|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-1117 |
4.59e-136 |
|
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: 442.49 E-value: 4.59e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLS-------------------------- 55
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILP-FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKslrserlsdlihsksgafvnsaevei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 56 --------------------QVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMI 115
Cdd:pfam02463 80 tfdnedhelpidkeevsirrRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 116 EEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDT 195
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 196 KVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLA 275
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 276 CEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMAC 355
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 356 KNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQL 435
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 436 SRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGKKLLE 515
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 516 RGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPeLQKAMEFVFGTTFVCDNMDNAKKVAFDKRI 595
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL-DKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 596 MTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEE 675
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 676 ADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKA 755
Cdd:pfam02463 719 AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 756 DASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQ 835
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 836 DTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNNPKEA 915
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEE 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 916 GQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIF 995
Cdd:pfam02463 959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 996 STLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQ 1075
Cdd:pfam02463 1039 YLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVS 1118
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|...
gi 1034663584 1076 NIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFV-DGVST 1117
Cdd:pfam02463 1119 RVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVeNGVST 1161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-1094 |
3.29e-109 |
|
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: 369.39 E-value: 3.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG---------------ISN-------------- 53
Cdd:TIGR02168 2 LKKLELAGFKSFADPTTIN-FDKGITGIVGPNGCGKSNIVDAIRWVLGeqsakalrggkmedvIFNgsetrkplslaeve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 54 --------------LSQVVI------GGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMKPPEILS 113
Cdd:TIGR02168 81 lvfdnsdgllpgadYSEISItrrlyrDGESEYFINGQPCRLKDIQDLFLDTGLGKRS-YSIIEQGKISEIIEAKPEERRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 114 MIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE 193
Cdd:TIGR02168 160 IFEEAAGISKYKERRKETERKLERTRENLDRLEDILNE-LERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 194 DTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGI--------------------LRSLEDAL 253
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneisrleqqkqilrerLANLERQL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 254 AEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAV 333
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 334 SAGLSSNEDGAEAtLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEvkkmdsgyrKDQEALEAVKRLKEKLEA 413
Cdd:TIGR02168 399 NNEIERLEARLER-LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE---------ELQEELERLEEALEELRE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 414 EMKKlnyeenKEESLLEKRRQLSRDIGRLKETyEALLARFPNLRFAYKDPEKN-WNRNCVKGLVASLISVkDTSATTALE 492
Cdd:TIGR02168 469 ELEE------AEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNqSGLSGILGVLSELISV-DEGYEAAIE 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 493 LVAGERLYNVVVDTEVTGKK---LLERGELKRRyTIIPLNKISARCIAPETLRVAQNlvGPDNVHVALSLVEYKPELQKA 569
Cdd:TIGR02168 541 AALGGRLQAVVVENLNAAKKaiaFLKQNELGRV-TFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPKLRKA 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 570 MEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALE 649
Cdd:TIGR02168 618 LSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 650 EELAGLKntaekyrqlKQQWEMKTEEADLLQTKLQQS-SYHKQQEELDALKKTIEESEETLKNT-KEIQRKAEEKYEVLE 727
Cdd:TIGR02168 698 KALAELR---------KELEELEEELEQLRKELEELSrQISALRKDLARLEAEVEQLEERIAQLsKELTELEAEIEELEE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 728 NKMKNAE--AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIE 805
Cdd:TIGR02168 769 RLEEAEEelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 806 VMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKML 885
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 886 KDYDWINAER-HLFGQPNSAY-----------DFKTNNPKEAGQRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYNDLMK 953
Cdd:TIGR02168 929 LRLEGLEVRIdNLQERLSEEYsltleeaealeNKIEDDEEEARRRLKRLENKIKELG-PVNLAAIEEYEELKERYDFLTA 1007
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 954 KKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTWKENL 1032
Cdd:TIGR02168 1008 QKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPEDLLEaGIEIFAQPPGKKNQNL 1087
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034663584 1033 TELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVS 1094
Cdd:TIGR02168 1088 SLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVIT 1149
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1118 |
1.85e-103 |
|
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: 353.22 E-value: 1.85e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGIS--------NLSQVVIGGRNK--------- 64
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIP-FSKGFTVISGPNGSGKSNIGDAILFALGLSsskamraeRLSDLISNGKNGqsgneayvt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 65 ------------------------------YLINGVNANNTRVQDLFCSVGLNVNNPHFlIMQGRITKVLNMKPPEILSM 114
Cdd:TIGR02169 80 vtfknddgkfpdelevvrrlkvtddgkysyYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 115 IEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITpTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAED 194
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 195 TKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNL 274
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 275 -------ACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAt 347
Cdd:TIGR02169 318 edaeerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 348 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEA----VKRLKEKLEAEMKKLNYEEN 423
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqewkLEQLAADLSKYEQELYDLKE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 424 KEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKdpEKNWNRNCVKGLVASLISVKDTSATtALELVAGERLYNVV 503
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE--VLKASIQGVHGTVAQLGSVGERYAT-AIEVAAGNRLNNVV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 504 VDTEVTGKKLLERgeLKR----RYTIIPLNKISARCIAPETLRVaqnlvgPDNVHVALSLVEYKPELQKAMEFVFGTTFV 579
Cdd:TIGR02169 554 VEDDAVAKEAIEL--LKRrkagRATFLPLNKMRDERRDLSILSE------DGVIGFAVDLVEFDPKYEPAFKYVFGDTLV 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 580 CDNMDNAKkvafdkRIM--TRTVTLGGDVFDPHGTLSGGARSQAASILTKFQ---ELKDVQDELRIKENELRALEEELAG 654
Cdd:TIGR02169 626 VEDIEAAR------RLMgkYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSepaELQRLRERLEGLKRELSSLQSELRR 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 655 LKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLE---NKMK 731
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEedlHKLE 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 732 NAEAERERELKDAQKKldcaktKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEavnEAIKSYESQIEvmaaEV 811
Cdd:TIGR02169 779 EALNDLEARLSHSRIP------EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE---KEIQELQEQRI----DL 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 812 AKNKESVNKAQEEVTKQKEVItaqDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWI 891
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEEL---EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 892 NAERHLFGQPNSAYDFKTNNPKE---AGQRLQKLQEMKEKLGRN------VNMRAMNVLTEAEERYNDLMKKKRIVENDK 962
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEiralepVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 963 SKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSL 1042
Cdd:TIGR02169 1003 KAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSL 1082
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 1043 VALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA-NVLFKTKFVDGVSTV 1118
Cdd:TIGR02169 1083 TALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYAdRAIGVTMRRNGESQV 1159
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1107 |
2.58e-70 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 254.86 E-value: 2.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1 MHIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG---ISNL----------------------- 54
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLGeqsAKSLrggkmedvifagsssrkplgrae 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 55 ----------------SQVVI------GGRNKYLINGVNANNTRVQDLFCSVGLNVNNpHFLIMQGRITKVLNMKPPEIL 112
Cdd:COG1196 80 vsltfdnsdgtlpidyDEVTItrrlyrSGESEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 113 SMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEeITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLA 192
Cdd:COG1196 159 AIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGE-LERQLEPLERQAEKAERYRELKEELKELEAELLLLKLREL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 193 EDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKK 272
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 273 NLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDgAEATLAGQM 352
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-ELLEALRAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 353 MACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN----YEENKEESL 428
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLellaELLEEAALL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 429 LEKRRQLSRDIGRLKETYEALL---ARFPNLRFAYKDPEKNWNRNCVKGLVASLISVkDTSATTALELVAGERLYNVVVD 505
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLeaeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQNIVVE 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 506 TEVTGKKLLERGELKR--RYTIIPLNKISARciAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNM 583
Cdd:COG1196 555 DDEVAAAAIEYLKAAKagRATFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 584 DNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASiltkfqelkdvqdELRIKENELRALEEELAglkntaekyr 663
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA-------------ALLEAEAELEELAERLA---------- 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 664 qlkqqwemkteeadllqtklqqssyhKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKD 743
Cdd:COG1196 690 --------------------------EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 744 AQKKLDcaktkadasskkmkEKQQEVEAITLELEELKRehtsykqqleavneaiksyesqievmaaevaknkesvnkaqe 823
Cdd:COG1196 744 EEELLE--------------EEALEELPEPPDLEELER------------------------------------------ 767
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 824 evtkqkevitaqdtvikakyaevakhkeqnndsqlkikeldhniskhkreaedgaakvskmlkdydwinaerhlfgqpns 903
Cdd:COG1196 --------------------------------------------------------------------------------
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 904 aydfktnnpkeagqRLQKLQEMKEKLGrNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIA 983
Cdd:COG1196 768 --------------ELERLEREIEALG-PVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLET 832
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 984 WQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLD-GLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYIL 1062
Cdd:COG1196 833 FDAVNENFQELFPRLFGGGEAELLLTDPDDPLEtGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVL 912
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*
gi 1034663584 1063 DEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1107
Cdd:COG1196 913 DEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAADRLY 957
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1024-1118 |
1.39e-63 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 216.40 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1024 LGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNA 1103
Cdd:cd03273 156 MGGVWKESLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNA 235
|
90
....*....|....*
gi 1034663584 1104 NVLFKTKFVDGVSTV 1118
Cdd:cd03273 236 NVLFRTRFVDGTSTV 250
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-122 |
3.91e-61 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 209.46 E-value: 3.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1 MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLS------------------------- 55
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNLStvrasnlqdliykrgqagitkasvt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 56 -------------------------QVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPE 110
Cdd:cd03273 81 ivfdnsdksqspigfenypeitvtrQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNMGGVW 160
|
170
....*....|..
gi 1034663584 111 ILSMIEEAAGTR 122
Cdd:cd03273 161 KESLTELSGGQR 172
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
472-589 |
2.15e-33 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 125.04 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 472 VKGLVASLISVKDtSATTALELVAGERLYNVVVDTEVTGKKLLERGELKR--RYTIIPLNKISARCIAPETLRvAQNLVG 549
Cdd:smart00968 3 VLGRVADLISVDP-KYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRlgRATFLPLDKIKPRSPAGSKLR-EALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034663584 550 PDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKV 589
Cdd:smart00968 81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1035-1117 |
4.46e-31 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 120.49 E-value: 4.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1035 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTKFVD 1113
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 1034663584 1114 GVST 1117
Cdd:cd03239 175 GVST 178
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1031-1107 |
1.62e-23 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 99.46 E-value: 1.62e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 1031 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLF 1107
Cdd:cd03278 110 RLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
472-590 |
3.95e-23 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 95.41 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 472 VKGLVASLISVKDTsATTALELVAGERLYNVVVDTEVTGKKLLErgELKR----RYTIIPLNKISARCIAPETLRVAqnl 547
Cdd:pfam06470 4 VLGRLADLIEVDEG-YEKAVEAALGGRLQAVVVDDEDDAKRAIE--FLKKnklgRATFLPLDRLKPRPRRPGADLKG--- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1034663584 548 vgpdNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVA 590
Cdd:pfam06470 78 ----GAGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-107 |
4.23e-21 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 92.53 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVViGGRNKYLINgvNANNTRVQDLFC 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIP-FPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLR-GEKMSDVIF--AGSETRKPANFA 76
|
90 100
....*....|....*....|....*...
gi 1034663584 83 SVGL---NVNNPHFLIMQGRITKVLNMK 107
Cdd:cd03278 77 EVTLtfdNSDGRYSIISQGDVSEIIEAP 104
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-104 |
4.24e-21 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 91.99 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 3 IKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGISNLSQvvigGRNKYLINGVNANNTRVQDlfC 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNS-FNAIVGPNGSGKSNIVDAICFVLGGKAAKL----RRGSLLFLAGGGVKAGINS--A 73
|
90 100
....*....|....*....|..
gi 1034663584 83 SVGLNVNNPHFLIMQGRITKVL 104
Cdd:cd03239 74 SVEITFDKSYFLVLQGKVEQIL 95
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1032-1117 |
5.69e-19 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 85.10 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1032 LTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNANVLFKTK 1110
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLIHIK 154
|
....*...
gi 1034663584 1111 FV-DGVST 1117
Cdd:cd03227 155 KViTGVYK 162
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-114 |
1.56e-18 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 86.16 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 3 IKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLL--------------------GISNLSQVV---- 58
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLsdeythlreeqrqallhegsGPSVMSAYVeiif 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663584 59 --------IGG------------RNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSM 114
Cdd:cd03272 81 dnsdnrfpIDKeevrlrrtiglkKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQQEM 156
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1031-1118 |
4.03e-18 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 85.00 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1031 NLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTK 1110
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
....*...
gi 1034663584 1111 FVDGVSTV 1118
Cdd:cd03272 235 FRNKVSTI 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
115-911 |
1.51e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.58 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 115 IEEAagTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEhlsrlyiayqfllaed 194
Cdd:PTZ00121 1214 AEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---------------- 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 195 tKVRSAEELKEMQDKviKLQEELSENDKKIKAlnheiEELEKRKDKEtggilRSLEDALAEAQRVNTKSQSAfdlKKKnl 274
Cdd:PTZ00121 1276 -EARKADELKKAEEK--KKADEAKKAEEKKKA-----DEAKKKAEEA-----KKADEAKKKAEEAKKKADAA---KKK-- 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 275 aCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHAlQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmma 354
Cdd:PTZ00121 1338 -AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-------- 1407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 355 ckNDISKAQTEAKQAQmklkhaqqELKNKQAEVKKMDSGYRKDQE---ALEAVKRLKEKLEAEMKKLNYEENKEESLLEK 431
Cdd:PTZ00121 1408 --DELKKAAAAKKKAD--------EAKKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 432 RRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKnwnrncvkglvaslisvkdtsattALELVAGErlynvvvdtEVTGK 511
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK------------------------ADEAKKAE---------EAKKA 1524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 512 KLLERGELKRRytiiplnkisarciaPETLRVAQNLVGPDNVHVAlslveykPELQKAMEfvfgttfvCDNMDNAKKVAF 591
Cdd:PTZ00121 1525 DEAKKAEEAKK---------------ADEAKKAEEKKKADELKKA-------EELKKAEE--------KKKAEEAKKAEE 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 592 DKRIMTRTVTLGGDV----FDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQ 667
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 668 QWEMKTEEADLLQTKLQQSSyhKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAE----AERERELK- 742
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKa 1732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 743 -DAQKKLDCAKTKADASSKKMKEK----------QQEVEAITLELEELKREHTSYK--QQLEAVNEAIKSYESQIEVMAA 809
Cdd:PTZ00121 1733 eEAKKEAEEDKKKAEEAKKDEEEKkkiahlkkeeEKKAEEIRKEKEAVIEEELDEEdeKRRMEVDKKIKDIFDNFANIIE 1812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 810 EVAKNKESVNKAQE-EVTKQKEVITAQDTVIKaKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV--SKMLK 886
Cdd:PTZ00121 1813 GGKEGNLVINDSKEmEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIeeADEIE 1891
|
810 820
....*....|....*....|....*
gi 1034663584 887 DYDWINAERHLfgqPNSAYDFKTNN 911
Cdd:PTZ00121 1892 KIDKDDIEREI---PNNNMAGKNND 1913
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1035-1106 |
2.97e-16 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 79.54 E-value: 2.97e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 1035 LSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFT-HSQFIVVSLKEGMFNNANVL 1106
Cdd:cd03275 156 LSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGpNFQFIVISLKEEFFSKADAL 228
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-153 |
1.02e-15 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 76.97 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 2 HIKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGisnlSQVVIGGRNKYLINGVNANNTRVqdlf 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALY----GKARSRSKLRSDLINVGSEEASV---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663584 82 cSVGLNVNNPHFLI--MQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTI--LEEEI 153
Cdd:COG0419 72 -ELEFEHGGKRYRIerRQGEFAEFLEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAELqkLKQEI 146
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1028-1106 |
2.45e-15 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 76.18 E-value: 2.45e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663584 1028 WKeNLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVL 1106
Cdd:cd03274 122 WK-NISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRL 199
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-106 |
1.76e-13 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 70.79 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 3 IKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGI-------SNLSQVVIGGRNKYLIN----GVN 71
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFraskmrqKKLSDLIHNSAGHPNLDscsvEVH 82
|
90 100 110
....*....|....*....|....*....|....*
gi 1034663584 72 ANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNM 106
Cdd:cd03274 83 FQEIIDKPLLKSKGIDLDHNRFLILQGEVEQIAQM 117
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
148-897 |
3.97e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.71 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 148 ILEE-EITPTIQKLKEERSSYLEYQKVM----REIEHLSRLYIAYQFLLAEDTKVRSAEELKEM------QDKVIKLQEE 216
Cdd:COG4913 217 MLEEpDTFEAADALVEHFDDLERAHEALedarEQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfaQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 217 LSENDKKIKALNHEIEELEKRKDkETGGILRSLEDALAEA--QRVNtksqsafDLKKknlaceESKRKEleknmvedsKT 294
Cdd:COG4913 297 LEELRAELARLEAELERLEARLD-ALREELDELEAQIRGNggDRLE-------QLER------EIERLE---------RE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 295 LAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagqmmackndiskAQTEAKQAQMKLK 374
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---------------ALAEAEAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 375 HAQQELKNKQAEVKKMDSGYRKDQEALeavkrlkekleaemkklnyeenkeesllekRRQLSRDIGrLKETyeallarfp 454
Cdd:COG4913 419 RELRELEAEIASLERRKSNIPARLLAL------------------------------RDALAEALG-LDEA--------- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 455 NLRFaykdpeknwnrncvkglVASLISVKDTSA--TTALELVAGERLYNVVVDTEVTGK--KLLERGELKRRytiIPLNK 530
Cdd:COG4913 459 ELPF-----------------VGELIEVRPEEErwRGAIERVLGGFALTLLVPPEHYAAalRWVNRLHLRGR---LVYER 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 531 ISARCIAPETLRVAQN-LVGpdnvhvalsLVEYKP-ELQKAMEFVFGTTFV---CDNMDNAKKVafdkrimTRTVTLGGD 605
Cdd:COG4913 519 VRTGLPDPERPRLDPDsLAG---------KLDFKPhPFRAWLEAELGRRFDyvcVDSPEELRRH-------PRAITRAGQ 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 606 VFDPHGTLSGGARSQAAS-----------ILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEmktE 674
Cdd:COG4913 583 VKGNGTRHEKDDRRRIRSryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW---D 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 675 EADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERelkdAQKKLDCAKTK 754
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ----AEEELDELQDR 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 755 ADASSKKmkekqqEVEAITLELEELKREHtsykQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ-KEVIT 833
Cdd:COG4913 736 LEAAEDL------ARLELRALLEERFAAA----LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETA 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 834 AQDTVIKA--KYAEV---------AKHKEQ-----NNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWiNAERHL 897
Cdd:COG4913 806 DLDADLESlpEYLALldrleedglPEYEERfkellNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPF-GPGRYL 884
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
996-1094 |
9.48e-12 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 64.19 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 996 STLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKEN---LTELSGGQRSLVALSLILsmlLFKPaPIYILDEVDAALDLS 1072
Cdd:cd00267 39 STLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRigyVPQLSGGQRQRVALARAL---LLNP-DLLLLDEPTSGLDPA 114
|
90 100
....*....|....*....|...
gi 1034663584 1073 HTQNIGQMLRTHF-THSQFIVVS 1094
Cdd:cd00267 115 SRERLLELLRELAeEGRTVIIVT 137
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-50 |
2.82e-11 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 63.15 E-value: 2.82e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034663584 5 SIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLG 50
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALG 46
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-109 |
6.65e-11 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 63.75 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 3 IKSIILEGFKSYAQRTEVNGFDPlFNAITGLNGSGKSNILDSICFLLGI--SNL-------------------------- 54
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDR-FTCIIGPNGSGKSNLMDAISFVLGEksSHLrsknlkdliyrarvgkpdsnsayvta 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 55 ------------SQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPP 109
Cdd:cd03275 80 vyedddgeektfRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPP 146
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
618-862 |
8.71e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 618 RSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDA 697
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL-----EERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 698 LKKTIEESEETLKNTKEIQRKAEE---------KYEVLENKMKNAEAERERELKDAQKKLdcaktkadassKKMKEKQQE 768
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEyiklsefyeEYLDELREIEKRLSRLEEEINGIEERI-----------KELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 769 VEAITLELEELKREHTSYKQQLEAVNEAiKSYESQIEVMAAEVA-KNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVA 847
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250
....*....|....*
gi 1034663584 848 KHKEQNNDSQLKIKE 862
Cdd:PRK03918 419 KEIKELKKAIEELKK 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
207-459 |
8.96e-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: 65.17 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 207 QDKVIKLQEELSENDKKIKALNHEIEELEKRKdKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLAceeskrkELEK 286
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-KALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 287 NMVEDSKTLAAKEKEVKKItdgLHALQEASNKDAEALaaaqqhfnavsagLSSNEDGAEATLAGQMMACKNDISKAQTEA 366
Cdd:COG4942 91 EIAELRAELEAQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 367 -KQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEM-KKLNYEENKEESLLEKRRQLSRDIGRLKE 444
Cdd:COG4942 155 lRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|....*
gi 1034663584 445 TYEALLARFPNLRFA 459
Cdd:COG4942 235 EAAAAAERTPAAGFA 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-887 |
1.79e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 192 AEDtkVRSAEELKEMQDkVIKLQEELSENDKKIKALNHEIEELEKRKdketggILRSLEDAL-AEAQRVNTKSQSAFDLK 270
Cdd:PTZ00121 1124 AED--ARKAEEARKAED-ARKAEEARKAEDAKRVEIARKAEDARKAE------EARKAEDAKkAEAARKAEEVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 271 KknlaCEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAvsaGLSSNEDGAEATLAG 350
Cdd:PTZ00121 1195 K----AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE---EIRKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 351 QMMACKNDISKAQTEAKQAQMKLKHAQ----------QELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLE-------A 413
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEakkaeekkkaDEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeakkaaeA 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 414 EMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKnwnrncvkglvaslisvKDTSATTALEL 493
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK-----------------AEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 494 VAGERLYNVVVDTEVTGKKLLERGELKRRytiiplnkisarciAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAmefv 573
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAEEKKKADEAKKK--------------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---- 1472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 574 fgttfvcdnmDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELA 653
Cdd:PTZ00121 1473 ----------DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 654 GLKNTAEKYR---QLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIqrKAEEKYEVLENKM 730
Cdd:PTZ00121 1543 EEKKKADELKkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKAEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 731 KNAEAERERELKdaqKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMA-- 808
Cdd:PTZ00121 1621 KAEELKKAEEEK---KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKke 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 809 AEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNND--SQLKIKELDHNISKHKREAEDGAAKVSKMLK 886
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
.
gi 1034663584 887 D 887
Cdd:PTZ00121 1778 E 1778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
617-980 |
2.22e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 617 ARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKtEEADLLQTKLQQssyhkqQEELD 696
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK-KKADEAKKKAEE------KKKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 697 ALKKTIEESeetlKNTKEIQRKAEEKYEVLENKMKnaeAERERELKDAQKKLDCAKtKADASSKKMKEKQQEVEAITLEL 776
Cdd:PTZ00121 1435 EAKKKAEEA----KKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAA 1506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 777 EELKREHTSYKQQLEAVNEAIKSYEsqiEVMAAEVAKNKESVNKAqEEVTKQKEVITAQDTvikaKYAEVAKHKEQNNDS 856
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAE---EAKKADEAKKAEEKKKA-DELKKAEELKKAEEK----KKAEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 857 QLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHlfgqpnsayDFKTNNPKEAGQRLQKLQEMKEKLGRNVNmR 936
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---------KIKAEELKKAEEEKKKVEQLKKKEAEEKK-K 1648
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034663584 937 AMNVLTEAEERYNDLMKKKRIVENDKSKI--LTTIEDLDQKKNQAL 980
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEAL 1694
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
618-975 |
1.52e-09 |
|
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: 62.15 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 618 RSQAASILTKFQELKDvqdELRIKENELRALEEELAGLKNTAEKYRQ----LKQQWEMKTEEADLLQTklqqssyhkqqe 693
Cdd:pfam10174 281 KSHSKFMKNKIDQLKQ---ELSKKESELLALQTKLETLTNQNSDCKQhievLKESLTAKEQRAAILQT------------ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 694 ELDALKKTIEESEETL-KNTKEIQRKAEE--------------------KYEVLENKMKN-AEAERERE-----LKDAQK 746
Cdd:pfam10174 346 EVDALRLRLEEKESFLnKKTKQLQDLTEEkstlageirdlkdmldvkerKINVLQKKIENlQEQLRDKDkqlagLKERVK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 747 KLDCAKTKADASSKKMKEKQQEVEAITLEL-EELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEV 825
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 826 TKQKEVITAQDTVIKAKYAEVAKHKEQ--------------------NNDSQLKIKELDHNISKHKREAEDGAAKVSKML 885
Cdd:pfam10174 506 SSLASSGLKKDSKLKSLEIAVEQKKEEcsklenqlkkahnaeeavrtNPEINDRIRLLEQEVARYKEESGKAQAEVERLL 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 886 ------------KDYDWINAE----RHLFGQPNSAYDFKTNNPKEagqRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYN 949
Cdd:pfam10174 586 gilrevenekndKDKKIAELEsltlRQMKEQNKKVANIKHGQQEM---KKKGAQLLEEARRREDNLADNSQQLQLEELMG 662
|
410 420
....*....|....*....|....*.
gi 1034663584 950 DLMKKKRIVENDKSKILTTIEDLDQK 975
Cdd:pfam10174 663 ALEKTRQELDATKARLSSTQQSLAEK 688
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
198-863 |
1.73e-09 |
|
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: 62.44 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 198 RSAEELK-EMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGgILRSLEDALAEAQRVNTKSQSAFD----LKKK 272
Cdd:pfam15921 138 QSQEDLRnQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEG-VLQEIRSILVDFEEASGKKIYEHDsmstMHFR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 273 NLACEESK-RKELEKNmvedsktLAAKEKEVKKITDGLHALQEASNKDAEALAaaQQHFNAVSAGLSSNEDgaeatlagQ 351
Cdd:pfam15921 217 SLGSAISKiLRELDTE-------ISYLKGRIFPVEDQLEALKSESQNKIELLL--QQHQDRIEQLISEHEV--------E 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 352 MMACKNDISKAQTEAKQAQMKLKHAQQELKNKQA----EVKKMDSGYRKDQEALEAVKRLKE-KLEAEMKKLNYEENKEE 426
Cdd:pfam15921 280 ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEdKIEELEKQLVLANSELT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 427 SLLEKRRQLSRDIGRLKETYEALLA----RFPNLRFAYKDPEKNWNRNC-------------------VKGLVASLISVK 483
Cdd:pfam15921 360 EARTERDQFSQESGNLDDQLQKLLAdlhkREKELSLEKEQNKRLWDRDTgnsitidhlrrelddrnmeVQRLEALLKAMK 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 484 D----------------------TSATTALELVAGERLYNVVvdTEVTGKKL-LERGELKrrytiipLNKISARCIAPET 540
Cdd:pfam15921 440 SecqgqmerqmaaiqgkneslekVSSLTAQLESTKEMLRKVV--EELTAKKMtLESSERT-------VSDLTASLQEKER 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 541 LRVAQNL-VGPDNVHVALSLVEYKpELQKAMEFVFGTTFVCD----NMDNAKKVAfdkRIMTRTVTLGGDVFDPHGTLSG 615
Cdd:pfam15921 511 AIEATNAeITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEalklQMAEKDKVI---EILRQQIENMTQLVGQHGRTAG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 616 GARSQAASI----------LTKFQELKDVQDElRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLL-QTKLQ 684
Cdd:pfam15921 587 AMQVEKAQLekeindrrleLQEFKILKDKKDA-KIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnEVKTS 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 685 QSSYHKQQEELDALKKTI----EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDA---QKKLDCAKTKADA 757
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQKQITAKRGQIDA 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 758 SSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDT 837
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
730 740
....*....|....*....|....*.
gi 1034663584 838 VIKAKYAEVAKHKEQNNdsqLKIKEL 863
Cdd:pfam15921 826 IIQRQEQESVRLKLQHT---LDVKEL 848
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
627-789 |
1.92e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 627 KFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQ-QSSYHKQQEELDALKKTIEES 705
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAlEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 706 EETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTS 785
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
....
gi 1034663584 786 YKQQ 789
Cdd:COG4717 239 AALE 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
110-875 |
8.50e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 110 EILSMIEEAagtRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSY-LEYQKVMREIEHLSRLYIAYQ 188
Cdd:PTZ00121 1095 EAFGKAEEA---KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEARK 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 189 fllAEDTK----------VRSAEELKEMQDKVIKLQEELSENDKKIkalnheiEELEKRKDKETGGILRSLEDALAEAqr 258
Cdd:PTZ00121 1172 ---AEDAKkaeaarkaeeVRKAEELRKAEDARKAEAARKAEEERKA-------EEARKAEDAKKAEAVKKAEEAKKDA-- 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 259 vntksqsafdlkkknlacEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEasnKDAEALAAAQQHFNAVSAGLS 338
Cdd:PTZ00121 1240 ------------------EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA---RKADELKKAEEKKKADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 339 SNEDGAEatlagqmmacknDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKL 418
Cdd:PTZ00121 1299 EEKKKAD------------EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 419 NYEENKEESLLEKRRQLSRDIGRLKETYEAllarfpnLRFAYKDPEKnwnrncvkglvASLISVKDTSATTALELVAGER 498
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEA-------KKKAEEDKKK-----------ADELKKAAAAKKKADEAKKKAE 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 499 LYNVVVDTEVTGKKLLERGELKRRytiiplnkisarciaPETLRVAQNLV-GPDNVHVALSLVEYKPELQKAMEFVFGTT 577
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKK---------------AEEAKKAEEAKkKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 578 FVCDNMDNAKKVAFDKRIMTRTVTlgGDVFDPHGTLSGGARSQAASILTKFQELKDVqDELRiKENELRALEEelaglKN 657
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKADEAKKAEEKKKA-DELK-KAEELKKAEE-----KK 1564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 658 TAEKYRQLKQQWEMKTEEADLLQT--KLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLEnKMKNAEA 735
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEA 1643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 736 ERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAiksyeSQIEVMAAEVAKNK 815
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----EELKKKEAEEKKKA 1718
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 816 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAE 875
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-832 |
2.13e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1 MHIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSI---------CFLLGISNLSQVVIGGRNKYLINGVN 71
Cdd:PRK03918 1 MKIEELKIKNFRSHKS-SVVE-FDDGINLIIGQNGSGKSSILEAIlvglywghgSKPKGLKKDDFTRIGGSGTEIELKFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 72 ANNTRvqdlfCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEE---------AAGTRMYEYKKIaaqktIEKKEAKL 142
Cdd:PRK03918 79 KNGRK-----YRIVRSFNRGESYLKYLDGSEVLEEGDSSVREWVERlipyhvflnAIYIRQGEIDAI-----LESDESRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 143 KEIKTIL--------EEEITPTIQKLKEERSSYLEYQKVMREIEHLSRlyiayqflLAEDTKVRSAEELKEMQDKVIKLQ 214
Cdd:PRK03918 149 KVVRQILglddyenaYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK--------EKEKELEEVLREINEISSELPELR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 215 EEL---SENDKKIKALNHEIEELEKRKDKETGGiLRSLEDALAEAQrvntksqsafdlkkKNLACEESKRKELEKNmVED 291
Cdd:PRK03918 221 EELeklEKEVKELEELKEEIEELEKELESLEGS-KRKLEEKIRELE--------------ERIEELKKEIEELEEK-VKE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 292 SKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDgaeatlagqMMACKNDISKAQTEAKQAQM 371
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE---------KEERLEELKKKLKELEKRLE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 372 KLKHAQQELKNKQAEVKKMDsGYRKDQEALEAVKRLKEKLEAEMKKLNYEEnKEESLLEKRRQLSRDIGRLKETYEALla 451
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEIEE-EISKITARIGELKKEIKELKKAIEEL-- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 452 rfpnlrfaykdpeKNWNRNCvkglvaslisvkdtsattalelvagerlynvvvdtEVTGKKLLE--RGELKRRYTiIPLN 529
Cdd:PRK03918 432 -------------KKAKGKC-----------------------------------PVCGRELTEehRKELLEEYT-AELK 462
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 530 KISA---------RCIAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVfgttfvcdNMDNAKKVAFDKRIMTRtv 600
Cdd:PRK03918 463 RIEKelkeieekeRKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKY--------NLEELEKKAEEYEKLKE-- 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 601 tlggdvfdphgtLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLkntaekyrqLKQQWEMKTEEADLLQ 680
Cdd:PRK03918 533 ------------KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL---------LKELEELGFESVEELE 591
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 681 TKLQQ-SSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKnaeaERERELKDAQKKLDcaktkadass 759
Cdd:PRK03918 592 ERLKElEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKKYS---------- 657
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663584 760 kkmkekQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNK------ESVNKAQEEVTKQKEVI 832
Cdd:PRK03918 658 ------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREkakkelEKLEKALERVEELREKV 730
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-863 |
4.13e-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: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1 MHIKSIILEGFKSYaQRTEVNGFDPL--FNAITGLNGSGKSNILDSICFLL--GISNLSQVVI----------------- 59
Cdd:TIGR00618 1 MKPLRLTLKNFGSY-KGTHTIDFTALgpIFLICGKTGAGKTTLLDAITYALygKLPRRSEVIRslnslyaapseaafael 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 60 -----------------------------------GGRNKYLINGVNANNTRVQDLfcsvgLNVNNPHF----LIMQGRI 100
Cdd:TIGR00618 80 efslgtkiyrvhrtlrctrshrkteqpeqlyleqkKGRGRILAAKKSETEEVIHDL-----LKLDYKTFtrvvLLPQGEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 101 TKVLNMKPPEILSMIEEAAGTRMYE---------YKKIAAQKTIEKKEAKL------------KEIKTILEEEITPTIQK 159
Cdd:TIGR00618 155 AQFLKAKSKEKKELLMNLFPLDQYTqlalmefakKKSLHGKAELLTLRSQLltlctpcmpdtyHERKQVLEKELKHLREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 160 LKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHeIEELEKRKD 239
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ-IEQQAQRIH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 240 KETGGILRSLEDALAEAQRVnTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEvKKITDGLHALQEASNKD 319
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAH-VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 320 AEALAAAQQHFNAVS--AGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKD 397
Cdd:TIGR00618 392 TQKLQSLCKELDILQreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 398 QEALEAVKRLKEKlEAEMKKLnyEENKEESLLEKRRQLSrdiGRLKETYEAllarfpnlrfaykdpeknwnrncvkgLVA 477
Cdd:TIGR00618 472 EQQLQTKEQIHLQ-ETRKKAV--VLARLLELQEEPCPLC---GSCIHPNPA--------------------------RQD 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 478 SLISVKDTSATTALE------LVAGERLYNVVVDTEVTGKKLLERGELKRRYTIIPLNKISA-RCIAPETLRVAQNLvgp 550
Cdd:TIGR00618 520 IDNPGPLTRRMQRGEqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRsKEDIPNLQNITVRL--- 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 551 dnvhvalslveyKPELQKamefvfgttfvcdNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQE 630
Cdd:TIGR00618 597 ------------QDLTEK-------------LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL 651
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 631 LKDVQDE------LRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQ---TKLQQSS--YHKQQEELDALK 699
Cdd:TIGR00618 652 QLTLTQErvrehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLReleTHIEEYDreFNEIENASSSLG 731
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 700 KTIEESEETLKNT-KEIQRKAEEKYEVLENKMKNAEaerERELKDAQKKLDCAKTKADasskkMKEKQQEVEAITLELEE 778
Cdd:TIGR00618 732 SDLAAREDALNQSlKELMHQARTVLKARTEAHFNNN---EEVTAALQTGAELSHLAAE-----IQFFNRLREEDTHLLKT 803
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 779 LKREHTSYkqqleavneaIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQdtviKAKYAEVAKHKEQNNDSQL 858
Cdd:TIGR00618 804 LEAEIGQE----------IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ----LLKYEECSKQLAQLTQEQA 869
|
....*
gi 1034663584 859 KIKEL 863
Cdd:TIGR00618 870 KIIQL 874
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-181 |
4.22e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 55.77 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1 MHIKSIILEGFKSYAQRtEVN-GFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVVIGGRNKYLINGVNANNTRV-- 77
Cdd:COG3950 1 MRIKSLTIENFRGFEDL-EIDfDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKLil 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 78 ----QDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEIlSMIEeaAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILeEEI 153
Cdd:COG3950 80 yygtSRLLLDGPLKKLERLKEEYFSRLDGYDSLLDEDS-NLRE--FLEWLREYLEDLENKLSDELDEKLEAVREAL-NKL 155
|
170 180 190
....*....|....*....|....*....|..
gi 1034663584 154 TPTIQKLKEERSSYLEYQKVMR----EIEHLS 181
Cdd:COG3950 156 LPDFKDIRIDRDPGRLVILDKNgeelPLNQLS 187
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
639-810 |
7.92e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 639 RIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKL----QQSSYHKQQEELDALKKTIEESEETLKNTKE 714
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeelrEELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 715 IQRKAEEKYEVLENKMkNAEAERERELKDAQKKLDCAKTKADASSKK-MKEKQQEVEAITLELEELKREHTSYKQQLEAV 793
Cdd:COG4717 147 RLEELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170
....*....|....*..
gi 1034663584 794 NEAIKSYESQIEVMAAE 810
Cdd:COG4717 226 EEELEQLENELEAAALE 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
694-848 |
7.98e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.55 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 694 ELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSKkmkekQQEVE 770
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNVRN-----NKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034663584 771 AITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAK 848
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
619-1092 |
1.14e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 619 SQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYH---KQQEEL 695
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEelqDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 696 DALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKK---------------------------- 747
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlfl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 748 ----LDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQE 823
Cdd:COG4717 282 vlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 824 EV------TKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHL 897
Cdd:COG4717 362 ELqleeleQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 898 fgqpnsaydfktnnpKEAGQRLQKL-QEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKK 976
Cdd:COG4717 442 ---------------EELEEELEELrEELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 977 NQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEgqtvldGLEFKVALGNTWKENLTELSGGQRSLVALSL---ILSMLL 1053
Cdd:COG4717 507 EEYREERLPPVLERASEYFSRLTDGRYRLIRIDE------DLSLKVDTEDGRTRPVEELSRGTREQLYLALrlaLAELLA 580
|
490 500 510
....*....|....*....|....*....|....*....
gi 1034663584 1054 FKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIV 1092
Cdd:COG4717 581 GEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIY 618
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-449 |
1.85e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1 MHIKSIILEGFKSYAQrTEVnGFDPLFNAITGLNGSGKSNILDSICFLLGIS-----NLSQVVIGGRN------------ 63
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADL-RLEDGVTVIHGVNGSGKSSLLEACFFALYGSkalddTLDDVITIGAEeaeielwfehag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 64 -KYLI------NGVNANN---------------TRVQDLFCSVgLNVNNPHFL----IMQGRITKVLNMKPPEILSMIEE 117
Cdd:PRK02224 79 gEYHIerrvrlSGDRATTakcvletpegtidgaRDVREEVTEL-LRMDAEAFVncayVRQGEVNKLINATPSDRQDMIDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 118 AAGT-RMYEYKKIAA--------------------QKTIEKKEAK------------LKEIKTILE--EEITPTIQKLKE 162
Cdd:PRK02224 158 LLQLgKLEEYRERASdarlgvervlsdqrgsldqlKAQIEEKEEKdlherlngleseLAELDEEIEryEEQREQARETRD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 163 ERSSYLE-YQKVMREIEHLSRLYIAYQFLLAEDTKVRS--AEELKEMQDKVIKLQEELSE-------NDKKIKALNHEIE 232
Cdd:PRK02224 238 EADEVLEeHEERREELETLEAEIEDLRETIAETEREREelAEEVRDLRERLEELEEERDDllaeaglDDADAEAVEARRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 233 ELEKRKDketgGILRSLEDALAEAQRVNTKSQS----AFDLKKKNLACEEsKRKELEKNMVEDSKTLAAKEKEVKKITDG 308
Cdd:PRK02224 318 ELEDRDE----ELRDRLEECRVAAQAHNEEAESlredADDLEERAEELRE-EAAELESELEEAREAVEDRREEIEELEEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 309 LHALQEASNKDAEALAAAQQHfnavSAGLSSNEDGA---EATLAGQMMACKNDISKAqtEAKQAQMKLKHAQQELKnkqa 385
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDF----LEELREERDELrerEAELEATLRTARERVEEA--EALLEAGKCPECGQPVE---- 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 386 evkkmDSGyrkDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLS---RDIGRLKETYEAL 449
Cdd:PRK02224 463 -----GSP---HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDL 521
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-48 |
1.90e-07 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 54.39 E-value: 1.90e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034663584 2 HIKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFL 48
Cdd:COG1195 1 RLKRLSLTNFRNYES-LELE-FSPGINVLVGPNGQGKTNLLEAIYLL 45
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-48 |
2.63e-07 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 54.01 E-value: 2.63e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1034663584 1 MHIKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFL 48
Cdd:PRK00064 1 MYLTRLSLTDFRNYE-ELDLE-LSPGVNVLVGENGQGKTNLLEAIYLL 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
627-976 |
2.73e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 627 KFQELKDVQDELRIKENELRALEEelagLKNTAEKYRQlKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESE 706
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADE----AKKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 707 ETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADA-SSKKMKEKQQEVEAITLE---------- 775
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEekkkadelkk 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 776 ------------LEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNK----ESVNKAQEEVTKQKEVITAQDTVI 839
Cdd:PTZ00121 1554 aeelkkaeekkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKAEELKKAEEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 840 KAKYAEVAKHKEQNNDSQLKIKELDHNISKH--KREAEDGAAKVSKMLKDYDwinAERHlfgqpnsaydfKTNNPKEAGQ 917
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKAEE---DEKK-----------AAEALKKEAE 1699
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663584 918 RLQKLQEMKEKLGRNVNmRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKK 976
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
614-981 |
2.95e-07 |
|
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: 55.12 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 614 SGGARSQAASILTkfqELKDVQDELRIKEN----ELRALEEELAGLKNtaeKYRQLKQQWEMKTEE---------ADLLQ 680
Cdd:pfam15921 287 ASSARSQANSIQS---QLEIIQEQARNQNSmymrQLSDLESTVSQLRS---ELREAKRMYEDKIEElekqlvlanSELTE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 681 TKLQQSSYHKQQEELD-ALKKTIEESEetlKNTKEIQRKAEEKYEVLENKMKNAeaererelkdaqkkldcakTKADASS 759
Cdd:pfam15921 361 ARTERDQFSQESGNLDdQLQKLLADLH---KREKELSLEKEQNKRLWDRDTGNS-------------------ITIDHLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 760 KKMKEKQQEVEAITLELEELKRE-HTSYKQQLEAVNEAIKSYEsQIEVMAAEVAKNKESVNKAQEEVTKQKEVITA---- 834
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESsert 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 835 ----------QDTVIKAKYAEVAKHKEQNNdsqLKIKELDH--NISKHKR--EAEDGAAKVSKMLKD------YDWINAE 894
Cdd:pfam15921 498 vsdltaslqeKERAIEATNAEITKLRSRVD---LKLQELQHlkNEGDHLRnvQTECEALKLQMAEKDkvieilRQQIENM 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 895 RHLFGQPNSAYDF----KTNNPKEAGQRLQKLQEMK-EKLGRNVNMRamnvltEAEERYNDLMKKKRIVENDKSKILTTI 969
Cdd:pfam15921 575 TQLVGQHGRTAGAmqveKAQLEKEINDRRLELQEFKiLKDKKDAKIR------ELEARVSDLELEKVKLVNAGSERLRAV 648
|
410
....*....|..
gi 1034663584 970 EDLDQKKNQALN 981
Cdd:pfam15921 649 KDIKQERDQLLN 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
631-876 |
3.23e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 631 LKDVQDELRIKENELR-ALEEE---LAGLKNTAEKYR----QLKQQWEMKTEEADLLQTKLQ--QSSYHKQQEELDALKK 700
Cdd:PRK02224 312 VEARREELEDRDEELRdRLEECrvaAQAHNEEAESLRedadDLEERAEELREEAAELESELEeaREAVEDRREEIEELEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 701 TIEESEETLKNTKEIQRKAEEKYEVLE---NKMKNAEAERERELKDAQKKLDCAKTKADASskKMKEKQQEVEaitlele 777
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELReerDELREREAELEATLRTARERVEEAEALLEAG--KCPECGQPVE------- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 778 elKREHTsykqqleavnEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTV----IKAKYAE--VAKHKE 851
Cdd:PRK02224 463 --GSPHV----------ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIerleERREDLEelIAERRE 530
|
250 260
....*....|....*....|....*
gi 1034663584 852 QNNDSQLKIKELDHNISKHKREAED 876
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEE 555
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
936-1094 |
3.40e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 53.08 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 936 RAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKdfgsIFSTLLPGANAMLAPPEGQTVL 1015
Cdd:COG3950 97 RLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVRE----ALNKLLPDFKDIRIDRDPGRLV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1016 ----DGLEFkvalgntwkeNLTELSGGQRSLVAL--SLILSMLLFKPAP--------IYILDEVDAALDLSHTQNIGQML 1081
Cdd:COG3950 173 ildkNGEEL----------PLNQLSDGERSLLALvgDLARRLAELNPALenplegegIVLIDEIDLHLHPKWQRRILPDL 242
|
170
....*....|...
gi 1034663584 1082 RTHFTHSQFIVVS 1094
Cdd:COG3950 243 RKIFPNIQFIVTT 255
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
628-979 |
3.44e-07 |
|
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: 54.31 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 628 FQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEmkteeadllqtklqqsSYHKQQEELDALKKTIEESEE 707
Cdd:pfam05622 96 VLELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVE----------------TYKKKLEDLGDLRRQVKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 708 tlKNTKEIQRKAEekyevLENKMKNAEAER------ERELKDAQKKLDCAKTKADA---SSKKMKEK----QQEVEAITL 774
Cdd:pfam05622 160 --RNAEYMQRTLQ-----LEEELKKANALRgqletyKRQVQELHGKLSEESKKADKlefEYKKLEEKlealQKEKERLII 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 775 E-------LEELKREHTSYKQQLEAVNEAIKSYESqIEVMAAEV--AKNKESVNKAQEEvtkQKEVITAQDTVIKAKYAE 845
Cdd:pfam05622 233 ErdtlretNEELRCAQLQQAELSQADALLSPSSDP-GDNLAAEImpAEIREKLIRLQHE---NKMLRLGQEGSYRERLTE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 846 VAKH-----------KEQNNDSQLKIKELDHNISKHKRE-------AEDGAAKVSKMLKDYDWINaERHLFGQPNSAYdF 907
Cdd:pfam05622 309 LQQLledanrrknelETQNRLANQRILELQQQVEELQKAlqeqgskAEDSSLLKQKLEEHLEKLH-EAQSELQKKKEQ-I 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 908 KTNNPKEAGQRLQKLQEMKEKL-GRNVNMRAMnvlteaEERYndlmkkKRIVENDKSKILTtiedLDQKKNQA 979
Cdd:pfam05622 387 EELEPKQDSNLAQKIDELQEALrKKDEDMKAM------EERY------KKYVEKAKSVIKT----LDPKQNPA 443
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
630-847 |
3.68e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 630 ELKDVQDELRIKENELRALEEELAGLKNTAEkyrQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETL 709
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 710 KNTKEIQRKAEEKYEVLE------------------NKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 771
Cdd:COG3883 89 GERARALYRSGGSVSYLDvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663584 772 ITLELEELKREHTSYKQQLEAvneAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVA 847
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-57 |
3.75e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 53.47 E-value: 3.75e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 1 MHIKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQV 57
Cdd:COG3593 1 MKLEKIKIKNFRSI-KDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKF 55
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
625-894 |
4.60e-07 |
|
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: 54.26 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 625 LTKFQELKDVQDELRIKENELRALEEELAGLKNtaeKYRQLKQQWEMKTEEADLLQTKLQ--QSSYHKQQEELDALKKTI 702
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLES---QINDLESKIQNQEKLNQQKDEQIKklQQEKELLEKEIERLKETI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 703 EESEETLKNTKEIQRKAEEKYEVLENKMKnaeaERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKRE 782
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRE----SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 783 HTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ--KEVITAQDTVIKAKYAEVAKHKEQNNDSQLKI 860
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
250 260 270
....*....|....*....|....*....|....
gi 1034663584 861 KELDHNISKHKREAEDGAAKVSKMLKDYDWINAE 894
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
617-842 |
6.63e-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: 53.69 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 617 ARSQAASILTKFQE-LKDVQDELRIKENELRALEEELAGLKNTAekyrqlKQQWEMKTEEADLLQTKLQQ------SSYH 689
Cdd:pfam12128 270 DETLIASRQEERQEtSAELNQLLRTLDDQWKEKRDELNGELSAA------DAAVAKDRSELEALEDQHGAfldadiETAA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 690 KQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKnaeAERERELKDAQKKLDcaktkadaSSKKMKEKQQEV 769
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK---EQNNRDIAGIKDKLA--------KIREARDRQLAV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 770 EAITLE-LEELKREHtsYKQQLEAVNEAIKSYESQIE--------VMAAE-----VAKNKESVNKAQEEVTK-QKEVITA 834
Cdd:pfam12128 413 AEDDLQaLESELREQ--LEAGKLEFNEEEYRLKSRLGelklrlnqATATPelllqLENFDERIERAREEQEAaNAEVERL 490
|
....*...
gi 1034663584 835 QDTVIKAK 842
Cdd:pfam12128 491 QSELRQAR 498
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
642-820 |
7.31e-07 |
|
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: 53.49 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 642 ENELRALEEELAgLKNTAEKYRQLKQQWEMKTeeadlLQTKLQ--QSSYHKQQEELDALKKTIEESEEtlkNTKEIQRKA 719
Cdd:pfam05667 309 TNEAPAATSSPP-TKVETEEELQQQREEELEE-----LQEQLEdlESSIQELEKEIKKLESSIKQVEE---ELEELKEQN 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 720 EEKYEVLENKMKNAEaererELKDAQKKLDCAKTKADASSKKMKEKQQEVEA----ITLELEELKREHTSYKQQLEAVNE 795
Cdd:pfam05667 380 EELEKQYKVKKKTLD-----LLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNKEDESQRKLE 454
|
170 180
....*....|....*....|....*
gi 1034663584 796 AIKSYESQIEVMAAEvAKNKESVNK 820
Cdd:pfam05667 455 EIKELREKIKEVAEE-AKQKEELYK 478
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
659-855 |
9.00e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 659 AEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKnTKEIQRKAEEKYEVLENKMKNAEAERE 738
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLA-AQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 739 RELKDAQKKLDCAKTKADASSKKMKE---KQQEVEAITLELEELKREHTSYKQQlEAVNEAIKSYESQIEVMAAEVAKNK 815
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAAeakKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAEAEAKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034663584 816 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNND 855
Cdd:PRK09510 219 AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-49 |
9.66e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.68 E-value: 9.66e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034663584 3 IKSIILEGFKSYAQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLL 49
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIE-FFSPLTLIVGQNGAGKTTIIEALKYAL 46
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-112 |
9.82e-07 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 51.06 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 3 IKSIILEGFKSYAQrTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG--ISNLsqvvigGRNK----YLINGVNANNTR 76
Cdd:cd03277 3 IVRIKLENFVTYDE-TEFR-PGPSLNMIIGPNGSGKSSIVCAICLGLGgkPKLL------GRAKkvgeFVKRGCDEGTIE 74
|
90 100 110
....*....|....*....|....*....|....*...
gi 1034663584 77 VQdLFCSVG-LNVNNP-HFLiMQGRITKVLNMKPPEIL 112
Cdd:cd03277 75 IE-LYGNPGnIQVDNLcQFL-PQDRVGEFAKLSPIELL 110
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-48 |
1.02e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 52.24 E-value: 1.02e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034663584 3 IKSIILEGFKSYaQRTEVNgFDPLfNAITGLNGSGKSNILDSICFL 48
Cdd:COG4637 2 ITRIRIKNFKSL-RDLELP-LGPL-TVLIGANGSGKSNLLDALRFL 44
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
629-771 |
1.16e-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: 51.08 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAGLKntaEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQ----QEELDALKKTIEE 704
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQKEIESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 705 SEETLKNTKEIQRKAEEKYEVLENKMknaeAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 771
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAEL----AELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
613-861 |
1.48e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 613 LSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLkntAEKYRQLKQQWEMKTEEADLLQTKLQQssyhkQQ 692
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL---LKQLAALERRIAALARRIRALEQELAA-----LE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 693 EELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSK---KMKEKQQEV 769
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqaeELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 770 EAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKH 849
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|..
gi 1034663584 850 KEQNNDSQLKIK 861
Cdd:COG4942 243 TPAAGFAALKGK 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
684-882 |
2.31e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 684 QQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSK 760
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIralEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 761 KMKEKQQEVEAITLELEELKREHT-------------------------SYKQQLEAVNEAIKSYESQIEVMAAEVAKNK 815
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 816 ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVS 882
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-884 |
3.05e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 372 KLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLA 451
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 452 RFPNLRFAYKD-PEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVV--------DTEVTGKKLLERGELKRR 522
Cdd:PRK03918 274 EIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEerikeleeKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 523 YTIIP-----LNKISARCIAPETLRVAQNLVGPDNVHVALSLVE-YKPELQKAMEFVFGTTFVCDNMDNAKKVAFD--KR 594
Cdd:PRK03918 354 LEELEerhelYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEkAKEEIEEEISKITARIGELKKEIKELKKAIEelKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 595 IMTRTVTLGGDVFDPH-GTLSGGARSQAASILTKFQELKDVQDELRIKENELRAL---EEELAGLKNTAEKYRQLK---- 666
Cdd:PRK03918 434 AKGKCPVCGRELTEEHrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEeklk 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 667 ----QQWEMKTEEADLLQTKL-----QQSSYHKQQEELDALKKTIEESEETLKNT--------KEIQRKAEEKYEVLENK 729
Cdd:PRK03918 514 kynlEELEKKAEEYEKLKEKLiklkgEIKSLKKELEKLEELKKKLAELEKKLDELeeelaellKELEELGFESVEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 730 MKNAE---------AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTsyKQQLEAVNEAIKSY 800
Cdd:PRK03918 594 LKELEpfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLEL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 801 ESQIEVMAAEVAKNKESVNKAQEEVTKQKEVitaqdtviKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGA-A 879
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEE--------LEEREKAKKELEKLEKALERVEELREKVKKYKALLKERAlS 743
|
....*
gi 1034663584 880 KVSKM 884
Cdd:PRK03918 744 KVGEI 748
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
615-842 |
4.78e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 615 GGARSQAASILTKFQE-LKDVQDELRIKENE-----LRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTklqqsSY 688
Cdd:PRK02224 172 SDARLGVERVLSDQRGsLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLE-----EH 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 689 HKQQEELDALKKTIEESEETLkntkeiqRKAEEKYEVLENKMKNAEAERErELKDAQKKL--DCAKTKADAsskkmkekq 766
Cdd:PRK02224 247 EERREELETLEAEIEDLRETI-------AETEREREELAEEVRDLRERLE-ELEEERDDLlaEAGLDDADA--------- 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 767 qevEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEV-TKQKEVITAQDTVIKAK 842
Cdd:PRK02224 310 ---EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAaELESELEEAREAVEDRR 383
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
624-803 |
7.07e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 624 ILTKFQELKDVQDELRIKENELRALEEELAglkntAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIE 703
Cdd:pfam05262 182 VVEALREDNEKGVNFRRDMTDLKERESQED-----AKRAQQLKEELDKKQIDADKAQQKADFA-----QDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 704 ESEETLKNTKEIQR--KAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKR 781
Cdd:pfam05262 252 QKQQEAKNLPKPADtsSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKRE 331
|
170 180
....*....|....*....|..
gi 1034663584 782 EHTSYKQQLEAVNEAIKSYESQ 803
Cdd:pfam05262 332 PVAEDLQKTKPQVEAQPTSLNE 353
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
620-884 |
7.24e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 620 QAASILTKFQeLKDVQDELRIKENELRaleEELAGLKNtaeKYRQLKQQWEMKTEEADLLQTKLQQssYHKQQEELD-AL 698
Cdd:pfam05557 1 RAELIESKAR-LSQLQNEKKQMELEHK---RARIELEK---KASALKRQLDRESDRNQELQKRIRL--LEKREAEAEeAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 699 KKTIEESEETLKNTKEIQRKAEEKYEVLEnkmknaeaererelkDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEE 778
Cdd:pfam05557 72 REQAELNRLKKKYLEALNKKLNEKESQLA---------------DAREVISCLKNELSELRRQIQRAELELQSTNSELEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 779 LKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVikAKYAEVAKHKEQNNDSQL 858
Cdd:pfam05557 137 LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL--ARIPELEKELERLREHNK 214
|
250 260
....*....|....*....|....*.
gi 1034663584 859 KIKELDHNISKHKREAEDGAAKVSKM 884
Cdd:pfam05557 215 HLNENIENKLLLKEEVEDLKRKLERE 240
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
628-830 |
8.52e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 628 FQELKDVQDELRIKENELRALEEELAGLKNT----AEKYRQLKQQWEMKTEEADLLQTKL-----QQSSYHKQQEELDAL 698
Cdd:COG1340 35 NEELKELAEKRDELNAQVKELREEAQELREKrdelNEKVKELKEERDELNEKLNELREELdelrkELAELNKAGGSIDKL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 699 KKTIEESEETLKN---TKEIQRKAEEKYEVLENKMKNAEAERE--RELKDAQKKLDCAKTKADASSKKMKEKQQEVEAIT 773
Cdd:COG1340 115 RKEIERLEWRQQTevlSPEEEKELVEKIKELEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKELAEEAQELH 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 774 LELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 830
Cdd:COG1340 195 EEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRK 251
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
629-830 |
8.81e-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: 50.34 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWemktEEADLLQTKLQQssyhkqqeELDALKKTI------ 702
Cdd:COG3096 903 DAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADY----LQAKEQQRRLKQ--------QIFALSEVVqrrphf 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 703 --EESEETLKNTKEIQrkaeekyEVLENKMKNAEAERER---ELKDAQKKLDCA-------KTKADASSKKMKEKQQEVE 770
Cdd:COG3096 971 syEDAVGLLGENSDLN-------EKLRARLEQAEEARREareQLRQAQAQYSQYnqvlaslKSSRDAKQQTLQELEQELE 1043
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034663584 771 AITL----ELEELKREHTS-YKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 830
Cdd:COG3096 1044 ELGVqadaEAEERARIRRDeLHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1003-1083 |
1.05e-05 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 47.85 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1003 NAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLR 1082
Cdd:cd03225 103 NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM---DP-DILLLDEPTAGLDPAGRRELLELLK 178
|
.
gi 1034663584 1083 T 1083
Cdd:cd03225 179 K 179
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
372-829 |
1.18e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 372 KLKHAQQELKNKQAEVKKmdsgYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEE------SLLEKRRQLSRDIGRLKET 445
Cdd:COG4717 72 ELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 446 YEALLARFPNLRFaykdpeknwnrncvkgLVASLISVKDTSATTALELVAGERLYNVVVDTEVTgKKLLERGELKRRYTI 525
Cdd:COG4717 148 LEELEERLEELRE----------------LEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 526 IpLNKISARCIAPETLRvaQNLVGPDNVHVALSLVEykpELQKAMEFVFGTTFVCDnmdnakKVAFDKRIMTRTVTLGGD 605
Cdd:COG4717 211 L-EEELEEAQEELEELE--EELEQLENELEAAALEE---RLKEARLLLLIAAALLA------LLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 606 VFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGL--------KNTAEKYRQLKQQWEMKTEEAD 677
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 678 lLQTKLQQSSYHKQQEELdaLKKTIEESEETLK---NTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQK-----KLD 749
Cdd:COG4717 359 -LEEELQLEELEQEIAAL--LAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeleeELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 750 CAKTKADASSKKMKEKQQEVEAITLELEELKREHTsykqqLEAVNEAIKSYESQIEVMAAEVAKNK---ESVNKAQEEVT 826
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWAALKlalELLEEAREEYR 510
|
...
gi 1034663584 827 KQK 829
Cdd:COG4717 511 EER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-457 |
1.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1 MHIKSIILEGFKSYAQRTEVngFDPLFNAITGLNGSGKSNILDSICFLLgisnLSQVVIGGRNKYLINGVNA--NNTRVQ 78
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIE--FSPGLNVIYGPNEAGKSTLLAFIRAML----LERLEKEADELFKPQGRKPelNLKELK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 79 DLfcsvglnvnnphflimQGRItKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTI---------L 149
Cdd:COG4717 75 EL----------------EEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqeleaL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 150 EEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE---DTKVRSAEELKEMQDKVIKLQEELSENDKKIKA 226
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 227 LNHEIEELEKRKDK-ETGGILRSLEDALAEAQRV------------NTKSQSAFDLKKKNLAC-----------EESKRK 282
Cdd:COG4717 218 AQEELEELEEELEQlENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFlvlgllallflLLAREK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 283 ELEKNMVEDSKTLAAKE----KEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEdgAEATLAGQMMACKND 358
Cdd:COG4717 298 ASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE--EELQLEELEQEIAAL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 359 ISKAQTEAKQA-QMKLKHAQ--QELKNKQAEVKKMDSGYRKDQEALEAV---KRLKEKLEAEMKKLNYEENKEESLLEKR 432
Cdd:COG4717 376 LAEAGVEDEEElRAALEQAEeyQELKEELEELEEQLEELLGELEELLEAldeEELEEELEELEEELEELEEELEELREEL 455
|
490 500
....*....|....*....|....*..
gi 1034663584 433 RQLSRDIGRLKE--TYEALLARFPNLR 457
Cdd:COG4717 456 AELEAELEQLEEdgELAELLQELEELK 482
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
629-814 |
1.28e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 49.47 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDEL---RIKENELRALEEELAGLKntaekyRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEeldalKKTIEES 705
Cdd:pfam09726 402 QDIKKLKAELqasRQTEQELRSQISSLTSLE------RSLKSELGQLRQENDLLQTKLHNAVSAKQKD-----KQTVQQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 706 EETLKNTKEiQRKAEEKYEVLENKMKnaeaeRERELKDAQKKLDCAKTKAD-ASSKKMKEKQQEVEAITLEL-----EEL 779
Cdd:pfam09726 471 EKRLKAEQE-ARASAEKQLAEEKKRK-----KEEEATAARAVALAAASRGEcTESLKQRKRELESEIKKLTHdiklkEEQ 544
|
170 180 190
....*....|....*....|....*....|....*
gi 1034663584 780 KREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKN 814
Cdd:pfam09726 545 IRELEIKVQELRKYKESEKDTEVLMSALSAMQDKN 579
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
630-805 |
1.49e-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: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 630 ELKDVQDELRIKENELRALEEELAGLKNTAEKYRQlkqqwEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETL 709
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA-----RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 710 KNTKEiqrkaeekYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREhtsY 786
Cdd:COG1579 86 RNNKE--------YEALQKEIESLKRRIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---L 154
|
170
....*....|....*....
gi 1034663584 787 KQQLEAVNEAIKSYESQIE 805
Cdd:COG1579 155 EAELEELEAEREELAAKIP 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-978 |
1.68e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 685 QSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEaERERELKDAQKKLDcaktkadasskKMKE 764
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN-EISSELPELREELE-----------KLEK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 765 KQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVnkaqEEVTKQKEVitaqdtviKAKYA 844
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV----KELKELKEK--------AEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 845 EVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERhlfgqpnSAYDFKTNNPKEAGQRLQKLQE 924
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-------KELEKRLEELEERHELYEEAKA 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1034663584 925 MKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQ 978
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
125-976 |
1.82e-05 |
|
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: 49.27 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 125 EYKKIAAQKTIEKKEAKLKEIKTILE--EEITPTIQKLKEE----RSSYLEYQKVMREIEH-LSRLYIAYQFLLAEDTKV 197
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKeiEHNLSKIMKLDNEikalKSRKKQMEKDNSELELkMEKVFQGTDEQLNDLYHN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 198 RSAEeLKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALA-EAQRVNTKSQSAFDLKKKNLAC 276
Cdd:TIGR00606 310 HQRT-VREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArDSLIQSLATRLELDGFERGPFS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 277 E--------------ESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNED 342
Cdd:TIGR00606 389 ErqiknfhtlvierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 343 GAEatlagqmmacknDISKAQTEAKQAQMKLKHAQqelKNKQAEVKKMDSGYRKDQEAleAVKRLKEKLEAEMKKLNYEE 422
Cdd:TIGR00606 469 SSD------------RILELDQELRKAERELSKAE---KNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 423 NKEESLL-------EKRRQLSRDIGRLKETYEALLARFPNLR-----FAYKDPEKNWNRNCVKGLVASLISV-------- 482
Cdd:TIGR00606 532 TTRTQMEmltkdkmDKDEQIRKIKSRHSDELTSLLGYFPNKKqledwLHSKSKEINQTRDRLAKLNKELASLeqnknhin 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 483 KDTSATTALELVAGERLYNVV--VDTEVTGKKLLERGElKRRYTIIPLNKISARCIAPETLRVAQNlvgPDNVHVALSLV 560
Cdd:TIGR00606 612 NELESKEEQLSSYEDKLFDVCgsQDEESDLERLKEEIE-KSSKQRAMLAGATAVYSQFITQLTDEN---QSCCPVCQRVF 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 561 EYKPELQKamefvfgttfVCDNMDNAKKVAFDKriMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQdelri 640
Cdd:TIGR00606 688 QTEAELQE----------FISDLQSKLRLAPDK--LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR----- 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 641 keNELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLqqSSYHKQQEELDALKKTIEE------SEETLKNTKE 714
Cdd:TIGR00606 751 --NKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV--TIMERFQMELKDVERKIAQqaaklqGSDLDRTVQQ 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 715 IQRKAEEKYEVLENKMKNAE------AERERELKDAQKKLDCAKTKADASSKKMKEKQQ---EVEAITLELEELKREHTS 785
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIElnrkliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQfeeQLVELSTEVQSLIREIKD 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 786 YKQQLEAVNEAIKSYESQIEVMaaeVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKE-QNNDSQLKIKELD 864
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEEL---ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVN 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 865 HNISKHKREAEDGAAKVSKMLKDYDwINAERHLFGQPNSAYDFKTNnpkeagqrlqKLQEMKEKLGRNVNMRAMNVLTEA 944
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDID-TQKIQERWLQDNLTLRKREN----------ELKEVEEELKQHLKEMGQMQVLQM 1052
|
890 900 910
....*....|....*....|....*....|..
gi 1034663584 945 EERYNDLMKKKRIVENDKSKILTTIEDLDQKK 976
Cdd:TIGR00606 1053 KQEHQKLEENIDLIKRNHVLALGRQKGYEKEI 1084
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
726-889 |
1.98e-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: 47.23 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 726 LENKMKNAEAERE---RELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAV--NEAIKSY 800
Cdd:COG1579 15 LDSELDRLEHRLKelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 801 ESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDsqlKIKELDHNISKHKREAEDGAAK 880
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREELAAK 171
|
170
....*....|
gi 1034663584 881 VSK-MLKDYD 889
Cdd:COG1579 172 IPPeLLALYE 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
692-828 |
2.08e-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: 47.23 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 692 QEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAE-----RERELKDAQKKLDCAKTKADASSKKMKEKQ 766
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEYEALQKEIESLKRRISDLEDEILELM 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034663584 767 QEveaitleLEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ 828
Cdd:COG1579 117 ER-------IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
670-866 |
2.40e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 670 EMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEES-EETLKNTKEIQR-KAEEKYEVLE--NKMKNAE-----AERERE 740
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQApAKLRQAQAELEAlKDDNDEETREtlSTLSLRQlesrlAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 741 LKDAQKKLDCA-------KTKADASSKKMKEKQQEVEAITLELEELKRE---------------------HTSYKQQLEA 792
Cdd:PRK11281 137 LQNAQNDLAEYnsqlvslQTQPERAQAALYANSQRLQQIRNLLKGGKVGgkalrpsqrvllqaeqallnaQNDLQRKSLE 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034663584 793 VNEAIKS-YESQIEVMAAEVAKNKESVNKAQEEVTkQKEVITAQDTVIKAKYAEVAKHKEQNNdsqLKIKELDHN 866
Cdd:PRK11281 217 GNTQLQDlLQKQRDYLTARIQRLEHQLQLLQEAIN-SKRLTLSEKTVQEAQSQDEAARIQANP---LVAQELEIN 287
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1031-1093 |
2.52e-05 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 46.27 E-value: 2.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 1031 NLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1093
Cdd:cd03214 94 PFNELSGGERQRV----LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVV 152
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
97-439 |
2.54e-05 |
|
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: 48.58 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 97 QGRITKVLNMKPPEILSMIEEAAGTRMyEYKKIAAQKTIEKKEAKLKEIKTILE-EEITPTIQKLKEE-RSSYLEYQKVM 174
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTEKASSARS-QANSIQSQLEIIQEQARNQNSMYMRQlSDLESTVSQLRSElREAKRMYEDKI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 175 REIEHlsrlyiayQFLLA--EDTKVRS-----AEELKEMQDKvikLQEELSENDKKIKALNHEIEELEKRKDKETGG--- 244
Cdd:pfam15921 345 EELEK--------QLVLAnsELTEARTerdqfSQESGNLDDQ---LQKLLADLHKREKELSLEKEQNKRLWDRDTGNsit 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 245 ---ILRSLEDALAEAQRVNT-----KSQSAFDLKKKnLACEESKRKELEKnmvedSKTLAAKEKEVKKItdgLHALQEAS 316
Cdd:pfam15921 414 idhLRRELDDRNMEVQRLEAllkamKSECQGQMERQ-MAAIQGKNESLEK-----VSSLTAQLESTKEM---LRKVVEEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 317 NKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMKLKHAQQE---LKNKQAEVKKMDSG 393
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNA--------EITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQ 556
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034663584 394 YRKDQEALEAvkrLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDI 439
Cdd:pfam15921 557 MAEKDKVIEI---LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
582-976 |
2.75e-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: 48.56 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 582 NMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELrikenelraLEEELAGLKNTAEK 661
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL---------LRTEQQRLEKNEDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 662 YRQLKQQWEMKTEEADLLqTKLQQSsyhkQQEELDALKKTIEESEETLKNTKEIQRKAEEkYEVLENKMKNAEAEREREL 741
Cdd:pfam05483 379 LKIITMELQKKSSELEEM-TKFKNN----KEVELEELKKILAEDEKLLDEKKQFEKIAEE-LKGKEQELIFLLQAREKEI 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 742 KDAQKKLDCAKTKADASSKKMKEKQQEVE--------------AITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVM 807
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahcdKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 808 AAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLK----IKELDHNISKHKREAEDGAAKVSK 883
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKkekqMKILENKCNNLKKQIENKNKNIEE 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 884 MLKDYDWINAERHLFGQPNSAYDFKTNNPK-EAGQRLQKLQEMKEKLGRNVNMRAMnvlteAEERYNDLMKKKRIVENDK 962
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIEDKKI-----SEEKLLEEVEKAKAIADEA 687
|
410
....*....|....
gi 1034663584 963 SKILTTIEDLDQKK 976
Cdd:pfam05483 688 VKLQKEIDKRCQHK 701
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
634-842 |
4.15e-05 |
|
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: 47.86 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 634 VQDELRIKENELRALEEELAGLKNTAE----KYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEEldalkktieeseetl 709
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSNTEllndRLRKSTLQVEQLTTELAAERSTSQKSESARQQLE--------------- 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 710 KNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQ 789
Cdd:pfam01576 945 RQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQ 1024
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663584 790 LEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQ---EEVTKQKEVITAQDTVIKAK 842
Cdd:pfam01576 1025 AEKGNSRMKQLKRQLEEAEEEASRANAARRKLQrelDDATESNESMNREVSTLKSK 1080
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
618-832 |
4.23e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 618 RSQAASILTKFQELKDVQDELRIKENELRaleEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEelda 697
Cdd:COG1340 63 REKRDELNEKVKELKEERDELNEKLNELR---EELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEE---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 698 lKKTIEESEEtLKNTKEIQRKAEEKYEVLENKMKNAEAERErELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELE 777
Cdd:COG1340 136 -KELVEKIKE-LEKELEKAKKALEKNEKLKELRAELKELRK-EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 778 ELKREHTSYKQQLEAVNEAIKSYESQI-----EVMAAEVAKNKESVNKAQEEVTKQKEVI 832
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELrelrkELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
618-1118 |
4.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 618 RSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQqwemKTEEADLLQTKLQQSSYHKQQEELDA 697
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLTGLTPEKLEKELEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 698 LKKTIEESEETLKNTKEIQRKAEEKYEVLE---NKMKNAE-------------------AERERELKDAQKKLdcakTKA 755
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKgkcpvcgrelteehrkellEEYTAELKRIEKEL----KEI 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 756 DASSKKMKEKQQEVEAITLELEELKREHTSYKQqLEAVNEAIKSYE-SQIEVMAAEVAKNKESVNKAQ------------ 822
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKgeikslkkelek 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 823 -EEVTKQKEVITAQDTVIKAKYAEVAK-----------------------HKEQNN--DSQLKIKELDHNISKHKREAED 876
Cdd:PRK03918 551 lEELKKKLAELEKKLDELEEELAELLKeleelgfesveeleerlkelepfYNEYLElkDAEKELEREEKELKKLEEELDK 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 877 GAAKVSKMLKDYDWINAERHLFGQPNSAYDF--KTNNPKEAGQRLQKLQEMKEKLGRNVNmRAMNVLTEAEERYNDLMKK 954
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEELEKRRE-EIKKTLEKLKEELEEREKA 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 955 KRIVENDKsKILTTIEDLDQK----KNQALNIAWQKVNKDFGSIFSTLLPGANAmlappegQTVLDGLEFKVALGNTW-- 1028
Cdd:PRK03918 710 KKELEKLE-KALERVEELREKvkkyKALLKERALSKVGEIASEIFEELTEGKYS-------GVRVKAEENKVKLFVVYqg 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1029 -KENLTELSGGQRSLVALS--LILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTH-SQFIVVSLKEGMFNNAN 1104
Cdd:PRK03918 782 kERPLTFLSGGERIALGLAfrLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKiPQVIIVSHDEELKDAAD 861
|
570
....*....|....
gi 1034663584 1105 VLFKTKFVDGVSTV 1118
Cdd:PRK03918 862 YVIRVSLEGGVSKV 875
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
637-876 |
4.28e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 637 ELRIKENELRALEEELAGLKN--TAEKYRQ--LKQQWEMKTEEADLLQTKLQQSSYH--------KQQEELDALKKTIEE 704
Cdd:COG3096 279 ERRELSERALELRRELFGARRqlAEEQYRLveMARELEELSARESDLEQDYQAASDHlnlvqtalRQQEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 705 SEETLKNTKEIQRKAEEKYEVLENKMKNAEAERER---ELKDAQKKLDCAKTKADA---SSKKMKEKQQEVEAITLELEE 778
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSlksQLADYQQALDVQQTRAIQyqqAVQALEKARALCGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 779 LKREHTSYKQQLEAVNEAIKSYESQIEVmaAEVAKNK-----ESVNKAQEEVTKQ------KEVIT---------AQDTV 838
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSV--ADAARRQfekayELVCKIAGEVERSqawqtaRELLRryrsqqalaQRLQQ 516
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034663584 839 IKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAED 876
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE 554
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
629-983 |
4.63e-05 |
|
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: 47.81 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAGlknTAEKYRQLKQQWEMKTEEADLLQTKLQQSS--YHKQQEELDALKKTIEESE 706
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQG---QMERQMAAIQGKNESLEKVSSLTAQLESTKemLRKVVEELTAKKMTLESSE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 707 ETLKntkEIQRKAEEKYEVLEnkMKNAEAERERELKDAQ-KKLDCAKTKADasskKMKEKQQEVEAITLELEELKREHTS 785
Cdd:pfam15921 496 RTVS---DLTASLQEKERAIE--ATNAEITKLRSRVDLKlQELQHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEI 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 786 YKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTvikakyaevakhkeqnndsqlKIKELDH 865
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA---------------------KIRELEA 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 866 NISKHKREAEDGAAKVSKMLKDYDWINAERhlfgqpnsayDFKTNNPKEAGQRLQKLQEMKEKLGRNVNmramNVLTEAE 945
Cdd:pfam15921 626 RVSDLELEKVKLVNAGSERLRAVKDIKQER----------DQLLNEVKTSRNELNSLSEDYEVLKRNFR----NKSEEME 691
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034663584 946 ERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIA 983
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
692-967 |
5.11e-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: 47.66 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 692 QEELDA-LKKTIEESEETLKNTKEIQRKAEEKYEVLENKmKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVE 770
Cdd:TIGR00618 151 QGEFAQfLKAKSKEKKELLMNLFPLDQYTQLALMEFAKK-KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 771 AITLELEELKREHTSYKQQLEAVNEAiksyeSQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTviKAKYAEVAKHK 850
Cdd:TIGR00618 230 HLREALQQTQQSHAYLTQKREAQEEQ-----LKKQQLLKQLRARIEELRAQEAVLEETQERINRARK--AAPLAAHIKAV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 851 EQNNDsqlKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYD-FKTNNPKEAGQRLQKLQEMKEkl 929
Cdd:TIGR00618 303 TQIEQ---QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIhIRDAHEVATSIREISCQQHTL-- 377
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034663584 930 gRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILT 967
Cdd:TIGR00618 378 -TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDT 414
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-216 |
5.48e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 45.18 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 6 IILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLGiSNLSQVVIGGRNKYLINGVNANNTRVQDLFCSVG 85
Cdd:pfam13476 1 LTIENFRSF-RDQTID-FSKGLTLITGPNGSGKTTILDAIKLALY-GKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 86 LNVNNPhflimqgritkvlnmKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERS 165
Cdd:pfam13476 78 FENNDG---------------RYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQERE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034663584 166 SYLEYQKVMREIEHLSRlyiAYQFLLAEDTKVRSAEELKEMQDKVIKLQEE 216
Cdd:pfam13476 143 EEFERKEKKERLEELEK---ALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
131-258 |
5.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 131 AQKTIEKKEAKLKEIKT-----ILEEEITPTIQKLKEERSSYLEYQKVMREIEH--------LSRLYIAYQFLLAEDTKV 197
Cdd:COG3206 187 LRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEArlaalraqLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034663584 198 RSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQR 258
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQA 327
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
627-977 |
5.99e-05 |
|
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: 47.32 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 627 KFQELKDVQDELRIKENELRALEEELAGLKNTAEK--YRQLKQQWEMKTEEADLLQTKLQQS--SYHKQQEELDALKKTI 702
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNnkIISQLNEQISQLKKEL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 703 EESEetlKNTKEIQRKAEEKYEVLEnKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKRE 782
Cdd:TIGR04523 352 TNSE---SENSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 783 HTSYKQQLEAVNEAIKSYES---------------------QIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKA 841
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNqdsvkeliiknldntresletQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 842 KYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNNPKEAGQRLQK 921
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663584 922 LQEMKEKLGRNVNMRamNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKN 977
Cdd:TIGR04523 588 QELIDQKEKEKKDLI--KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
661-895 |
6.05e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 661 KYRQLKQQWEMKTEEADLLQTKLQqsSYHKQQEELDAlkktieeseetlKNTKEIQRKaEEKYEVLENKMKNAEAERErE 740
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIK--TYNKNIEEQRK------------KNGENIARK-QNKYDELVEEAKTIKAEIE-E 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 741 LKDaqKKLDCAKTKADASSKkMKEKQQEVEAITLELEELKREHTSY---------KQQLEAVNEAIKSYESQIevmaAEV 811
Cdd:PHA02562 239 LTD--ELLNLVMDIEDPSAA-LNKLNTAAAKIKSKIEQFQKVIKMYekggvcptcTQQISEGPDRITKIKDKL----KEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 812 AKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWI 891
Cdd:PHA02562 312 QHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
....
gi 1034663584 892 NAER 895
Cdd:PHA02562 392 VKTK 395
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
629-873 |
6.83e-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: 47.02 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDEL----RIKENELRALEEELAGLKNTAEKYrqLKQQWEMKTE--EADLLQTKLQQSS------YHKQQEELD 696
Cdd:pfam05483 432 EELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHY--LKEVEDLKTEleKEKLKNIELTAHCdkllleNKELTQEAS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 697 ALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKM---------KEKQ- 766
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENArsieyevlkKEKQm 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 767 -----------QEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNK----ESVNKAQEEVTKQK-- 829
Cdd:pfam05483 590 kilenkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKqkfeEIIDNYQKEIEDKKis 669
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034663584 830 ------EVITAQDTVIKAkyaeVAKHKEQNNDSQLKIKELDHNISKHKRE 873
Cdd:pfam05483 670 eeklleEVEKAKAIADEA----VKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
213-453 |
6.90e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 213 LQEELSENDKKIKALNHEIEELEKRkdketggiLRSLEDALAEAQRvntksqsafdlkKKNLACEESKRKELEKNMVEDS 292
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE--------LEEAEAALEEFRQ------------KNGLVDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 293 KTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQhfNAVSAGLSSNEDGAEATLAgqmmacknDISKAQTEAKQAQMK 372
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELA--------ELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 373 LKHAQQELKNK-QAEVKKMDSGYRKDQEALEA----VKRLKEKLEAEMKKLNyeenkeeSLLEKRRQLSRDIGRLKETYE 447
Cdd:COG3206 296 LRAQIAALRAQlQQEAQRILASLEAELEALQAreasLQAQLAQLEARLAELP-------ELEAELRRLEREVEVARELYE 368
|
....*.
gi 1034663584 448 ALLARF 453
Cdd:COG3206 369 SLLQRL 374
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
690-791 |
7.67e-05 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 43.33 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 690 KQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEV 769
Cdd:pfam13863 3 EKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEI 82
|
90 100
....*....|....*....|..
gi 1034663584 770 EAITLELEELKREHTSYKQQLE 791
Cdd:pfam13863 83 KKLTAQIEELKSEISKLEEKLE 104
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
648-771 |
8.10e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 648 LEEELAGLkntAEKYRQLKQQW---EMKTEEADLLQTKLQQSsYHKQQEELDALKKTIEES-EETLKNTKEiqRKAEEKY 723
Cdd:PRK00409 518 LNELIASL---EELERELEQKAeeaEALLKEAEKLKEELEEK-KEKLQEEEDKLLEEAEKEaQQAIKEAKK--EADEIIK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034663584 724 EVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEA 771
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
693-897 |
9.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 693 EELDALKKTIEESEETLKNTKEIQRKAEEkyevLENKMKNAEAERErELKDAQKKLDCAKTKADASsKKMKEKQQEVEAI 772
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELE-ELREELEKLEKLLQLLPLY-QELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 773 TLELEELKREHTSYKQQLEavneaiksyesQIEVMAAEVAKNKESVNKAQEEVTKQKEvitaqdtvikakyAEVAKHKEQ 852
Cdd:COG4717 145 PERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLSLATE-------------EELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034663584 853 NNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHL 897
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
629-835 |
1.00e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEElagLKNTAEKYRQLKQQW---------------EMKTEEADLLQTKLQQSSYHKQ-- 691
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQ---EQQQRSQLEQAKEGLsalnrllprlnlladETLADRVEEIREQLDEAEEAKRfv 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 692 --------------------QEELDALKKTIEESEETLKNTKE--------IQRKAEEKY--------------EVLENK 729
Cdd:PRK04863 914 qqhgnalaqlepivsvlqsdPEQFEQLKQDYQQAQQTQRDAKQqafaltevVQRRAHFSYedaaemlaknsdlnEKLRQR 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 730 MKNAEAERER---ELKDAQKKLD-------CAKTKADASSKKMKEKQQEVEAITL----ELEELKREHTS-YKQQLEAVN 794
Cdd:PRK04863 994 LEQAEQERTRareQLRQAQAQLAqynqvlaSLKSSYDAKRQMLQELKQELQDLGVpadsGAEERARARRDeLHARLSANR 1073
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034663584 795 EAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQ 835
Cdd:PRK04863 1074 SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-251 |
1.01e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.84 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 27 FNAITGLNGSGKSNILDSICFLLGISNL---SQVVIGGRNKY--LINGVNANNTRVQDLFCSVGLNVNNPHFLIMqgriT 101
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALvigLTDERSRNGGIggIPSLLNGIDPKEPIEFEISEFLEDGVRYRYG----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 102 KVLNMKPPEILSMIEEAAGTRMYEYKKIAaqKTIEKKEAKLKEIKTILEEEItpTIQKLKEERSSYLEYQKVMREIEHLS 181
Cdd:pfam13304 77 DLEREDVEEKLSSKPTLLEKRLLLREDSE--EREPKFPPEAEELRLGLDVEE--RIELSLSELSDLISGLLLLSIISPLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034663584 182 RLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELS----ENDKKIKALNHEIEELEKRKDKETGGILRSLED 251
Cdd:pfam13304 153 FLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVrglkLADLNLSDLGEGIEKSLLVDDRLRERGLILLEN 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
192-396 |
1.30e-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: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 192 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDkETGGILRSLEDALAE----AQRVNTKSQSAF 267
Cdd:COG4942 46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-ELRAELEAQKEELAEllraLYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 268 DLKKKNLAcEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEAT 347
Cdd:COG4942 125 LLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034663584 348 LAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRK 396
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
619-862 |
1.42e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 619 SQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNT-AEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQ--EEL 695
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDElNAQVKELREEAQELREKRDELNEKVKELKEERDElnEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 696 DALKKTIEESEETLKNTKEIQR---KAEEKYEVLENKMKNA----EAERE--RELKDAQKKLDCAKtKADASSKKMKEKQ 766
Cdd:COG1340 88 NELREELDELRKELAELNKAGGsidKLRKEIERLEWRQQTEvlspEEEKElvEKIKELEKELEKAK-KALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 767 QEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEV 846
Cdd:COG1340 167 AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
|
250
....*....|....*.
gi 1034663584 847 AKHKEQNNDSQLKIKE 862
Cdd:COG1340 247 KKLRKKQRALKREKEK 262
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-55 |
1.53e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 45.42 E-value: 1.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663584 2 HIKSIILEGFKSYAQRTEVN----GFDPL-FNAITGLNGSGKSNILDSICFLLGISNLS 55
Cdd:COG1106 1 MLISFSIENFRSFKDELTLSmvasGLRLLrVNLIYGANASGKSNLLEALYFLRNLVLNS 59
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1012-1093 |
1.77e-04 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 44.02 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1012 QTVLDGLEFKVALGNtwkENLtelSGGQRSLVALSLILsmllFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFI 1091
Cdd:cd03244 123 ESLPGGLDTVVEEGG---ENL---SVGQRQLLCLARAL----LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVL 192
|
..
gi 1034663584 1092 VV 1093
Cdd:cd03244 193 TI 194
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
629-806 |
2.09e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLlQTKLQQ--SSYHKQQEELDALKKTIEESE 706
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAElsARYTPNHPDVIALRAQIAALR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 707 EtlkntkEIQRKAEEKYEVLENKMKNAEAeRERELKDAQKKLDcaktkadASSKKMKEKQQEVEAITLELEELKREHTSY 786
Cdd:COG3206 305 A------QLQQEAQRILASLEAELEALQA-REASLQAQLAQLE-------ARLAELPELEAELRRLEREVEVARELYESL 370
|
170 180
....*....|....*....|
gi 1034663584 787 KQQLEAVNEAIKSYESQIEV 806
Cdd:COG3206 371 LQRLEEARLAEALTVGNVRV 390
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
629-830 |
2.22e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 44.25 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEA-DLLQTKLQQ-SSYHKQQEELDALKKTIEES- 705
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTeERLAEALEKlEEAEKAADESERGRKVLENRa 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 706 ----------EETLKNTKEIQRKAEEKYEVLENKMKNAEAERERelkdaqkkldcAKTKADASSKKMKEKQQEVEAIT-- 773
Cdd:pfam00261 88 lkdeekmeilEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLER-----------AEERAELAESKIVELEEELKVVGnn 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 774 ---LELEELK---REhTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKE 830
Cdd:pfam00261 157 lksLEASEEKaseRE-DKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1031-1070 |
2.75e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 43.94 E-value: 2.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1034663584 1031 NLTELSGGQRSLVALSLILSmllfKPAPIYILDEVDAALD 1070
Cdd:cd03237 112 EVPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLD 147
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1029-1094 |
3.11e-04 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 42.76 E-value: 3.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 1029 KENLteLSGGQRSLVALSLilsMLLfKPAPIYILDEVDAALDlSHTQN-IGQMLRTHFTHSQFIVVS 1094
Cdd:cd03228 93 RENI--LSGGQRQRIAIAR---ALL-RDPPILILDEATSALD-PETEAlILEALRALAKGKTVIVIA 152
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
630-862 |
3.20e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 630 ELKDVQDELRIKENELRALEEELAGLKNTaEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETL 709
Cdd:NF033838 175 ELEIAESDVEVKKAELELVKEEAKEPRDE-EKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 710 KNTKEIQRKAEEKYEVL---------ENKMKNAEA------------ERERELKDAQKKLDCAKTKADASSKKMKEKQQE 768
Cdd:NF033838 254 ATSEQDKPKRRAKRGVLgepatpdkkENDAKSSDSsvgeetlpspslKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 769 VEAITLELEELKREHTSYKQQLEAVNEAIKSyesqievmaaevAKNKESVNKAQEEVTKQKEVITAQDTVI--KAKYAEV 846
Cdd:NF033838 334 NTYKTLELEIAESDVKVKEAELELVKEEAKE------------PRNEEKIKQAKAKVESKKAEATRLEKIKtdRKKAEEE 401
|
250
....*....|....*.
gi 1034663584 847 AKHKEQNNDsqlKIKE 862
Cdd:NF033838 402 AKRKAAEED---KVKE 414
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-457 |
3.36e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 121 TRMYEYKKIAAQKTIEKKEAKLKEI---KTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKv 197
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 198 rsAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK--------RKDKETGGILRSLEDALAE--AQRVNTKSQSAF 267
Cdd:PRK03918 451 --KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeselIKLKELAEQLKELEEKLKKynLEELEKKAEEYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 268 DLKKK---------NLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLS 338
Cdd:PRK03918 529 KLKEKliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 339 SNEDGAEATLAgQMMACKNDISKAQTE------------AKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKR 406
Cdd:PRK03918 609 DAEKELEREEK-ELKKLEEELDKAFEElaetekrleelrKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034663584 407 LKEKLEAEMKKLnyEENKEEslLEKRRQLSRDIGRLKETYEALLARFPNLR 457
Cdd:PRK03918 688 RREEIKKTLEKL--KEELEE--REKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
658-886 |
3.37e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.04 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 658 TAEKYRQLKQQWEMKTEEADLLQTKLQQSSYhkqQEELDALKKTIEESEETLKNTKEIQRKAEEKyevlenKMKNAEAER 737
Cdd:PTZ00108 1100 TKEKVEKLNAELEKKEKELEKLKNTTPKDMW---LEDLDKFEEALEEQEEVEEKEIAKEQRLKSK------TKGKASKLR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 738 ERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEaiksyESQIEVMAAEVAKNKES 817
Cdd:PTZ00108 1171 KPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDD-----EEQKTKPKKSSVKRLKS 1245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 818 VNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHK-REAEDGAAKVSKMLK 886
Cdd:PTZ00108 1246 KKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGsKPSSPTKKKVKKRLE 1315
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
23-70 |
3.71e-04 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 43.73 E-value: 3.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1034663584 23 FDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVVIGGRNKYLINGV 70
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGV 66
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
639-835 |
4.01e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 639 RIKENELRALEEELAGL----KNTAEKYRQLKQQwEMKtEEADLLQTKLQQSsYHKQQEELDALKKTIEESEETLKNTKE 714
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRIleeaKKEAEAIKKEALL-EAK-EEIHKLRNEFEKE-LRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 715 IQRKAEEKyevLENKMKNAEaERERELKDAQKKLDcaktkadassKKMKEKQQEVEAITleleELKREhtsykqqlEAVN 794
Cdd:PRK12704 104 LLEKREEE---LEKKEKELE-QKQQELEKKEEELE----------ELIEEQLQELERIS----GLTAE--------EAKE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034663584 795 EAIKSYESQIEVMAAEVAKNKEsvNKAQEEVTKQKEVITAQ 835
Cdd:PRK12704 158 ILLEKVEEEARHEAAVLIKEIE--EEAKEEADKKAKEILAQ 196
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
94-418 |
4.39e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 94 LIMQGRITKVLNMKPPEILSMIEEAAGT--------RMYEYKKiAAQKTIEKKEAKLKEIKTILEEE---ITPTIQKLKE 162
Cdd:PRK10246 152 LLSQGQFAAFLNAKPKERAELLEELTGTeiygqisaMVFEQHK-SARTELEKLQAQASGVALLTPEQvqsLTASLQVLTD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 163 ERSSYLEYQKVM-REIEHLSRLYIAYQFLLAEDTKVRSA-EELKEMQDKVIKLqeELSENDKKIKALNHEIEELEKRkdk 240
Cdd:PRK10246 231 EEKQLLTAQQQQqQSLNWLTRLDELQQEASRRQQALQQAlAAEEKAQPQLAAL--SLAQPARQLRPHWERIQEQSAA--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 241 etggilrsLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEK------EVKkitdGLHALQE 314
Cdd:PRK10246 306 --------LAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnELA----GWRAQFS 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 315 ASNKDAEALAAAQQHFNAVSAGLS---------SNEDGAEA--------TLAGQMMACKNDISKAQTEAKQAQMKLKHAQ 377
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNalpaitltlTADEVAAAlaqhaeqrPLRQRLVALHGQIVPQQKRLAQLQVAIQNVT 453
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034663584 378 QELKNKQAEVKKMDSGYRKDQEALEAVKRLKEkLEAEMKKL 418
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDL 493
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
627-884 |
4.50e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 627 KFQELKdvQDELRiKENELRALEEELAGLKNTAEKYRQLK---------QQWEMKTE-EADLLQTKLQQSSYHKQQEELD 696
Cdd:pfam17380 292 KFEKME--QERLR-QEKEEKAREVERRRKLEEAEKARQAEmdrqaaiyaEQERMAMErERELERIRQEERKRELERIRQE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 697 ALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLEL 776
Cdd:pfam17380 369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 777 EELKREHTSYKQQLeavnEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTK--QKEVITAQDTVIKAKYAEVAKHKEQnN 854
Cdd:pfam17380 449 ERVRLEEQERQQQV----ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEM-E 523
|
250 260 270
....*....|....*....|....*....|
gi 1034663584 855 DSQLKIKEldhniSKHKREAEDGAAKVSKM 884
Cdd:pfam17380 524 ERQKAIYE-----EERRREAEEERRKQQEM 548
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
151-876 |
4.88e-04 |
|
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: 44.44 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 151 EEITPTIQKLKEERSSYLEyqkVMREIEHLSRLYIAYQFLLAEDTKVRSA------EEL----KEMQDKVIKLQEELSEN 220
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLES---AELRLSHLHFGYKSDETLIASRQEERQEtsaelnQLLrtldDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 221 DKKIKALNHEIEELEKRKdketggilRSLEDALAEaqrvntksQSAFDLKKknlacEESKRKELEkNMVEDSKTLAAKEK 300
Cdd:pfam12128 314 DAAVAKDRSELEALEDQH--------GAFLDADIE--------TAAADQEQ-----LPSWQSELE-NLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 301 EVKKITDGLHALQEASNKDaeALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQEL 380
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 381 KNKQAEV----------KKMDSGYRKDQEALEAVKRLKEKLEAEMKKLN-YEENKEESLLEKRRQLSRDIGRLKETYEAL 449
Cdd:pfam12128 450 KLRLNQAtatpelllqlENFDERIERAREEQEAANAEVERLQSELRQARkRRDQASEALRQASRRLEERQSALDELELQL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 450 LARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGER-LYNVVVD---TEVTGKKLLERgELKRRyti 525
Cdd:pfam12128 530 FPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELnLYGVKLDlkrIDVPEWAASEE-ELRER--- 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 526 iplnkisaRCIAPETLRVAQNLVGPDNVHVALSLVEYKpELQKAMEfvFGTTFVCDNMDNAKKVAFDKRIMTRTVTlggd 605
Cdd:pfam12128 606 --------LDKAEEALQSAREKQAAAEEQLVQANGELE-KASREET--FARTALKNARLDLRRLFDEKQSEKDKKN---- 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 606 vfdphgtlsggaRSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQ---WEMKTEEADLLQTK 682
Cdd:pfam12128 671 ------------KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvveGALDAQLALLKAAI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 683 LQQSSYHKQQeeLDALKKtieeseetlKNTKEIQRKAEEKYEVlenkmknaeAERERELKDAQKKL-DCAKTKADASSKK 761
Cdd:pfam12128 739 AARRSGAKAE--LKALET---------WYKRDLASLGVDPDVI---------AKLKREIRTLERKIeRIAVRRQEVLRYF 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 762 --MKEK-QQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEvmaaevaKNKESVNKAQEEVTkqkEVITAQDTV 838
Cdd:pfam12128 799 dwYQETwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLE-------MERKASEKQQVRLS---ENLRGLRCE 868
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1034663584 839 IKaKYAEVAKHKEqNNDSQLKIKE----LDHNISKHKREAED 876
Cdd:pfam12128 869 MS-KLATLKEDAN-SEQAQGSIGErlaqLEDLKLKRDYLSES 908
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1032-1082 |
4.91e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.08 E-value: 4.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1034663584 1032 LTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1082
Cdd:PRK11231 136 LTDLSGGQRQRA----FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR 182
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1034-1094 |
5.22e-04 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 42.70 E-value: 5.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034663584 1034 ELSGGQRSLVALSLILSMllfKPaPIYILDEVDAALDLSHTQNIGQMLRT-HFTHSQFIVVS 1094
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAM---EP-EVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVT 191
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
735-895 |
5.30e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 735 AERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKN 814
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 815 KESVNKAQ------------EEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVS 882
Cdd:COG3883 99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170
....*....|...
gi 1034663584 883 KMLKDYDWINAER 895
Cdd:COG3883 179 EQEALLAQLSAEE 191
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-342 |
5.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 132 QKTIEKKEAKLKEIKTILEE--EITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAE----DTKVRSAE---- 201
Cdd:COG4913 606 FDNRAKLAALEAELAELEEElaEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaelEAELERLDassd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 202 ELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkdketggilrsLEDALAEAQRVNTKSQSAFDLKKKNLaceeskR 281
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-----------LEQAEEELDELQDRLEAAEDLARLEL------R 748
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663584 282 KELEKnMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNA--------VSAGLSSNED 342
Cdd:COG4913 749 ALLEE-RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadLDADLESLPE 816
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
3-453 |
5.76e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 43.96 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 3 IKSII-LEGFKSYAQRTEVNGFDPLfNAITGLNGSGK---SNILDSICfllgiSNLSQVVIGGRNKYLINGVNANNTR-- 76
Cdd:COG4694 2 ITKIKkLKNVGAFKDFGWLAFFKKL-NLIYGENGSGKstlSRILRSLE-----LGDTSSEVIAEFEIEAGGSAPNPSVrv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 77 -----VQDLFCSVGlnvNNPHFLIMQGRITKVLNmkppEILSMIEEAAGtrmYEYKKIAAQKTIEKKEAKLKEIKTILEE 151
Cdd:COG4694 76 fnrdfVEENLRSGE---EIKGIFTLGEENIELEE----EIEELEKEIED---LKKELDKLEKELKEAKKALEKLLEDLAK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 152 EITPTIQKLKeeRSSYLEYQKvmreiEHLSRLYIAYQFLLAEDTKvRSAEELKEMQDKVIKLQEELSENDKKIKALNHEI 231
Cdd:COG4694 146 SIKDDLKKLF--ASSGRNYRK-----ANLEKKLSALKSSSEDELK-EKLKLLKEEEPEPIAPITPLPDLKALLSEAETLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 232 EELEKRKDKEtggILRSLEDALAEAQRVntksQSAFDLKKKN-----LACE----ESKRKELEKNMVEDSKTLAAK-EKE 301
Cdd:COG4694 218 EKSAVSSAIE---ELAALIQNPGNSDWV----EQGLAYHKEEeddtcPFCQqelaAERIEALEAYFDDEYEKLLAAlKDL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 302 VKKITDGLHALQEASN-----KDAEALAAAQQHFNAVSAGLSSNE--------------DGAEATLAGQMMACKNDISKA 362
Cdd:COG4694 291 LEELESAINALSALLLeilrtLLPSAKEDLKAALEALNALLETLLaaleekianpstsiDLDDQELLDELNDLIAALNAL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 363 QTEAKQAQMKLKHAQQELKNKQAEVKKmdsgyrkdQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSR----- 437
Cdd:COG4694 371 IEEHNAKIANLKAEKEEARKKLEAHEL--------AELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISEleael 442
|
490
....*....|....*..
gi 1034663584 438 -DIGRLKETYEALLARF 453
Cdd:COG4694 443 sSVDEAADEINEELKAL 459
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
629-812 |
6.36e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAGLKNT-AEKYRQLKQQWE---MKTEEADLLQTKLQQSSYHKQQEELDALKKTIEE 704
Cdd:COG3883 51 EEYNELQAELEALQAEIDKLQAEIAEAEAEiEERREELGERARalyRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 705 SEETLKNTKEIQRKAEEKYEVLENKMKNAEAERErELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHT 784
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKA-ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
170 180
....*....|....*....|....*...
gi 1034663584 785 SYKQQLEAVNEAIKSYESQIEVMAAEVA 812
Cdd:COG3883 210 AAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
632-850 |
6.42e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 632 KDVQDELRIKENELRALEEELAGLKNTAEkyRQLKQQWEMKTEEADLLQTKLQQSSYHKQQ-----EELDALKKTIEESE 706
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIE--EQRKKNGENIARKQNKYDELVEEAKTIKAEieeltDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 707 ETLK--NTKEIQRKAE-----------EKYEVLENKMKNAEAERER------ELKDAQKKLDCAKTKADasskKMKEKQQ 767
Cdd:PHA02562 255 AALNklNTAAAKIKSKieqfqkvikmyEKGGVCPTCTQQISEGPDRitkikdKLKELQHSLEKLDTAID----ELEEIMD 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 768 EVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKqkevitaqdtvIKAKYAEVA 847
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK-----------IVKTKSELV 399
|
...
gi 1034663584 848 KHK 850
Cdd:PHA02562 400 KEK 402
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
8-49 |
6.58e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 42.26 E-value: 6.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034663584 8 LEGFKSYAQRTEVN----GFDPLFnAITGLNGSGKSNILDSICFLL 49
Cdd:cd03279 8 LKNFGPFREEQVIDftglDNNGLF-LICGPTGAGKSTILDAITYAL 52
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
591-824 |
6.83e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 591 FDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENeLRALEEELAGLKNTAEKYRQlkqqwe 670
Cdd:cd22656 63 FKDDTYPSIVSLAGDIYNYAQNAGGTIDSYYAEILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQD------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 671 mkteEADLLQTKLQ--QSSYHKQQEELDALKKTI------EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELK 742
Cdd:cd22656 136 ----KAAKVVDKLTdfENQTEKDQTALETLEKALkdlltdEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 743 DAQKKLDcAKTKADASSKKMKEK----QQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEvmAAEVAKNKesV 818
Cdd:cd22656 212 DDEAKLA-AALRLIADLTAADTDldnlLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIP--AAILAKLE--L 286
|
....*.
gi 1034663584 819 NKAQEE 824
Cdd:cd22656 287 EKAIEK 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
130-328 |
6.85e-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: 43.21 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 130 AAQKTIEKKEAKLKEIKtileEEITPTIQKLKEERSSYLEYQKVMREIEhlsrlyiayqfllaedtkvrsaEELKEMQDK 209
Cdd:COG4942 17 AQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALE----------------------RRIAALARR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 210 VIKLQEELSENDKKIKALNHEIEELEKRKDKETGGI-------------------------------------------- 245
Cdd:COG4942 71 IRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlgrqpplalllspedfldavrrlqylkylaparre 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 246 -LRSLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALA 324
Cdd:COG4942 151 qAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
....
gi 1034663584 325 AAQQ 328
Cdd:COG4942 231 RLEA 234
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
617-895 |
7.68e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 617 ARSQAASILTKfQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQqwemKTEEADLLQTKLQQSsyHKQQEELD 696
Cdd:TIGR00618 201 LRSQLLTLCTP-CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE----AQEEQLKKQQLLKQL--RARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 697 ALKKTIEESEETL-------------KNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMK 763
Cdd:TIGR00618 274 AQEAVLEETQERInrarkaaplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 764 EK--QQEVEAITLELEELKREHT------SYKQQLEAVNEAIKSYESQIEVMAAEVAknKESVNKAQEEVTKQKEVITAQ 835
Cdd:TIGR00618 354 EIhiRDAHEVATSIREISCQQHTltqhihTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLAHAKK 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034663584 836 DTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHK-REAEDGAAKVSKMLKDYDWINAER 895
Cdd:TIGR00618 432 QQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQIHLQETRKKAVV 492
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
627-762 |
8.02e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 627 KFQELK-DVQDELRIKENELRALEEELaglkntAEKYRQLKQQWE-MKTEEADLLQtklQQSSYHKQQEELDALKKTIEE 704
Cdd:PRK12704 65 EIHKLRnEFEKELRERRNELQKLEKRL------LQKEENLDRKLElLEKREEELEK---KEKELEQKQQELEKKEEELEE 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 705 SEETLKntKEIQR-----KAEEKYEVLENKMKNAEAERERELKDAQKKldcAKTKADASSKKM 762
Cdd:PRK12704 136 LIEEQL--QELERisgltAEEAKEILLEKVEEEARHEAAVLIKEIEEE---AKEEADKKAKEI 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
192-417 |
8.03e-04 |
|
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: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 192 AEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRkdketggiLRSLEDALAEAQRVNTKSQSAFDLKK 271
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE--------LEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 272 KNLACE-----ESKRKELEKNMVEDSKTLAAkekevkkITDGLHALQEASNKDAEALAAAQQhfnavsaglssnedgAEA 346
Cdd:COG3883 86 EELGERaralyRSGGSVSYLDVLLGSESFSD-------FLDRLSALSKIADADADLLEELKA---------------DKA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034663584 347 TLAGQmmacKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKK 417
Cdd:COG3883 144 ELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
615-830 |
8.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 615 GGARSQAASILTKFQELKDVQDELRikeNELRALEEELAGLKNTAEKYR----QLKQQWEMKTEEADLLQTKLQQSSYHK 690
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELR---EEAAELESELEEAREAVEDRReeieELEEEIEELRERFGDAPVDLGNAEDFL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 691 Q--QEELDALKKTIEESEETLKNTKEIQRKAE----------------------------EKYEVLENKMKNAEAERER- 739
Cdd:PRK02224 415 EelREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEv 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 740 --------ELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEV 811
Cdd:PRK02224 495 eerleraeDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
250
....*....|....*....
gi 1034663584 812 AknkeSVNKAQEEVTKQKE 830
Cdd:PRK02224 575 A----ELNSKLAELKERIE 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
125-412 |
8.99e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 125 EYKKIAAQ-KTIEKKEAKLKEIKTILEEEIT--PTIQKLKEERSSYLEYQKVMREI--EHLSRLYIAYQFLLAEDTKVRS 199
Cdd:PRK03918 460 ELKRIEKElKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELEEKLKKYnlEELEKKAEEYEKLKEKLIKLKG 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 200 --------AEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKsqsafdlkK 271
Cdd:PRK03918 540 eikslkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA--------E 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 272 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQeaSNKDAEALAAAQQHFNAVSAGLSSNEDGAEAtlagq 351
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEE----- 684
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034663584 352 mmackndISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLE 412
Cdd:PRK03918 685 -------LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
629-814 |
1.05e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAGLKNtAEKyrQLKQQWEMKTEEADLLQTKL-QQSSYHKQQEELDALKKTIEESEE 707
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNE-AES--DLEQDYQAASDHLNLVQTALrQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 708 TLKNTKEIQRKAEEKYEVLENKMKNAEAererELKDAQKKLDCAKTKADA---SSKKMKEKQQEVEAITLELEELKREHT 784
Cdd:PRK04863 370 VVEEADEQQEENEARAEAAEEEVDELKS----QLADYQQALDVQQTRAIQyqqAVQALERAKQLCGLPDLTADNAEDWLE 445
|
170 180 190
....*....|....*....|....*....|
gi 1034663584 785 SYKQQLEAVNEAIKSYESQIEVmaAEVAKN 814
Cdd:PRK04863 446 EFQAKEQEATEELLSLEQKLSV--AQAAHS 473
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-370 |
1.09e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 201 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETggilRSLEDALAEAQR-----------VNTKSQSAFDL 269
Cdd:COG3883 44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR----EELGERARALYRsggsvsyldvlLGSESFSDFLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 270 KKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 349
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180
....*....|....*....|.
gi 1034663584 350 GQMMACKNDISKAQTEAKQAQ 370
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAA 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
725-845 |
1.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 725 VLENKMKNAEAERERELKDAQKKLDCAKtkadasSKKMKEKQQEVEAITLELEelkREHTSYKQQLEAVNEAIKSYESQI 804
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK------KEALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1034663584 805 EVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAE 845
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
125-300 |
1.15e-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: 43.19 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 125 EYKKIAAQKTIE----KKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQ----KVMREIEHLSRLYI-------AYQF 189
Cdd:pfam17380 338 EQERMAMEREREleriRQEERKRELERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVKIleeerqrKIQQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 190 LLAEDTKVRSAEElKEMQDKVIKLQEELSENDKKIK----ALNHEIEEL----EKRKDKETGGILRSLEDALAEAQRVNT 261
Cdd:pfam17380 418 QKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRleeqERQQQVERLrqqeEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034663584 262 KSQSaFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEK 300
Cdd:pfam17380 497 LEKE-LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER 534
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
617-823 |
1.17e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 617 ARSQAASILTKF--QELKDVQDELRIKENELRALEEElAGLKNTAEKYRQLKQQweMKTEEADLLQTKLQQSSYHKQQEE 694
Cdd:COG3206 168 LRREEARKALEFleEQLPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQ--LSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 695 LDALKKTIEESEETLKNTKEIQRkaeekyevLENKMKNAEAERER----------ELKDAQKKLdcaktkADASSKKMKE 764
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQ--------LRAQLAELEAELAElsarytpnhpDVIALRAQI------AALRAQLQQE 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663584 765 KQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSY---ESQIEVMAAEVAKNKES----VNKAQE 823
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELyeslLQRLEE 376
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
757-881 |
1.18e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 757 ASSKKMKEKQQEVEAITLELEELKREhtsYKQQLEAVNEAIKSYESQIEVMAaevaknKESVNKAQEEVtkqKEVITAQD 836
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEE---LEEKKEKLQEEEDKLLEEAEKEA------QQAIKEAKKEA---DEIIKELR 594
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034663584 837 TVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKV 881
Cdd:PRK00409 595 QLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
674-956 |
1.21e-03 |
|
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: 43.29 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 674 EEADLLQTKLQ-QSSYHKQQEE--------LDALKKTIEESEETLKNTKEIQRKaeekyevLENKMKNAEAERERELKDA 744
Cdd:pfam12128 604 ERLDKAEEALQsAREKQAAAEEqlvqangeLEKASREETFARTALKNARLDLRR-------LFDEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 745 QKKLDCAKTKADASSKKMKEKQQEVEAitlELEELKREHTSYKQQ-LEAVNEAIKSYESQIevmaaevaknkesvnkaqe 823
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLE---EQKEQKREARTEKQAyWQVVEGALDAQLALL------------------- 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 824 evtkqKEVITAQDTVIKAKyaevAKHKEQNNDSQLKIKELD-HNISKHKREAEDGAAKVSKMLKD----YDWINAERHLF 898
Cdd:pfam12128 735 -----KAAIAARRSGAKAE----LKALETWYKRDLASLGVDpDVIAKLKREIRTLERKIERIAVRrqevLRYFDWYQETW 805
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034663584 899 GQPNSAYDFKTNNPKEAGQRLQ---KLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKR 956
Cdd:pfam12128 806 LQRRPRLATQLSNIERAISELQqqlARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
624-859 |
1.29e-03 |
|
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: 43.09 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 624 ILTKFQELKDVQDELRIKENELRALEEELAGLKNTAE--KYRQLKQQWEMKTEEADLL----QTKLQQSSYHKQQEELDA 697
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdlNDKLKKNKDKINKLNSDLSkinsEIKNDKEQKNKLEVELNK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 698 LKKTIEESEETL-KNTKEIQRKAEE------KYEVLENKMKNAEAER---ERELKDAQKKLDCAKTKADASS------KK 761
Cdd:TIGR04523 129 LEKQKKENKKNIdKFLTEIKKKEKEleklnnKYNDLKKQKEELENELnllEKEKLNIQKNIDKIKNKLLKLElllsnlKK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 762 MKEKQQEVEAITLELEE----LKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVI---TA 834
Cdd:TIGR04523 209 KIQKNKSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIkelEK 288
|
250 260
....*....|....*....|....*
gi 1034663584 835 QDTVIKAKYAEVAKHKEQNNDSQLK 859
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWNKELK 313
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1016-1070 |
1.43e-03 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 42.78 E-value: 1.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034663584 1016 DGLEFKVAlgntwkENLTELSGGQRSLVALSlilsMLLFKPAPIYILDEVDAALD 1070
Cdd:TIGR02203 457 LGLDTPIG------ENGVLLSGGQRQRLAIA----RALLKDAPILILDEATSALD 501
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1035-1084 |
1.45e-03 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 41.31 E-value: 1.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1035 LSGGQRSLVALSLilsmLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTH 1084
Cdd:COG4133 132 LSAGQKRRVALAR----LLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
753-895 |
1.46e-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: 41.45 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 753 TKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKEsvnkAQEEVTKQKEvi 832
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----QLGNVRNNKE-- 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 833 taqdtvIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAER 895
Cdd:COG1579 91 ------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
744-820 |
1.55e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 744 AQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNK 820
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
198-449 |
1.59e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 198 RSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEK-----RKDKETGGILRSLEDA--LAEAQRVNTKSQSAFDLK 270
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKtikreKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLK 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 271 KKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHA-LQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLA 349
Cdd:COG5022 866 KETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESeIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEG 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 350 GQMMACKNDISKAQTEAKQaqmKLKHAQQELKNkqaEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLL 429
Cdd:COG5022 946 PSIEYVKLPELNKLHEVES---KLKETSEEYED---LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLK 1019
|
250 260
....*....|....*....|...
gi 1034663584 430 EKRRQLSR---DIGRLKETYEAL 449
Cdd:COG5022 1020 ELPVEVAElqsASKIISSESTEL 1042
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
751-828 |
1.68e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034663584 751 AKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQ 828
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1031-1082 |
1.73e-03 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 41.57 E-value: 1.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1034663584 1031 NLTELSGGQRSLVAlsliLSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1082
Cdd:COG1120 134 PVDELSGGERQRVL----IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLR 181
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1012-1064 |
1.74e-03 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 40.32 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 1012 QTVLDGLEFKVALGNTWKENLTELSGGQRSLVAlsliLSMLLFKPAPIYILDE 1064
Cdd:pfam00005 99 EEALEKLGLGDLADRPVGERPGTLSGGQRQRVA----IARALLTKPKLLLLDE 147
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
646-937 |
1.92e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 646 RALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSsyhkqQEELDALKKTIEESEETLKNTKEIQRKAEEKYEV 725
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA-----RSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 726 LENKMKNAEAERER---ELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYES 802
Cdd:COG4372 106 LQEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 803 QIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVakhKEQNNDSQLKIKELDHNISKHKREAEDGAAKVS 882
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA---KLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1034663584 883 KMLKDYDWINAERHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVNMRA 937
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-302 |
2.02e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 41.82 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1 MHIKSIILEGFKSYaQRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLgisnlsqvviggRNKYLINGVNANNTRVQDL 80
Cdd:pfam13175 1 MKIKSIIIKNFRCL-KDTEID-LDEDLTVLIGKNNSGKSSILEALDIFL------------NNKEKFFEDDFLVLYLKDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 81 FCSVGLNVNNPHFLIMQGRItkVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKL 160
Cdd:pfam13175 67 IKIDKEDLNIFENISFSIDI--EIDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 161 KEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEEL----KEMQDKVIKLQEELSENDKKIKALNHEIEELEK 236
Cdd:pfam13175 145 LKQFKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEikvdKEDLKKLINELEKSINYHENVLENLQIKKLLIS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663584 237 RKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKkknlacEESKRKELEKNMVEDSKTLAAKEKEV 302
Cdd:pfam13175 225 ADRNASDEDSEKINSLLGALKQRIFEEALQEELE------LTEKLKETQNKLKEIDKTLAEELKNI 284
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-48 |
2.07e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 41.51 E-value: 2.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034663584 3 IKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFL 48
Cdd:cd03242 1 LKSLELRNFRNYA-ELELE-FEPGVTVLVGENAQGKTNLLEAISLL 44
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1014-1082 |
2.27e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.59 E-value: 2.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663584 1014 VLDGLEFkVALGNTWKENLTELSGGQRSLValslILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLR 1082
Cdd:cd03235 113 VDEALER-VGLSELADRQIGELSGGQQQRV----LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
631-852 |
2.29e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 631 LKDVQDELRIKENEL----RALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSyhKQQEELDALKKTIEESE 706
Cdd:PRK01156 185 IDYLEEKLKSSNLELenikKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELS--SLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 707 ETLKNTKEIQRK---AEEKYEVLENKMKNAEAERERE----------LKDAQKKLDCAKTKADASSKKMKE--------- 764
Cdd:PRK01156 263 SDLSMELEKNNYykeLEERHMKIINDPVYKNRNYINDyfkykndienKKQILSNIDAEINKYHAIIKKLSVlqkdyndyi 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 765 -KQQEVEAITLELEELKREHTSYK---QQLEAVNEAIKSYESQIEVMAAEVAK-------NKESVNKAQEEVTKQKEVIT 833
Cdd:PRK01156 343 kKKSRYDDLNNQILELEGYEMDYNsylKSIESLKKKIEEYSKNIERMSAFISEilkiqeiDPDAIKKELNEINVKLQDIS 422
|
250
....*....|....*....
gi 1034663584 834 AQDTVIKAKYAEVAKHKEQ 852
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDE 441
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-50 |
2.37e-03 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 40.66 E-value: 2.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1034663584 3 IKSIILEGFKSYAqRTEVNgFDPLFNAITGLNGSGKSNILDSICFLLG 50
Cdd:cd03276 1 IESITLKNFMCHR-HLQIE-FGPRVNFIVGNNGSGKSAILTALTIGLG 46
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1009-1093 |
2.55e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.85 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1009 PEGQTVLDGLE-FKVALgNTWKENLTELSGGQRSLVALsliLSMLLFKPApIYILDEVDAALDLSHTQNIGQMLrTHFTH 1087
Cdd:PRK10247 112 PDPAIFLDDLErFALPD-TILTKNIAELSGGEKQRISL---IRNLQFMPK-VLLLDEITSALDESNKHNVNEII-HRYVR 185
|
....*.
gi 1034663584 1088 SQFIVV 1093
Cdd:PRK10247 186 EQNIAV 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1034-1093 |
2.62e-03 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 40.54 E-value: 2.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 1034 ELSGGQRSLVALsliLSMLLFKPAPIyILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVV 1093
Cdd:COG4136 133 TLSGGQRARVAL---LRALLAEPRAL-LLDEPFSKLDAALRAQFREFVFEQIRQRGIPAL 188
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
617-955 |
2.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 617 ARSQAASILTKFQELKDVQDELRIKENELRALEEELaGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELD 696
Cdd:PTZ00121 1062 AKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAF-GKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 697 ALK--KTIEESEETLKNTK-------EIQRKAEEKYEVlENKMKNAEAERERELKDAQ--KKLDCAKTKAD---ASSKKM 762
Cdd:PTZ00121 1141 KAEeaRKAEDAKRVEIARKaedarkaEEARKAEDAKKA-EAARKAEEVRKAEELRKAEdaRKAEAARKAEEerkAEEARK 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 763 KEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYES--------QIEVMAAEVAKNKESVNKAQE-----EVTKQK 829
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEarmahfarRQAAIKAEEARKADELKKAEEkkkadEAKKAE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 830 EVITAQDTVIKAKYAEVAKH-KEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFK 908
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034663584 909 TNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKK 955
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
629-761 |
2.92e-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: 41.37 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAglkNTAEKYRQLKQQWEMKTEEAdllqtKLQQSSYHKQQEELDALKKTIEESEET 708
Cdd:TIGR02794 80 AEKQRAAEQARQKELEQRAAAEKAA---KQAEQAAKQAEEKQKQAEEA-----KAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 709 LKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKK 761
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
189-431 |
3.00e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 189 FLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKetggilrsLEDALAEAQRvntksqsafd 268
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------LQAELEALQA---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 269 lkkknlaceesKRKELEKNMVEDSKTLAAKEKEVKKItdgLHALQEASNK--------DAEALAAAQQHFNAVSAGLSSN 340
Cdd:COG3883 66 -----------EIDKLQAEIAEAEAEIEERREELGER---ARALYRSGGSvsyldvllGSESFSDFLDRLSALSKIADAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 341 EDgaeatLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNY 420
Cdd:COG3883 132 AD-----LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
250
....*....|.
gi 1034663584 421 EENKEESLLEK 431
Cdd:COG3883 207 AAEAAAAAAAA 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
629-832 |
3.23e-03 |
|
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: 41.54 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 629 QELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQE------ELDALKKTI 702
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 703 EESEETLKNTKEIQRKAEEKYEVLENKMKNAEAE-------------------RERELKDAQKKLDCAKTKADASSKKMK 763
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisdledelnkddfelkkenLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663584 764 EKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVI 832
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
358-432 |
3.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034663584 358 DISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKR 432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
27-63 |
4.25e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.15 E-value: 4.25e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1034663584 27 FNAITGLNGSGKSNILDSICFLLGISNlSQVVIGGRN 63
Cdd:cd00267 27 IVALVGPNGSGKSTLLRAIAGLLKPTS-GEILIDGKD 62
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
642-792 |
4.31e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 642 ENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTklqqssyhkQQEELDALK------KTIEESEETLKNTKEI 715
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDLLRF---------QLEELEAAAlqpgeeEELEEERRRLSNAEKL 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034663584 716 QRKAEEKYEVLENKMKNAEAererELKDAQKKLDcaktKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEA 792
Cdd:COG0497 225 REALQEALEALSGGEGGALD----LLGQALRALE----RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEF 293
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
127-375 |
4.91e-03 |
|
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: 41.26 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 127 KKIAAQKTIEKKEAKLKEIKtILEEEITPTIQKLkEERSSYLEYQKVmreiehlsrlyiayQFLLAEDTKVRSAEELKEM 206
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFK-ILKDKKDAKIREL-EARVSDLELEKV--------------KLVNAGSERLRAVKDIKQE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 207 QDKVIKlQEELSENDKKIKALNHEI---------EELEKRKDK-------------ETGGILRSLEDALAEAQRVNTKSQ 264
Cdd:pfam15921 655 RDQLLN-EVKTSRNELNSLSEDYEVlkrnfrnksEEMETTTNKlkmqlksaqseleQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 265 SAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDA---EALAAAQQHFNAVSAGLSSNE 341
Cdd:pfam15921 734 KQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVANMEVAL 813
|
250 260 270
....*....|....*....|....*....|....
gi 1034663584 342 DGAEAtlagQMMACKNDISKAQTEAkqAQMKLKH 375
Cdd:pfam15921 814 DKASL----QFAECQDIIQRQEQES--VRLKLQH 841
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
639-835 |
5.22e-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: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 639 RIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEE--LDALKKTIEESEETLKNTKEIQ 716
Cdd:TIGR02794 54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQaaKQAEEKQKQAEEAKAKQAAEAK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 717 RKAEEKYEVLENKMKNAEAERERELK---DAQKKLDCAKTKADASSKKMKEKQQEVEAitlelEELKREHTSYKQQLEAv 793
Cdd:TIGR02794 134 AKAEAEAERKAKEEAAKQAEEEAKAKaaaEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-----EEAKAKAEAAKAKAAA- 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034663584 794 nEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQ 835
Cdd:TIGR02794 208 -EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
201-451 |
6.12e-03 |
|
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: 40.77 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 201 EELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKR---KDKETGGILRSLEDALAEAQRVNTKSQSAFD------LKK 271
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltnSESENSEKQRELEEKQNEIEKLKKENQSYKQeiknleSQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 272 KNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAE---ATL 348
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLEtqlKVL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 349 AGQMMACKNDISKAQTEAKQAQ---MKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEK----LEAEMKKLNYE 421
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisdLEDELNKDDFE 553
|
250 260 270
....*....|....*....|....*....|
gi 1034663584 422 ENKEEsLLEKRRQLSRDIGRLKETYEALLA 451
Cdd:TIGR04523 554 LKKEN-LEKEIDEKNKEIEELKQTQKSLKK 582
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
691-850 |
6.84e-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: 40.21 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 691 QQEELDALKKTIEEseetlknTKEIQRKAEEKyevleNKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVE 770
Cdd:TIGR02794 56 QQQKKPAAKKEQER-------QKKLEQQAEEA-----EKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 771 AITLELEELKREHTSYKQQlEAVNEAIKSYESQIEVMAAEVAKNK--ESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAK 848
Cdd:TIGR02794 124 AKAKQAAEAKAKAEAEAER-KAKEEAAKQAEEEAKAKAAAEAKKKaeEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAK 202
|
..
gi 1034663584 849 HK 850
Cdd:TIGR02794 203 AK 204
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
617-834 |
7.32e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 617 ARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTaekyrqlkqQWEMKTEEADLLQTKLQQSSYHKQQEELD 696
Cdd:PRK01156 527 ARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRT---------SWLNALAVISLIDIETNRSRSNEIKKQLN 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 697 ALKKTIEESEETLKNTKEIQ----RKAEEKYEVLENKMKNAEaERERELKDAQKKLDCAKTKadasSKKMKEKQQEVEAI 772
Cdd:PRK01156 598 DLESRLQEIEIGFPDDKSYIdksiREIENEANNLNNKYNEIQ-ENKILIEKLRGKIDNYKKQ----IAEIDSIIPDLKEI 672
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034663584 773 TLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITA 834
Cdd:PRK01156 673 TSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
646-805 |
8.12e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.12 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 646 RALEEELAGLKNTAEKYRQLKQQWEMKTEEadlLQTKLQQssyhkQQEELDALKKTIEESE---ETLKNTKEIQRKAEEK 722
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEKLMSEIQQENKR---LTEPLQK-----AQEEVEELRKQLENYEkdkQSLKNLKARLKVLEKE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 723 -------YEVLENKMKNAEAER-------ERELKDAQKKLDCaktKADASSKKMKEKQQEVEAITLELEELKR----EHT 784
Cdd:pfam13851 101 lkdlkweHEVLEQRFEKVERERdelydkfEAAIQDVQQKTGL---KNLLLEKKLQALGETLEKKEAQLNEVLAaanlDPD 177
|
170 180
....*....|....*....|.
gi 1034663584 785 SYKQQLEAVNEAIKSYESQIE 805
Cdd:pfam13851 178 ALQAVTEKLEDVLESKNQLIK 198
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
206-427 |
8.93e-03 |
|
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: 40.19 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 206 MQDKVIKLQEELSENDKKIKALNHEIEELEKrKDKETGGILRSLEDALAEAQRVntksqsafdlkkknlacEESKRKELE 285
Cdd:pfam10174 399 LQKKIENLQEQLRDKDKQLAGLKERVKSLQT-DSSNTDTALTTLEEALSEKERI-----------------IERLKEQRE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 286 KNMVEDSKTLAAKEKEVKKITDGLHALQ-EASNKDAEALAAAQQHFNAVSAGLssNEDGAEATLAGQMMACKNDISKAQT 364
Cdd:pfam10174 461 REDRERLEELESLKKENKDLKEKVSALQpELTEKESSLIDLKEHASSLASSGL--KKDSKLKSLEIAVEQKKEECSKLEN 538
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034663584 365 EAKQAQM-------------KLKHAQQELKNKQAEVKKMDSGYRKDQEAL---EAVKRLKEKLEAEMKKLNYEENKEES 427
Cdd:pfam10174 539 QLKKAHNaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILrevENEKNDKDKKIAELESLTLRQMKEQN 617
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
638-816 |
9.20e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 638 LRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTE-EADLLQTKLQQSSYHK---------------QQEELDALKKT 701
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSlKAEVLIQKFGRSLKAKkrfsllkketiylqsAQRVELAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 702 IEESEE--TLKNTKEIQRKAEEKY----------EVLENKMKNAEAERERELK---DAQKKLDCAKTKADASSK------ 760
Cdd:COG5022 885 QELKIDvkSISSLKLVNLELESEIielkkslssdLIENLEFKTELIARLKKLLnniDLEEGPSIEYVKLPELNKlheves 964
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034663584 761 KMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKE 816
Cdd:COG5022 965 KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKE 1020
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
191-320 |
9.48e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034663584 191 LAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKdketggilRSLEDALAEAQRVNTKSQSAFDLK 270
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV--------EELEAELEEKDERIERLERELSEA 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034663584 271 KKNLACEESKRKELEK--NMVED-SKTLAAKEKEVKKITDGLHALQEASNKDA 320
Cdd:COG2433 454 RSEERREIRKDREISRldREIERlERELEEERERIEELKRKLERLKELWKLEH 506
|
|
| |
