRDENEILsQQLSKAE----SKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKE 197
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
874-1335 |
5.70e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.43 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 874 VLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVG 953
Cdd:COG5278 70 LLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 954 EEEECsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFS 1033
Cdd:COG5278 150 LMDEI-RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1034 SQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDEL 1113
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1114 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKR 1193
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1194 EQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQ 1273
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039779964 1274 KRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAE 1335
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1796-1888 |
5.96e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1796 AERSFSAKAESGRQQLERQIQELRAR--LGEEDAGARARQKMLIAALESKLAQAEEQLEQ-----ESRERILSGKLVRRA 1868
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSqaLAEAQQQELVALEGLAAELEEKQQELEAQLEQlqekaAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|
gi 1039779964 1869 EKRLKEVVLQVDEERRVADQ 1888
Cdd:PRK11448 223 DQAAKRLELSEEETRILIDQ 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
865-1176 |
6.12e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 865 LLQVTRQDEV--LQARAQELQKVQELQQQSAREVGELQGRV------AQLEEERTRLAEQLRAEAELCSEAEETRARLAA 936
Cdd:PRK04863 790 QLRAEREELAerYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 937 RKQELELV-----------VTELEARVGEEEECSRQLQSEKKRLQQH-------------IQELESHLEAEEgaRQKLQL 992
Cdd:PRK04863 870 AKEGLSALnrllprlnllaDETLADRVEEIREQLDEAEEAKRFVQQHgnalaqlepivsvLQSDPEQFEQLK--QDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 993 EKVTTEAKMKKF--------------EEDLLLLE---DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA 1055
Cdd:PRK04863 948 QQTQRDAKQQAFaltevvqrrahfsyEDAAEMLAknsDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS 1027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1056 TISDMEDRLKKEEkgrQELEKLKRRLDGE--------SSELQEQMVEQKQRAEELLAQLGRKEDELQAallraeeeggar 1127
Cdd:PRK04863 1028 SYDAKRQMLQELK---QELQDLGVPADSGaeerararRDELHARLSANRSRRNQLEKQLTFCEAEMDN------------ 1092
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039779964 1128 aqLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1176
Cdd:PRK04863 1093 --LTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRREL 1139
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
888-1156 |
6.44e-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: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 888 LQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaEETRARLAARKQELELVVTELEARVGEEEecSRQLQSEKK 967
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKEL----------EEAEAALEEFRQKNGLVDLSEEAKLLLQQ--LSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 968 RLQQHIQELESHLEAeegARQKLQLEKVTTEAkmkkfeedlLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLn 1047
Cdd:COG3206 230 EARAELAEAEARLAA---LRAQLGSGPDALPE---------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1048 klrlkyeatisdmedrlkkeekgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGAR 1127
Cdd:COG3206 297 -----------------------RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
250 260
....*....|....*....|....*....
gi 1039779964 1128 AQLLKSLREAQAGLAEAQEDLEAERVARA 1156
Cdd:COG3206 354 RRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1128-1950 |
6.51e-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: 41.86 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1128 AQLLKSLREAQAGLAEAQEDLEaeRVARAKAEKQRR--DLGEELEALRGELEDTLDSTnAQQELRSKREQEVTELKKALE 1205
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRLV--EMARELEELSAResDLEQDYQAASDHLNLVQTAL-RQQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1206 EESrahevsmqelrqrhsQALVEMAEQLEQArrgkgvwEKTRLSLEAEVSELKAELSSLQtsRQEGEQKRRRLESQ---- 1281
Cdd:COG3096 365 EQE---------------EVVEEAAEQLAEA-------EARLEAAEEEVDSLKSQLADYQ--QALDVQQTRAIQYQqavq 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1282 -LQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKairlgkelssaesqLHDTQELLQEETRAKLALGSRVR 1360
Cdd:COG3096 421 aLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQK--------------LSVADAARRQFEKAYELVCKIAG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1361 ALEAEAAGlreqmeeeVVARE--RAGRELQSTQAQLSEWRRRQEEeaavleageearrraareaetLTQRLAEKTEAVER 1438
Cdd:COG3096 487 EVERSQAW--------QTAREllRRYRSQQALAQRLQQLRAQLAE---------------------LEQRLRQQQNAERL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1439 LERARRRLQQELDDATvdlgQQKQLLSTLEKKQRKFDQLLAEekaavlrAVEDRERIEAEGREREARALSLTRALEEEqe 1518
Cdd:COG3096 538 LEEFCQRIGQQLDAAE----ELEELLAELEAQLEELEEQAAE-------AVEQRSELRQQLEQLRARIKELAARAPAW-- 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1519 areelerqnRALRAELEALlsskddvgknvHELERARKAAEQAASDLRTQVTELEDELTAAEDaklRLEVTVQALKAQHE 1598
Cdd:COG3096 605 ---------LAAQDALERL-----------REQSGEALADSQEVTAAMQQLLEREREATVERD---ELAARKQALESQIE 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1599 RDLQGrDDAGEERRRQLAKQL---------------------------RDAEVERDEERKQRALAmaARKKLELELEELK 1651
Cdd:COG3096 662 RLSQP-GGAEDPRLLALAERLggvllseiyddvtledapyfsalygpaRHAIVVPDLSAVKEQLA--GLEDCPEDLYLIE 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1652 AQTSAAGQGKEEAVKQLKKMQVQMKElwREVEETRSSRDEMFTlSRENEKKLKGLEAEVLRLQEELAASdRARRQAQQDR 1731
Cdd:COG3096 739 GDPDSFDDSVFDAEELEDAVVVKLSD--RQWRYSRFPEVPLFG-RAAREKRLEELRAERDELAEQYAKA-SFDVQKLQRL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1732 DEMAEEVASGNLSKA---------ATLEEKR-QLEGRLSQLEEELEEEQNNSELLKDHY---RKLVLQVESLTTELSAER 1798
Cdd:COG3096 815 HQAFSQFVGGHLAVAfapdpeaelAALRQRRsELERELAQHRAQEQQLRQQLDQLKEQLqllNKLLPQANLLADETLADR 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1799 SFSAKAESGR-QQLERQIQELRARLGEEDAgararqkmLIAALESKLAQaEEQLEQESRERILSGKLVRRAEKRLKEVVl 1877
Cdd:COG3096 895 LEELREELDAaQEAQAFIQQHGKALAQLEP--------LVAVLQSDPEQ-FEQLQADYLQAKEQQRRLKQQIFALSEVV- 964
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779964 1878 qvdeERRVA---DQVRDQLEKSNLRLKQLKRQLEeaeeeasRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLR 1950
Cdd:COG3096 965 ----QRRPHfsyEDAVGLLGENSDLNEKLRARLE-------QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRD 1029
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
927-1049 |
6.55e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 927 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLE----KVTTEAKMK 1002
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERElseaRSEERREIR 462
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1039779964 1003 KfEEDLLLLEDQNSKLSKERRLLEERLAEFSsqaaEEEEKVKSLNKL 1049
Cdd:COG2433 463 K-DREISRLDREIERLERELEEERERIEELK----RKLERLKELWKL 504
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
857-965 |
6.71e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 857 RLFIKVKP--LLQVTRQDEVLQARAQELQKvqELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARL 934
Cdd:COG0542 403 RMEIDSKPeeLDELERRLEQLEIEKEALKK--EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 1039779964 935 AARKQELELVVTELEARVGEEEECSRQLQSE 965
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1037-1383 |
7.26e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1037 AEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAA 1116
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1117 LLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE 1196
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1197 VTELKKALEEESRAHEVS-MQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKR 1275
Cdd:COG4372 166 LAALEQELQALSEAEAEQaLDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1276 RRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLAL 1355
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|....*...
gi 1039779964 1356 GSRVRALEAEAAGLREQMEEEVVARERA 1383
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
960-1217 |
7.42e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 960 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKfeedlllLEDQNSKLSKERRLLEERLAEFSSQaaee 1039
Cdd:pfam15905 83 RALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------LEKQLLELTRVNELLKAKFSEDGTQ---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1040 eEKVKSLN----KLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV-------EQKQRAEELLAQLgr 1108
Cdd:pfam15905 152 -KKMSSLSmelmKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVstekekiEEKSETEKLLEYI-- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1109 keDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVArakAEKQRRDLGEELEALRGELEDTLdstNAQQE 1188
Cdd:pfam15905 229 --TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQE---LSKQIKDLNEKCKLLESEKEELL---REYEE 300
|
250 260
....*....|....*....|....*....
gi 1039779964 1189 LRSKREQEVTELKKALEEESRAHEVSMQE 1217
Cdd:pfam15905 301 KEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1249-1360 |
7.51e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1249 SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGR-SSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL 1327
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEeDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1039779964 1328 GK--ELSSAESQLHDTQELLQE------ETRAKLALGSRVR 1360
Cdd:PRK00409 604 VKahELIEARKRLNKANEKKEKkkkkqkEKQEELKVGDEVK 644
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
872-1129 |
9.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 872 DEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaEETRARLAARKQELELVVTELEAR 951
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----------EALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 952 VGEEEECSRQLQsekkRLQQHIQELESHLEAE--EGARQKLQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERL 1029
Cdd:COG3883 85 REELGERARALY----RSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1030 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK 1109
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260
....*....|....*....|
gi 1039779964 1110 EDELQAALLRAEEEGGARAQ 1129
Cdd:COG3883 237 AAAAAAAASAAGAGAAGAAG 256
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1079-1228 |
9.16e-03 |
|
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: 40.48 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1079 RRLDGESSELQEQM---VEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1155
Cdd:pfam00529 54 TDYQAALDSAEAQLakaQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779964 1156 AKAEKQRRDLgEELEALRGELEDTLDSTNAQQE-LRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVE 1228
Cdd:pfam00529 134 PIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLD 206
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1062-1171 |
9.21e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1062 DRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELlaqlgRKEDELQAALLRAEEEGGARAQLLKSLREAQAGL 1141
Cdd:COG2268 220 NREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETA-----RAEAEAAYEIAEANAEREVQRQLEIAEREREIEL 294
|
90 100 110
....*....|....*....|....*....|....*
gi 1039779964 1142 AEA-----QEDLEAERVARAKAEKQRRDLGEELEA 1171
Cdd:COG2268 295 QEKeaereEAELEADVRKPAEAEKQAAEAEAEAEA 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1250-1408 |
9.25e-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: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1250 LEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESkairlGK 1329
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-----NK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039779964 1330 ELSSAESQLhDTQELLQEEtraklalgsrvraLEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVL 1408
Cdd:COG1579 90 EYEALQKEI-ESLKRRISD-------------LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1054-1271 |
9.97e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1054 EATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKs 1133
Cdd:TIGR02794 39 QAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779964 1134 lrEAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEvtELKKALEEESRAHEV 1213
Cdd:TIGR02794 118 --QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE--AKAKAEAEAKAKAEE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039779964 1214 SMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEG 1271
Cdd:TIGR02794 194 AKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| |
