|
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 ... |
11-1202 |
0e+00 |
|
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: 595.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 11 MITHIVNQNFKSYAgEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK-IRSKKLSVLIHnSDEHKDIQSCTVE 89
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKsLRSERLSDLIH-SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 90 VHFqkiidKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 169
Cdd:pfam02463 79 ITF-----DNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 170 GQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNH 249
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 250 VCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVR 329
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 330 EKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKESR 409
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 410 EKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLPQTEQELKEKEKE 489
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 490 LQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDVAISSCCHALD 569
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 570 YIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFdlvkvkdekirqafyfalrdtlvadNL 649
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA-------------------------QL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 650 DQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLE 729
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 730 ERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVE 809
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 810 AEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAE 889
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 890 LKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISK 969
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 970 ISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYLQRVAELDKITYERDSFR 1049
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1050 QAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSL 1129
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVAL 1088
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925443 1130 ALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNITKS 1202
Cdd:pfam02463 1089 ALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
12-1193 |
6.60e-122 |
|
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: 405.61 E-value: 6.60e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 12 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGY-RAQKIRSKKLSVLIHNSDEHKDIQSCTVEV 90
Cdd:TIGR02169 2 IERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLsSSKAMRAERLSDLISNGKNGQSGNEAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 91 HFQKIIDKEGDDYEVIpnsnfyVSRTACRDN-TSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFlILQGEVEQIAMMKPK 169
Cdd:TIGR02169 81 TFKNDDGKFPDELEVV------RRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 170 GQTEhdegmleYLEDIIGCGRLNEPIKVLCRRVEILnehrGEKLNRVKMVEKEK----DALEGEKNIAIEFLTLENEIFr 245
Cdd:TIGR02169 154 ERRK-------IIDEIAGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKrqqlERLRREREKAERYQALLKEKR- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 246 kknhvcQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEEN--------KEK 317
Cdd:TIGR02169 222 ------EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 318 FTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKsnniINETTTRNNALEKEKEKEEKKLKEVMDSLKQ 397
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE----LEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 398 ETQGLQK-------EKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIR 470
Cdd:TIGR02169 372 ELEEVDKefaetrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 471 DIEGKLPQTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGrIPGIYGRLGDL 550
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS-IQGVHGTVAQL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 551 GAIDEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFDLVKVkD 629
Cdd:TIGR02169 531 GSVGERYATAIEVAAGNrLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-D 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 630 EKIRQAFYFALRDTLVADNLDQATRVAYQkdrrWRVVTLQGQIIEQSGTMTGGgSKVMKGRMGSSLVIEISEEEVNKMES 709
Cdd:TIGR02169 610 PKYEPAFKYVFGDTLVVEDIEAARRLMGK----YRMVTLEGELFEKSGAMTGG-SRAPRGGILFSRSEPAELQRLRERLE 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 710 QLQNDSKKAMQ-IQEQKVQLEERVVKLRHSEREMRnTLEKftaSIQRLIEQEEYLNVQVKELEANVlatapDKKKQKLle 788
Cdd:TIGR02169 685 GLKRELSSLQSeLRRIENRLDELSQELSDASRKIG-EIEK---EIEQLEQEEEKLKERLEELEEDL-----SSLEQEI-- 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 789 ENVSAFKTEYDAV----AEKAGKVEAEVKRL-----HNTIVEINNHkLKAQQDKLDKINKQLDECASAITKAQVAIKTAD 859
Cdd:TIGR02169 754 ENVKSELKELEARieelEEDLHKLEEALNDLearlsHSRIPEIQAE-LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 860 RNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHalqkda 939
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE------ 906
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 940 lSIKLKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEiSVLSPEDLEAiknpdsitnQIALLEARCHEMKP-NL 1018
Cdd:TIGR02169 907 -ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQA---------ELQRVEEEIRALEPvNM 975
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1019 GAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTlGGDAELELVDSLDPF 1098
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELILENPDDPF 1054
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1099 SEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIIS 1178
Cdd:TIGR02169 1055 AGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVS 1134
|
1210
....*....|....*
gi 767925443 1179 LRNNMFEISDRLIGI 1193
Cdd:TIGR02169 1135 LRSPMIEYADRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-1193 |
4.33e-99 |
|
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: 342.42 E-value: 4.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 20 FKSYAgEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFqkiiD 97
Cdd:TIGR02168 10 FKSFA-DPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGeQSAKALRGGKMEDVIFNgSETRKPLSLAEVELVF----D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 98 KEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLL-------RSHGIdldhnrflILQGEVEQIAMMKPkg 170
Cdd:TIGR02168 85 NSDGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFldtglgkRSYSI--------IEQGKISEIIEAKP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 171 qtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILN--EHRGEKLNRV----KMVEKEKDALEGEKNIAIEFLTLENEIF 244
Cdd:TIGR02168 155 -----EERRAIFEEAAGISKYKE------RRKETERklERTRENLDRLedilNELERQLKSLERQAEKAERYKELKAELR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 245 RKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLE 324
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 325 DVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEkekeekklkevMDSLKQETQGLQK 404
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELES 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 405 EKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKErkAAIRDIEGKLPQTEQELK 484
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 485 EKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQE------------KKSGRIPGIYGRLGDLGA 552
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsegvkallKNQSGLSGILGVLSELIS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 553 IDEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPR----LFDLVKV 627
Cdd:TIGR02168 531 VDEGYEAAIEAALGGrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvAKDLVKF 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 628 kDEKIRQAFYFALRDTLVADNLDQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKM 707
Cdd:TIGR02168 611 -DPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 708 ESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlatapdkkkqkll 787
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL------------- 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 788 eENVSAFKTEYDAVAEKAGKVEAEVKRlhntiveinnhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQD 867
Cdd:TIGR02168 757 -TELEAEIEELEERLEEAEEELAEAEA-----------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 868 SVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLE 947
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 948 QIDGHIAEHNSKIKYWHKEISKISLHPIE-----DNPIEEISVLSPEDLE-AIKNPDSITNQIALLEARCHEMKP----- 1016
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGlevriDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENkikel 984
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1017 ---NLGAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVD 1093
Cdd:TIGR02168 985 gpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTD 1064
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1094 SLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQ 1173
Cdd:TIGR02168 1065 PEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQ 1144
|
1210 1220
....*....|....*....|
gi 767925443 1174 FIIISLRNNMFEISDRLIGI 1193
Cdd:TIGR02168 1145 FIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
10-169 |
2.61e-67 |
|
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: 225.64 E-value: 2.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 10 LMITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVE 89
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHPNLDSCSVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 90 VHFQKIIDKEgddyevipnsnfyvsrtacrdntsvyhisgkkktfkdvgnLLRSHGIDLDHNRFLILQGEVEQIAMMkPK 169
Cdd:cd03274 81 VHFQEIIDKP----------------------------------------LLKSKGIDLDHNRFLILQGEVEQIAQM-PK 119
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-1193 |
8.19e-67 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 244.85 E-value: 8.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 12 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG---YRAqkIRSKKLSVLIHN-SDEHKDIQSCT 87
Cdd:COG1196 3 LKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGeqsAKS--LRGGKMEDVIFAgSSSRKPLGRAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 88 VEVHF---QKIIDkeGDDYEVIpnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLD-HNrfLILQGEVEQI 163
Cdd:COG1196 80 VSLTFdnsDGTLP--IDYDEVT------ITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPEsYS--IIGQGMIDRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 164 AMMKPkgqtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILNEHRG--EKLNRVK--MVEKEK--DALEGEKNIAIEFL 237
Cdd:COG1196 150 IEAKP-------EERRAIIEEAAGISKYKE------RKEEAERKLEAteENLERLEdiLGELERqlEPLERQAEKAERYR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 238 TLENEIFRKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEK 317
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 318 FTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLkevmDSLKQ 397
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL----LEAEA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 398 ETQGLQKEKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLP 477
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 478 QTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSS----LAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAI 553
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARllllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 554 DEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVwAKKMTEIQTPENTPRLFDLVKVkDEKI 632
Cdd:COG1196 533 EAAYEAALEAALAAaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA-RAALAAALARGAIGAAVDLVAS-DLRE 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 633 RQAFYFALRDTLV-----ADNLDQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKvmKGRMGSSLVIEISEEEVNKM 707
Cdd:COG1196 611 ADARYYVLGDTLLgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR--ELLAALLEAEAELEELAERL 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 708 ESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEkftasiQRLIEQEEYLNVQVKELEANVLATAPDkkkqkll 787
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE------QLEAEREELLEELLEEEELLEEEALEE------- 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 788 eenvsafkteydavaekagkveaevkrlhntiveinnhklkaqqdkldkinkqldecasaitkaqvaiktadrnlqkaqd 867
Cdd:COG1196 --------------------------------------------------------------------------------
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 868 svLRTEKEIKDTEKEVDDLTAELKSLEDkaaeVvkNTNAAEEsLPEIQKEHRNLLQELkviqenehalqkdalsiklkle 947
Cdd:COG1196 756 --LPEPPDLEELERELERLEREIEALGP----V--NLLAIEE-YEELEERYDFLSEQR---------------------- 804
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 948 qidghiaehnskikywhkeiskislhpiednpieeisvlspEDLEaiknpdsitnqiallEARchemkpnlgaiaeykkk 1027
Cdd:COG1196 805 -----------------------------------------EDLE---------------EAR----------------- 811
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1028 EELyLQRVAELDKITYERdsFRQAYEDLRKQrlnefmagfyiitnkLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVR 1107
Cdd:COG1196 812 ETL-EEAIEEIDRETRER--FLETFDAVNEN---------------FQELFPRLFGGGEAELLLTDPDDPLETGIEIMAQ 873
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1108 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEIS 1187
Cdd:COG1196 874 PPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAA 953
|
....*.
gi 767925443 1188 DRLIGI 1193
Cdd:COG1196 954 DRLYGV 959
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1109-1203 |
3.23e-65 |
|
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: 219.47 E-value: 3.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1109 PKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISD 1188
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAD 197
|
90
....*....|....*
gi 767925443 1189 RLIGIYKTYNITKSV 1203
Cdd:cd03274 198 RLVGIYKTNNCTKSV 212
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
541-655 |
1.51e-32 |
|
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: 122.72 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 541 PGIYGRLGDLGAIDEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAV-----WAKKMTEIQT 614
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGrLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPrspagSKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767925443 615 PENTPRLFDLVKVkDEKIRQAFYFALRDTLVADNLDQATRV 655
Cdd:smart00968 81 PGFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1119-1201 |
2.81e-32 |
|
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: 123.96 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1119 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKN-AQFIIISLRNNMFEISDRLIGIYKTY 1197
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 767925443 1198 NITK 1201
Cdd:cd03239 175 GVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
18-170 |
2.94e-31 |
|
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: 123.45 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 18 QNFKSYAGEKILGPFhKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFQkii 96
Cdd:cd03275 7 ENFKSYKGRHVIGPF-DRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRaRVGKPDSNSAYVTAVYE--- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925443 97 dkegDDYEVIPnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKG 170
Cdd:cd03275 83 ----DDDGEEK-----TFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPPG 147
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1108-1195 |
1.83e-29 |
|
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: 118.06 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1108 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEI 1186
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEFFSK 224
|
....*....
gi 767925443 1187 SDRLIGIYK 1195
Cdd:cd03275 225 ADALVGVYR 233
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
540-656 |
1.08e-28 |
|
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: 111.58 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 540 IPGIYGRLGDLGAIDEKYDVAISSCC-HALDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTpENT 618
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALgGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLK-GGA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 767925443 619 PRLFDLVKVKDEkIRQAFYFALRDTLVADNLDQATRVA 656
Cdd:pfam06470 80 GPLLDLVEYDDE-YRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1114-1193 |
1.25e-27 |
|
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: 111.40 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1114 KKIFN---LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRL 1190
Cdd:cd03278 106 KKVQRlslLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
...
gi 767925443 1191 IGI 1193
Cdd:cd03278 186 YGV 188
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
12-95 |
3.21e-27 |
|
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: 109.32 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 12 ITHIVNQNFKSYAGEKILGPFHkRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHnSDEHKDIQSCTVEVH 91
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSN-SFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAG-GGVKAGINSASVEIT 78
|
....
gi 767925443 92 FQKI 95
Cdd:cd03239 79 FDKS 82
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1116-1196 |
1.07e-23 |
|
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: 98.97 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1116 IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEISDRLIGIY 1194
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIK 154
|
..
gi 767925443 1195 KT 1196
Cdd:cd03227 155 KV 156
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1113-1199 |
9.66e-17 |
|
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: 81.19 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1113 WKK-IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLi 1191
Cdd:cd03273 160 WKEsLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVL- 238
|
....*...
gi 767925443 1192 giYKTYNI 1199
Cdd:cd03273 239 --FRTRFV 244
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1114-1193 |
1.30e-16 |
|
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: 80.77 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1114 KKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1193
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
12-92 |
2.96e-16 |
|
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: 78.28 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 12 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHNSDEHKDIQS-CTVE 89
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGeQSAKSLRGEKMSDVIFAGSETRKPANfAEVT 79
|
...
gi 767925443 90 VHF 92
Cdd:cd03278 80 LTF 82
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
12-166 |
2.05e-15 |
|
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: 77.34 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 12 ITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRA-QKIRSKKLSVLIHNSDEhKDIQSCTVEV 90
Cdd:cd03273 3 IKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKRGQ-AGITKASVTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 91 HFqKIIDKEG-----DDYEVIPnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAM 165
Cdd:cd03273 82 VF-DNSDKSQspigfENYPEIT-----VTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLN 155
|
.
gi 767925443 166 M 166
Cdd:cd03273 156 M 156
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-98 |
7.62e-15 |
|
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: 73.55 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 14 HIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKklsvlihnSDEHKDIQSCTVEVHFQ 93
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRR--------SGVKAGCIVAAVSAELI 72
|
....*
gi 767925443 94 KIIDK 98
Cdd:cd03227 73 FTRLQ 77
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
12-173 |
9.85e-13 |
|
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: 69.21 E-value: 9.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 12 ITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIqSCTVEVH 91
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVM-SAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 92 FQKIidkegDDYEVIPNSNFYVSRT--ACRDNtsvYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 169
Cdd:cd03272 80 FDNS-----DNRFPIDKEEVRLRRTigLKKDE---YFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQD 151
|
....
gi 767925443 170 GQTE 173
Cdd:cd03272 152 EQQE 155
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1116-1195 |
3.00e-08 |
|
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: 54.17 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1116 IFNLSGGEKTLSSLALVFALhhyKPtPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFE-ISDRLIGI 1193
Cdd:cd00267 78 VPQLSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVL 153
|
..
gi 767925443 1194 YK 1195
Cdd:cd00267 154 KD 155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
780-960 |
3.74e-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: 55.70 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 780 DKKKQKLLEEnVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKtad 859
Cdd:COG1579 2 MPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 860 rNLQKAQDSVlRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQEnehALQKDA 939
Cdd:COG1579 77 -KYEEQLGNV-RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEEL 151
|
170 180
....*....|....*....|.
gi 767925443 940 LSIKLKLEQIDGHIAEHNSKI 960
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
11-57 |
5.23e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.48 E-value: 5.23e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767925443 11 MITHIVNQNFKSYAGEKI-LGPFHkrfsCIIGPNGSGKSNVIDSMLFV 57
Cdd:COG4637 1 MITRIRIKNFKSLRDLELpLGPLT----VLIGANGSGKSNLLDALRFL 44
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
694-1061 |
5.62e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 694 SLVIEISEEEVNKMESQLQNDSKKAMQiQEQKVQLEERVVKLRHSEREMRN--TLEKFTA--SIQRLIEQEEYLNVQVKE 769
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETLIASRQEER-QETSAELNQLLRTLDDQWKEKRDelNGELSAAdaAVAKDRSELEALEDQHGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 770 -LEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKI----------- 837
Cdd:pfam12128 334 fLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIreardrqlava 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 838 -----------NKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVD-------DLTAELKSLEDKAAE 899
Cdd:pfam12128 414 eddlqaleselREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDErierareEQEAANAEVERLQSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 900 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIklkleqidghIAEHNSKIKYWHKEISKI--------- 970
Cdd:pfam12128 494 LRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL----------LHFLRKEAPDWEQSIGKVispellhrt 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 971 SLHPI--EDNPIEEISVLSPE-DLEAIKNPDSITNQIAlLEARCHEMKPNLGAIAE-YKKKEELYLQRVAELDKITYERD 1046
Cdd:pfam12128 564 DLDPEvwDGSVGGELNLYGVKlDLKRIDVPEWAASEEE-LRERLDKAEEALQSAREkQAAAEEQLVQANGELEKASREET 642
|
410
....*....|....*..
gi 767925443 1047 SFRQAYE--DLRKQRLN 1061
Cdd:pfam12128 643 FARTALKnaRLDLRRLF 659
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
11-106 |
8.07e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 53.86 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 11 MITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFgYRAQKIRSKKLSVLIHNSDEhkdiqSCTVEV 90
Cdd:COG0419 1 KLLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYAL-YGKARSRSKLRSDLINVGSE-----EASVEL 73
|
90
....*....|....*.
gi 767925443 91 HFQkiidKEGDDYEVI 106
Cdd:COG0419 74 EFE----HGGKRYRIE 85
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
709-955 |
2.45e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.13 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 709 SQLQNDSK-KAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKE-LEANVLATAPDKKKQKL 786
Cdd:pfam05557 12 SQLQNEKKqMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREqAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 787 LEENVSAFKTEYDAVAEKAGKVeAEVKRlhntIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKtadrNLQKAQ 866
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNEL-SELRR----QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 867 DSVLRTEKEIKDTEKEVddltaelkSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQE---LKVIQENEHALQKDALSIK 943
Cdd:pfam05557 163 SSLAEAEQRIKELEFEI--------QSQEQDSEIVKNSKSELARIPELEKELERLREHnkhLNENIENKLLLKEEVEDLK 234
|
250
....*....|..
gi 767925443 944 LKLEQIDGHIAE 955
Cdd:pfam05557 235 RKLEREEKYREE 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
701-1135 |
4.19e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 701 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKL---RHSEREMRNTLEKFTASIQRLIEQEEYLNVQVK-ELEANVLA 776
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAcEQHALLRK 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 777 TAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRlhntivEINNHKLKAQQDKLDKINKQLDECASAITKAQVAik 856
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE------RVREHALSIRVLPKELLASRQLALQKMQSEKEQL-- 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 857 TADRNLQKAQDSVLRTEKE-IKDTEKEVDDLTAELKSLEdkaAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHAL 935
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELEThIEEYDREFNEIENASSSLG---SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEE 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 936 QKDALSIKLKLEQIDGHIAEHNSKIKYWHKEIsKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMK 1015
Cdd:TIGR00618 770 VTAALQTGAELSHLAAEIQFFNRLREEDTHLL-KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1016 PNLGAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVDSL 1095
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNAR 928
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 767925443 1096 DPFSEGIMF------SVRPPKkswkkifNLSGGEKTLSSLALVFAL 1135
Cdd:TIGR00618 929 KYQGLALLVadaytgSVRPSA-------TLSGGETFLASLSLALAL 967
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
727-956 |
4.61e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 727 QLEERVVKLRhserEMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATApdKKKQKLLEENVSAFKTEYDAVAEKAG 806
Cdd:COG4913 239 RAHEALEDAR----EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 807 KVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDEcasaitkAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDL 886
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLEREIER-------LERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 887 TAELKSLEDKAAEVVKntnAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEH 956
Cdd:COG4913 386 RAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
701-912 |
1.64e-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: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 701 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELE---ANVLAT 777
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 778 APDKKKQKLLEENVSAfktEYDAVAEKAGKVEAEVKRLHNTIVEinnhKLKAQQDKLDKINKQLDECASAITKAQVAIKT 857
Cdd:COG4942 113 LYRLGRQPPLALLLSP---EDFLDAVRRLQYLKYLAPARREQAE----ELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767925443 858 ADRNLQKAQDS----VLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLP 912
Cdd:COG4942 186 ERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
786-1009 |
2.82e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 786 LLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKA 865
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE-ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 866 QDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 945
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767925443 946 -LEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEA 1009
Cdd:COG4372 187 eLLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
237-973 |
4.12e-06 |
|
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: 51.27 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 237 LTLENEIFRKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMK-----------AKNKDVKDTEKKLN 305
Cdd:pfam15921 94 LNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvheleaakcLKEDMLEDSNTQIE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 306 KITKFIEENKEKFTQLDLEDVQVREklkhatSKAKKLEKQlqkDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEE 385
Cdd:pfam15921 174 QLRKMMLSHEGVLQEIRSILVDFEE------ASGKKIYEH---DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 386 KKlkevMDSLKQETQG-----LQKEKESREK-------ELMGFSKSVNEARSKMDVAQSELDI--------------YLS 439
Cdd:pfam15921 245 DQ----LEALKSESQNkiellLQQHQDRIEQlisehevEITGLTEKASSARSQANSIQSQLEIiqeqarnqnsmymrQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 440 RHNTAVSQLtkaKEALIAASETLKERkaaIRDIEGKLPQTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLA 519
Cdd:pfam15921 321 DLESTVSQL---RSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 520 MNRSRGKVLdaiiQEKKSGR---IPGIYGRLGDLGAIDEKYDV---AISSCCHA---LDYIVVDSIDIAQECVNFLKRQN 590
Cdd:pfam15921 395 LEKEQNKRL----WDRDTGNsitIDHLRRELDDRNMEVQRLEAllkAMKSECQGqmeRQMAAIQGKNESLEKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 591 IGVATFIGLDKMAVWAKKMTeIQTPENTprLFDLVKVKDEKIRQAfyfalrdtlvadnldQATRVAYQKDRRWRVVTLQG 670
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMT-LESSERT--VSDLTASLQEKERAI---------------EATNAEITKLRSRVDLKLQE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 671 -QIIEQSGTM---TGGGSKVMKGRM-GSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNT 745
Cdd:pfam15921 533 lQHLKNEGDHlrnVQTECEALKLQMaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 746 LEKFTASIQRL---IEQEEYLNVQVKELEANVLATAPDKKKQK--LLEEnVSAFKTEYDAVAEkagkvEAEVKRlhntiv 820
Cdd:pfam15921 613 KDKKDAKIRELearVSDLELEKVKLVNAGSERLRAVKDIKQERdqLLNE-VKTSRNELNSLSE-----DYEVLK------ 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 821 eiNNHKLKAQQDKL--DKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAA 898
Cdd:pfam15921 681 --RNFRNKSEEMETttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 899 EVVK-------NTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISKIS 971
Cdd:pfam15921 759 NANKekhflkeEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
..
gi 767925443 972 LH 973
Cdd:pfam15921 839 LQ 840
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
18-476 |
5.87e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 18 QNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSmLFVFGYRAQKIRSKKLSvlihNSDEHKDIQSCT-VEVHFqkii 96
Cdd:PRK03918 9 KNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEA-ILVGLYWGHGSKPKGLK----KDDFTRIGGSGTeIELKF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 97 DKEGDDYEVIPNSNFYVSRTACRDNTSVYHiSGKKKTFKDVGNLLRSHgidLDHNRFLILQGEVEQIammkpkgqTEHDE 176
Cdd:PRK03918 78 EKNGRKYRIVRSFNRGESYLKYLDGSEVLE-EGDSSVREWVERLIPYH---VFLNAIYIRQGEIDAI--------LESDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 177 GMLEYLEDIIGCGRLnepikvlcrrveilnEHRGEKLNRV-KMVEKEKDALEgekniaiEFLTLENEIfrkknhvcqyyi 255
Cdd:PRK03918 146 SREKVVRQILGLDDY---------------ENAYKNLGEViKEIKRRIERLE-------KFIKRTENI------------ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 256 yelQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDtekklnkitkfIEENKEKFTQLDLEDVQVREKLKHA 335
Cdd:PRK03918 192 ---EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-----------LEELKEEIEELEKELESLEGSKRKL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 336 TSKAKKLEKQLQKDKEKVEEFKSIPAKSNNI--INETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQK------EKE 407
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEErikeleEKE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 408 SR-----------EKELMGFSKSV---NEARSKMDVAQ---SELDIY-LSRHNTAVSQLTKAKEALIAASETLKERKAAI 469
Cdd:PRK03918 338 ERleelkkklkelEKRLEELEERHelyEEAKAKKEELErlkKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
....*..
gi 767925443 470 RDIEGKL 476
Cdd:PRK03918 418 KKEIKEL 424
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
713-950 |
7.87e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 713 NDSKKAMQIQEQKVQLEERVvklrhseREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLatapdKKKQKLLEENVS 792
Cdd:COG4913 238 ERAHEALEDAREQIELLEPI-------RELAERYAAARERLAELEYLRAALRLWFAQRRLELL-----EAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 793 AFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRT 872
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767925443 873 EKEIKDTekeVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALqKDALSIKLKLEQID 950
Cdd:COG4913 386 RAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAEALGLDEAE 459
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
701-961 |
8.19e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 701 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA-------- 772
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNtresletq 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 773 --------NVLATAPDKKKQKL----------------LEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLK 828
Cdd:TIGR04523 470 lkvlsrsiNKIKQNLEQKQKELkskekelkklneekkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 829 AQQD-KLDKINKQLDECASAITKaqvaIKTADRNLQKAQDSVlrtEKEIKDTEKEVDDLTAELKSLEDKAAEVvkntnaa 907
Cdd:TIGR04523 550 DDFElKKENLEKEIDEKNKEIEE----LKQTQKSLKKKQEEK---QELIDQKEKEKKDLIKEIEEKEKKISSL------- 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767925443 908 EESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIK 961
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
697-917 |
8.59e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 697 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQvkeLEANVLA 776
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL---LGSESFS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 777 TAPDkkkqklleeNVSAFKTEYDAVAEKAGKVEAEVKrlhntiveinnhKLKAQQDKLDkinKQLDECASAITKAQVAIK 856
Cdd:COG3883 116 DFLD---------RLSALSKIADADADLLEELKADKA------------ELEAKKAELE---AKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925443 857 TADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKE 917
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
721-1076 |
1.34e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 721 IQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATapdkkkqkllEENVSAFKTEYDA 800
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA----------REAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 801 VAEKagkVEAEVKRLHNTIVEinnhkLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDsvLRTE------- 873
Cdd:PRK02224 389 LEEE---IEELRERFGDAPVD-----LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA--LLEAgkcpecg 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 874 ---------KEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAE-----ESLPEIQKEHRNLLQELkvIQENEHALQKDA 939
Cdd:PRK02224 459 qpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaEDRIERLEERREDLEEL--IAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 940 lsikLKLEQIDGHIAEHNSKIKYWHKEISKisLHPIEDNPIEEISVLS------PEDLEAIKNPDSITNQIALLEARCHE 1013
Cdd:PRK02224 537 ----ERAEELRERAAELEAEAEEKREAAAE--AEEEAEEAREEVAELNsklaelKERIESLERIRTLLAAIADAEDEIER 610
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925443 1014 MKPNLGAIAEYKKKEELYLQ----RVAELDKiTYERDSFRQAYEDlrKQRLNEFMAGfyiITNKLKE 1076
Cdd:PRK02224 611 LREKREALAELNDERRERLAekreRKRELEA-EFDEARIEEARED--KERAEEYLEQ---VEEKLDE 671
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1119-1195 |
1.84e-05 |
|
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: 46.82 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1119 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTK---NAQFIIISLRNNMFEISDRLIGIYK 1195
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKkqpGRQFIFITPQDISGLASSDDVKVFR 189
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
844-938 |
1.87e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 844 CASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQ 923
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|....*
gi 767925443 924 ELKVIQENEHALQKD 938
Cdd:COG4942 91 EIAELRAELEAQKEE 105
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
12-98 |
1.98e-05 |
|
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: 48.46 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 12 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRaqkiRSKKLSVL-IHNSDEHKDIqSCTVEV 90
Cdd:COG3593 3 LEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPS----SSRKFDEEdFYLGDDPDLP-EIEIEL 75
|
....*...
gi 767925443 91 HFQKIIDK 98
Cdd:COG3593 76 TFGSLLSR 83
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
754-936 |
2.13e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.98 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 754 QRLIEQEEYLNVQVKEL---EANVLATAPDKKKQKLLEEnVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKL-KA 829
Cdd:pfam07111 59 QALSQQAELISRQLQELrrlEEEVRLLRETSLQQKMRLE-AQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLeEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 830 QQDKLDKINKQLDECASAITKAQ----VAIKTADRNLQKAQDSvLRTE-----KEIKDTEKEVDDLTAEL-KSLEDKAAE 899
Cdd:pfam07111 138 SQRELEEIQRLHQEQLSSLTQAHeealSSLTSKAEGLEKSLNS-LETKrageaKQLAEAQKEAELLRKQLsKTQEELEAQ 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767925443 900 VVKNTN----AAEESLPEIQK-----EHRNLLQELKVIQENEHALQ 936
Cdd:pfam07111 217 VTLVESlrkyVGEQVPPEVHSqtwelERQELLDTMQHLQEDRADLQ 262
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
720-898 |
2.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 720 QIQEQKVQLEERVVKLRHSeREMRNTLEKFTASIQRLIEQEEYLNVQVKELEAnVLATAPDKKKQKLLEENVSAFKTEYD 799
Cdd:COG4717 72 ELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 800 avaekagKVEAEVKRLHNTIVEInnhklKAQQDKLDKINKQLDECASAIT-KAQVAIKTADRNLQKAQDSVLRTEKEIKD 878
Cdd:COG4717 150 -------ELEERLEELRELEEEL-----EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|
gi 767925443 879 TEKEVDDLTAELKSLEDKAA 898
Cdd:COG4717 218 AQEELEELEEELEQLENELE 237
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
697-970 |
3.09e-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: 48.48 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 697 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA--NV 774
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESqiND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 775 LATAPDKKKQ--KLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINN--HKLKAQQDKLDKINKQLDECASAITK 850
Cdd:TIGR04523 396 LESKIQNQEKlnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 851 aqvAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQE 930
Cdd:TIGR04523 476 ---SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767925443 931 NehalqkdalsikLKLEQIDGHIAEHNSKIKYWHKEISKI 970
Cdd:TIGR04523 553 E------------LKKENLEKEIDEKNKEIEELKQTQKSL 580
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
213-463 |
3.59e-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: 48.18 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 213 LNRVKMVEKEKDALEGEKNIAIEFL-TLENEIFRKKNHVC------QYYIYELQKRIAEMETQKEKIHE----------D 275
Cdd:pfam05483 421 LDEKKQFEKIAEELKGKEQELIFLLqAREKEIHDLEIQLTaiktseEHYLKEVEDLKTELEKEKLKNIEltahcdklllE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 276 TKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAK-KLEKQLQKDK---- 350
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARsiey 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 351 ---EKVEEFKSIPAKSNNIINETTTRNNAlekekekeekklkevMDSLKQETQGLQKEKESREKELMGFSKSVNEARSKM 427
Cdd:pfam05483 581 evlKKEKQMKILENKCNNLKKQIENKNKN---------------IEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
250 260 270
....*....|....*....|....*....|....*.
gi 767925443 428 DVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLK 463
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
189-476 |
4.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 189 GRLNEPIKVLCRRVEILNEHR---GEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNHVCQYYIYELQKRIAEM 265
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 266 ETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEK--------------------------KLNKITKFIEENKEKFT 319
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 320 QLDLEDVQVREKLKHAT--SKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQ 397
Cdd:PRK03918 477 KLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 398 ETQGLQKEKESREKEL---------MGFSkSVNEARSKMdvaqSELDIYLSRHNTAVS----------QLTKAKEALIAA 458
Cdd:PRK03918 557 KLAELEKKLDELEEELaellkeleeLGFE-SVEELEERL----KELEPFYNEYLELKDaekelereekELKKLEEELDKA 631
|
330
....*....|....*...
gi 767925443 459 SETLKERKAAIRDIEGKL 476
Cdd:PRK03918 632 FEELAETEKRLEELRKEL 649
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
757-924 |
4.86e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 757 IEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAgKVEAEVKRLHNTIVEinnhkLKAQQDKLDK 836
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS-WDEIDVASAEREIAE-----LEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 837 INKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVkNTNAAEESLPEIQK 916
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL-RALLEERFAAALGD 761
|
....*...
gi 767925443 917 EHRNLLQE 924
Cdd:COG4913 762 AVERELRE 769
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
259-476 |
5.13e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 259 QKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLdledvqvREKLKHATSK 338
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-------EAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 339 AKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKE---SREKELMG 415
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAelaALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925443 416 FSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKL 476
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
826-925 |
5.90e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 826 KLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEvvkntn 905
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE------ 94
|
90 100
....*....|....*....|
gi 767925443 906 aAEESLPEIQKEHRNLLQEL 925
Cdd:COG4942 95 -LRAELEAQKEELAELLRAL 113
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
770-948 |
8.04e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 770 LEANVLATAPDKKKQKllEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAIT 849
Cdd:COG3883 6 LAAPTPAFADPQIQAK--QKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 850 KAQVAIKTADRNLQKAQDSVLRTE--------------------------KEIKDTEKEVDDLTAELKSLEDKAAEVVKN 903
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLDvllgsesfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767925443 904 TNAAEESLPEIQK---EHRNLLQELKViQENEHALQKDALSIKLKLEQ 948
Cdd:COG3883 163 KAELEAAKAELEAqqaEQEALLAQLSA-EEAAAEAQLAELEAELAAAE 209
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
698-1120 |
8.47e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 698 EISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELeanvlat 777
Cdd:COG5022 929 LIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL------- 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 778 apdkkkqklleenvSAFKTEYDAVAEKagkvEAEVKRLHNTIVEINNH-KLKAQQDKLDKINKQLDECASAITKAQVAIK 856
Cdd:COG5022 1002 --------------AELSKQYGALQES----TKQLKELPVEVAELQSAsKIISSESTELSILKPLQKLKGLLLLENNQLQ 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 857 TADRNLQKAQDSVLRTEKEIKDTEK-EVDDLTAELKSLEDKAAEVVKNTN------AAEESLPEIQKEHRNLLQELKVIQ 929
Cdd:COG5022 1064 ARYKALKLRRENSLLDDKQLYQLEStENLLKTINVKDLEVTNRNLVKPANvlqfivAQMIKLNLLQEISKFLSQLVNTLE 1143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 930 ENEHALQKDalsiKLKLEQIDGHIAEHNSKIKYWHKEISKISlhPIEDNPIEEISVLSPEDLEAIKNP-DSITNQIALLE 1008
Cdd:COG5022 1144 PVFQKLSVL----QLELDGLFWEANLEALPSPPPFAALSEKR--LYQSALYDEKSKLSSSEVNDLKNElIALFSKIFSGW 1217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1009 ARCHEMKPNLGAIAEYKKKEELYlqrvaeldKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAE 1088
Cdd:COG5022 1218 PRGDKLKKLISEGWVPTEYSTSL--------KGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSL 1289
|
410 420 430
....*....|....*....|....*....|..
gi 767925443 1089 LELVDSLDpFSEGIMfsvRPPKKSWKKIFNLS 1120
Cdd:COG5022 1290 LQYINVGL-FNALRT---KASSLRWKSATEVN 1317
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
721-932 |
8.87e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 721 IQEQKVQLEERVVKLRHSEREMRNTLEKFtasiQRLIEQEEYLNvQVKELEanvlatapdKKKQKLLEENVSAFKTEYDA 800
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKE----SELIKLKELAE-QLKELE---------EKLKKYNLEELEKKAEEYEK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 801 VAEKAGKVEAEVKRLHNTIVEIN--NHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKD 878
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD 609
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767925443 879 TEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEhrnlLQELKVIQENE 932
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE----LEELEKKYSEE 659
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
706-961 |
9.52e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.39 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 706 KMESQLQNdskkamqIQEQKVQLEERVVKLRHSE-REMRNTLEKFTASIQRLIEQ--------EEYLNVQVKELEANVla 776
Cdd:pfam06160 150 ELEKQLAE-------IEEEFSQFEELTESGDYLEaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEELKEGY-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 777 tapdkkkQKLLEENvsaFKTEYDAVAEKAGKVEaevKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIK 856
Cdd:pfam06160 221 -------REMEEEG---YALEHLNVDKEIQQLE---EQLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 857 TADRNLQKAQDSVLRTEKEIKDTEKEVD-----------------DLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHR 919
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELErvqqsytlnenelervrGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELE 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767925443 920 NLLQELKVIQENE-------HALQKDALSIKLKLEQIDGHIAEHNSKIK 961
Cdd:pfam06160 368 EILEQLEEIEEEQeefkeslQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
257-470 |
9.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 257 ELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHAT 336
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 337 SKAKKLEKQlqkdkekveEFKSIPAKSNNIinETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKESREKELMGF 416
Cdd:COG4942 111 RALYRLGRQ---------PPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767925443 417 SKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIR 470
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
833-961 |
1.29e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 833 KLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEvvkntnaAEESLP 912
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-------YEEQLG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767925443 913 EI--QKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIK 961
Cdd:COG1579 84 NVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA 134
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
800-948 |
1.38e-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: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 800 AVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDT 879
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 880 EKEVDDLTAELKSL---------EDKAAEVVKNTNAAE-----ESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 945
Cdd:COG4942 96 RAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
...
gi 767925443 946 LEQ 948
Cdd:COG4942 176 LEA 178
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
700-917 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 700 SEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA--NVLAT 777
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKeiAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 778 APDKKKQKLLEENVSAFKT---EYDAVAEKAGKVEAEVKRLhntivEINNHKLKAQQDKLDKINKQLDECASAITKAQVA 854
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgrqPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767925443 855 IKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKE 917
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
865-1059 |
2.01e-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: 45.14 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 865 AQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKL 944
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 945 KLEQIDGHIAEHNSKIkYWHKEISKISLhpiednpieeisVLSPED-LEAIKNPDSITNQIALLEARCHEMKPNLGAIAE 1023
Cdd:COG4942 98 ELEAQKEELAELLRAL-YRLGRQPPLAL------------LLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 767925443 1024 ykKKEELYLQRvAELDKITYERDSFRQAYEDLRKQR 1059
Cdd:COG4942 165 --LRAELEAER-AELEALLAELEEERAALEALKAER 197
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
664-967 |
2.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 664 RVVTLQGQIiEQSGTMtggGSKVMKGRMGSSLV--------IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERvvKL 735
Cdd:COG4913 575 RAITRAGQV-KGNGTR---HEKDDRRRIRSRYVlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQER--RE 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 736 RHSEREMRNTLEKFTASIQRLIEQeeyLNVQVKELEAN--VLATApdKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVK 813
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAE---LEAELERLDASsdDLAAL--EEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 814 RLhntiveinnhklkaqQDKLDKINKQLDEcASAITKAQVAIKTADRNLQKAQDSVLRTEKEikDTEKEVDDLTAELKSL 893
Cdd:COG4913 724 QA---------------EEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELRE--NLEERIDALRARLNRA 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 894 EDKAAEV-----------VKNTNAAEESLPEIQKEHRNLlqelkvIQENEHALQKDALsiKLKLEQIDGHIAEHNSKIKY 962
Cdd:COG4913 786 EEELERAmrafnrewpaeTADLDADLESLPEYLALLDRL------EEDGLPEYEERFK--ELLNENSIEFVADLLSKLRR 857
|
....*
gi 767925443 963 WHKEI 967
Cdd:COG4913 858 AIREI 862
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
845-1052 |
2.13e-04 |
|
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: 45.40 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 845 ASAITKAQVAIKTADRNLQKAQDSVLRT-EKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRN--- 920
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEElQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVkkk 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 921 LLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIkywhkeiskislhpiednpIEEISVLspEDLEAIKNPDS- 999
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPL-------------------IEEYRAL--KEAKSNKEDESq 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767925443 1000 -ITNQIALLEARCHEMkpnlgaIAEYKKKEELYLQRVAELDKITyeRDSFRQAY 1052
Cdd:pfam05667 451 rKLEEIKELREKIKEV------AEEAKQKEELYKQLVAEYERLP--KDVSRSAY 496
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
255-413 |
2.90e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 255 IYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQL------------- 321
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 322 --------DLED-VQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVM 392
Cdd:COG3883 105 ldvllgseSFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180
....*....|....*....|.
gi 767925443 393 DSLKQETQGLQKEKESREKEL 413
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAEL 205
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
875-971 |
2.95e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 875 EIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA-EESLPEIQKEHRNL---LQELKVIQENEHALQKDALSIKLKLEQID 950
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELeeeLEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100
....*....|....*....|.
gi 767925443 951 GHIAEHNSKIKYWHKEISKIS 971
Cdd:COG0542 485 GKIPELEKELAELEEELAELA 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
697-907 |
2.97e-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: 44.75 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 697 IEISEEEVNKMESQLQndskkamQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIeQEEYLNVQVKELEANVLA 776
Cdd:COG4942 57 LAALERRIAALARRIR-------ALEQELAALEAELAELEKEIAELRAELEAQKEELAELL-RALYRLGRQPPLALLLSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 777 TAPDKkkqklLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKlKAQQDKLDKINKQLDECASAITKAQVAIK 856
Cdd:COG4942 129 EDFLD-----AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767925443 857 TADRNLQKAQdsvlrteKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA 907
Cdd:COG4942 203 RLEKELAELA-------AELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
12-53 |
3.06e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 44.38 E-value: 3.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767925443 12 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDS 53
Cdd:COG1195 2 LKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEA 41
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
697-952 |
3.33e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 697 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRliEQEEYLNVQVKELEANVLA 776
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR--EKERELVDCQRELEKLNKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 777 TAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRL----------HNTIVEI---NNHKLK--AQQDKLDKINKQL 841
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLatrleldgfeRGPFSERqikNFHTLVieRQEDEAKTAAQLC 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 842 DECAS-------AITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKntnaAEESLPEI 914
Cdd:TIGR00606 415 ADLQSkerlkqeQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK----AERELSKA 490
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767925443 915 QKEH--RNLLQELKVIQENEHALQKDALSIKLKLEQIDGH 952
Cdd:TIGR00606 491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
826-1032 |
4.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 826 KLKAQQDKLDKINKQLDE-CASAITKAQVAIKTAD---RNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLED--KAAE 899
Cdd:COG4717 50 RLEKEADELFKPQGRKPElNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 900 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHalqkdalsiklKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNp 979
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLSLATEEELQDL- 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767925443 980 IEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYL 1032
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
697-907 |
5.10e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.17 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 697 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLN-----VQVKELE 771
Cdd:pfam06008 42 IEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGendfaLPSSDLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 772 aNVLATApdkkkQKLLEE----NVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASA 847
Cdd:pfam06008 122 -RMLAEA-----QRMLGEirsrDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLREL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 848 ITKAQVAIKTADRNLQKAQdsvlRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA 907
Cdd:pfam06008 196 LREAAAKTRDANRLNLANQ----ANLREFQRKKEEVSEQKNQLEETLKTARDSLDAANLL 251
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
666-1041 |
6.41e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 666 VTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDS--KKAMQIQEQKV---QLEERVVKL--RHS 738
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEadKNAKAIEKNKElfeQYKKDVTELlnKYS 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 739 EREMRNTLEKFTASIQRLIEQeeylnvqVKELEANVLATApDKKKQKLLEENVSAFKTEYDAVA-EKAGK----VEAEVK 813
Cdd:TIGR01612 1532 ALAIKNKFAKTKKDSEIIIKE-------IKDAHKKFILEA-EKSEQKIKEIKKEKFRIEDDAAKnDKSNKaaidIQLSLE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 814 RLHNTIVEINNHKLKAQQ--DKLDKINKQLDECASAITKAQVAIKTADRN-LQKAQDSVLRTEKEIKDTEKEVDDLTAEL 890
Cdd:TIGR01612 1604 NFENKFLKISDIKKKINDclKETESIEKKISSFSIDSQDTELKENGDNLNsLQEFLESLKDQKKNIEDKKKELDELDSEI 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 891 KSLEDKAAEVVKNTN-AAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKlKLEQIDGH--IAEHNSKIKYWHKEI 967
Cdd:TIGR01612 1684 EKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTN-DLEGIDPNekLEEYNTEIGDIYEEF 1762
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925443 968 skISLHPIEDNPIEEISVlSPEDLEAIKNpDSITNQIALLEarchemkpnlgaIAEYKKKEELYLQRVA--ELDKI 1041
Cdd:TIGR01612 1763 --IELYNIIAGCLETVSK-EPITYDEIKN-TRINAQNEFLK------------IIEIEKKSKSYLDDIEakEFDRI 1822
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
32-166 |
8.22e-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: 42.57 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 32 FHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK--IRSKKLSVLIH----NSDEHKdiqsctvevHFQKIIDKEGDDYEV 105
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGGRASAdlIRSGAEKAVVEgvfdISDEEE---------AKALLLELGIEDDDD 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925443 106 IpnsnfYVSRTACRDNTSVYHISGK---KKTFKDVGNLL------RSHGIDLDHNRFL-ILQGEVEQIAMM 166
Cdd:cd03241 90 L-----IIRREISRKGRSRYFINGQsvtLKLLRELGSLLvdihgqHDHQNLLNPERQLdLLDGGLDDVEFL 155
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
18-186 |
1.02e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.71 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 18 QNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNS--DEHKDIQSCTVEVHFQKI 95
Cdd:pfam13476 4 ENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDirIGLEGKGKAYVEITFENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 96 IDKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDvgnllrSHGIDLDHNRFLILQGEvEQIAMMKPKGQTEHD 175
Cdd:pfam13476 82 DGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISE------LLKSDKIILPLLVFLGQ-EREEEFERKEKKERL 154
|
170
....*....|.
gi 767925443 176 EGMLEYLEDII 186
Cdd:pfam13476 155 EELEKALEEKE 165
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
622-967 |
1.14e-03 |
|
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: 43.17 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 622 FDLVKVKDEKIRQAFYFALR-DTLVADNLDQAtrvaYQK---DRRWRVVTLQGQIIEQSGTMTGggskvmkgrmgSSLVI 697
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKeDHEKIQHLEEE----YKKeinDKEKQVSLLLIQITEKENKMKD-----------LTFLL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 698 EISEEEVNKMESQLQNDSKKAMQIQEQK----VQLEERVVKLRHS---EREMRNTLEKFTASIQRLIEQEEYL------- 763
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSmstQKALEEDLQIATKTICQLTEEKEAQmeelnka 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 764 ----NVQVKELEANVLATAPD-KKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINN-HKLKAQQDKLDKI 837
Cdd:pfam05483 344 kaahSFVVTEFEATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 838 NKQLDECASAITKAQVAI----KTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPE 913
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 767925443 914 IQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEI 967
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
701-950 |
1.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 701 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATapd 780
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 781 KKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADR 860
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 861 NlQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDAL 940
Cdd:COG4372 215 E-LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250
....*....|
gi 767925443 941 SIKLKLEQID 950
Cdd:COG4372 294 ELKLLALLLN 303
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
759-939 |
1.41e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 759 QEEYLNVQVKELEANVLATapdKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKIN 838
Cdd:COG3883 17 QIQAKQKELSELQAELEAA---QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA-EIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 839 KQL----------------DECASAITKAQV--AIKTADRN-LQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAE 899
Cdd:COG3883 93 RALyrsggsvsyldvllgsESFSDFLDRLSAlsKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767925443 900 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDA 939
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
716-902 |
1.41e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 716 KKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANvlATAPDKKKQklleenvsaFK 795
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG--GVCPTCTQQ---------IS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 796 TEYDAVAEkagkveaevkrLHNTIVEINnHKLKAQQDKLDKINKQLDECASAITKA---QVAIKTADRNLQKAQDSVLRT 872
Cdd:PHA02562 296 EGPDRITK-----------IKDKLKELQ-HSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKAKKV 363
|
170 180 190
....*....|....*....|....*....|
gi 767925443 873 EKEIKDTEKEVDDLTAELKSLEDKAAEVVK 902
Cdd:PHA02562 364 KAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
697-932 |
1.48e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 697 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLA 776
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 777 TAPDkkkqklleenVSAFKTEYDAVAEKAGKVEAEVKRLHntiveinnhklkaqqDKLDKINKQLDECASAITKAQVAIK 856
Cdd:PRK02224 333 CRVA----------AQAHNEEAESLREDADDLEERAEELR---------------EEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767925443 857 TadrnlqkaqdsvlrTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLlqeLKVIQENE 932
Cdd:PRK02224 388 E--------------LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA---RERVEEAE 446
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
11-57 |
1.51e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.34 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 767925443 11 MITHIVNQNFKSYAGEKIL-----GPFHKRFSCIIGPNGSGKSNVIDSMLFV 57
Cdd:COG1106 1 MLISFSIENFRSFKDELTLsmvasGLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
255-369 |
1.64e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.86 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 255 IYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDV------KDTEKKLN--KITKFIEENKEKFTQLDLEDV 326
Cdd:pfam09728 112 LKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFekllktKELEVQLAeaKLQQATEEEEKKAQEKEVAKA 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767925443 327 -QVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINE 369
Cdd:pfam09728 192 rELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTT 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
257-517 |
1.74e-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: 42.70 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 257 ELQKRIAEMETQKEKIHEDTKEINE---KSNILSNE-----MKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQV 328
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQlksEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 329 REKLKHATSKAKKLEKQLQKDKEKVEEFKS-IPAKSNNIINETTTRNNALEKEKEKEEKKLKevmdsLKQETQGLQKEKE 407
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQINDLESKIQNQEKLNQQ-----KDEQIKKLQQEKE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 408 SREKELMGFSKSVNEARSKMdvaqSELDIYLSRHNTAVSQLTKAKEALiaaSETLKERKAAIRDIEGKLPQTEQELKEKE 487
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEI----KDLTNQDSVKELIIKNLDNTRESL---ETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
250 260 270
....*....|....*....|....*....|
gi 767925443 488 KELQKLTQEETNFKSLVHDLFQKVEEAKSS 517
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
11-82 |
1.75e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.91 E-value: 1.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767925443 11 MITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKD 82
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGD 73
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
207-355 |
1.78e-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: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 207 EHRGEKLN-RVKMVEKEKDALEGE-KNIAIEFLTLENEIFRKKNHVCQyyiyeLQKRIAEMETQKEKIHeDTKEINeksn 284
Cdd:COG1579 23 EHRLKELPaELAELEDELAALEARlEAAKTELEDLEKEIKRLELEIEE-----VEARIKKYEEQLGNVR-NNKEYE---- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767925443 285 ILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEE 355
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
700-1081 |
2.39e-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: 42.41 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 700 SEEEVNKMESQL-----QNDSKKAMQIQeQKVQLEERVVKLRHSEREMRNTLEKFTASIQR--LIEQEEYLNVQVKELEA 772
Cdd:pfam15921 290 ARSQANSIQSQLeiiqeQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 773 NVLATAPDKKKQKLLEEnvsAFKTEYDAVAEKAGKVEAEVKRLHNTIV------EINNHKLKAQqdKLDKINKQL-DECA 845
Cdd:pfam15921 369 SQESGNLDDQLQKLLAD---LHKREKELSLEKEQNKRLWDRDTGNSITidhlrrELDDRNMEVQ--RLEALLKAMkSECQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 846 SAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEEslpeiqKEhrnllqel 925
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE------KE-------- 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 926 KVIQENEHALQKDALSIKLKLEQIDgHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAI-----KNPDSI 1000
Cdd:pfam15921 510 RAIEATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgRTAGAM 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 1001 TNQIALLEARCHEMKPNLGAIAEYKKKEELYLQ----RVAELD----KITYERDSFRQAYEDLRKQR---LNEFMAGFYI 1069
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIReleaRVSDLElekvKLVNAGSERLRAVKDIKQERdqlLNEVKTSRNE 668
|
410
....*....|..
gi 767925443 1070 ItNKLKENYQML 1081
Cdd:pfam15921 669 L-NSLSEDYEVL 679
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
809-961 |
2.47e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 809 EAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTA 888
Cdd:COG3883 15 DPQIQAKQKELSELQA-ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 889 EL----------------KSLED--KAAEVVKNTNAAEESLPEIQKEHRNLLQELKV-IQENEHALQKDALSIKLKLEQI 949
Cdd:COG3883 94 ALyrsggsvsyldvllgsESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAeLEAKLAELEALKAELEAAKAEL 173
|
170
....*....|..
gi 767925443 950 DGHIAEHNSKIK 961
Cdd:COG3883 174 EAQQAEQEALLA 185
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
257-459 |
2.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 257 ELQKRIAEMETQKEKIHEDTKEINEksniLSNEMKAKNKDVKDTEKKLNKITKFIEenkekFTQLDLEDVQVREKLKHAT 336
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 337 SKAKKLEKQLQKDKEKVEEfksIPAKSNNIINETTTRNNALEKEKEKEEKKlkevMDSLKQETQGLQKEKESREKELMGF 416
Cdd:COG4717 146 ERLEELEERLEELRELEEE---LEELEAELAELQEELEELLEQLSLATEEE----LQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767925443 417 SKSVNEARSKMDVAQSELdiylsRHNTAVSQLTKAKEALIAAS 459
Cdd:COG4717 219 QEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIAA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
628-814 |
3.15e-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: 41.65 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 628 KDEKIRQafyfalrdtlvadNLDQATRVAYQKDRRWRvvtlqgQIIEQSGTMTGGGSKVMKGRMGSSLVIEisEEEVNKM 707
Cdd:pfam17380 390 KNERVRQ-------------ELEAARKVKILEEERQR------KIQQQKVEMEQIRAEQEEARQREVRRLE--EERAREM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 708 ESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNtlekftasiQRLIEQEEYLNVQvKELEANVLATAPDKKKQKLL 787
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD---------RKRAEEQRRKILE-KELEERKQAMIEEERKRKLL 518
|
170 180
....*....|....*....|....*..
gi 767925443 788 EENVSAFKTeydAVAEKAGKVEAEVKR 814
Cdd:pfam17380 519 EKEMEERQK---AIYEEERRREAEEER 542
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
826-898 |
4.04e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 4.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925443 826 KLKAQQDKLDKINKQLDECASAITKAQ-VAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAA 898
Cdd:TIGR04320 283 ALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
701-969 |
4.33e-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: 41.36 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 701 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKEleanvlatapd 780
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK----------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 781 kkkqklleenvsAFKTEYDAVAEKAGKVEAEVKRLhntiveinnhkLKAQQDKLDKINKQLDECASAITKAQVAIKTAdr 860
Cdd:pfam12128 672 ------------ALAERKDSANERLNSLEAQLKQL-----------DKKHQAWLEEQKEQKREARTEKQAYWQVVEGA-- 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 861 nlQKAQDSVLRTEKEikdteKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHA------ 934
Cdd:pfam12128 727 --LDAQLALLKAAIA-----ARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfd 799
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767925443 935 -------LQKDALSIKL-----KLEQIDGHIAEHNSKIKYWHKEISK 969
Cdd:pfam12128 800 wyqetwlQRRPRLATQLsnierAISELQQQLARLIADTKLRRAKLEM 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
781-1057 |
4.47e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 781 KKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNH--KLKAQQDKLDKINKQLDECASAITKAQVAIKTA 858
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSElpELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 859 DRNLQKAQDSVLRTEKEIKDTEKEVDDL---TAELKSLEDKAAE---VVKNTNAAEESLPEIQKEHRNLLQELKVIQEne 932
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELeekVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEE-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 933 haLQKDALSIKLKLEQIDGHIAE---HNSKIKYWHKEISKISLHPIEDNPIE-EISVLSPEDLEAI-----KNPDSITNQ 1003
Cdd:PRK03918 329 --RIKELEEKEERLEELKKKLKElekRLEELEERHELYEEAKAKKEELERLKkRLTGLTPEKLEKEleeleKAKEEIEEE 406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767925443 1004 IALLEARCHEMKPNLG----AIAEYKK----------------KEELYLQRVAELDKITYERDSFRQAYEDLRK 1057
Cdd:PRK03918 407 ISKITARIGELKKEIKelkkAIEELKKakgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
262-479 |
5.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 262 IAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEkftqlDLEDVQvrEKLKHATSKAKK 341
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA-----EIAEAE--AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 342 LEKQLQKDKEKVEEFKSIpAKSNNiINETTTRNNAlekeKEKEEKKLKEVMDSLKQETQGLQKEKESREKELmgfsKSVN 421
Cdd:COG3883 91 RARALYRSGGSVSYLDVL-LGSES-FSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKL----AELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767925443 422 EARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLPQT 479
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
710-902 |
5.45e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 710 QLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlatapDKKKQKLleE 789
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-----KKYEEQL--G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 790 NVSAFKtEYDAVaekagkveaevkrlhntiveinNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSV 869
Cdd:COG1579 84 NVRNNK-EYEAL----------------------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|...
gi 767925443 870 LRTEKEIkdtEKEVDDLTAELKSLEDKAAEVVK 902
Cdd:COG1579 141 EEKKAEL---DEELAELEAELEELEAEREELAA 170
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
698-941 |
5.64e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 698 EISEEEVNKMESQLQN-------DSKKAMQIQeQKVQLEERVVKLRHSereMRNTLEKFTASIQRLIEQEEYLNVQVKEL 770
Cdd:PRK04863 386 EAAEEEVDELKSQLADyqqaldvQQTRAIQYQ-QAVQALERAKQLCGL---PDLTADNAEDWLEEFQAKEQEATEELLSL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 771 EanvlatapdkkkQKLleeNVS-AFKTEYDAVAEKAGKVEAEVKRL--HNTIVEINNH--KLKAQQDKLDKINKQLDECA 845
Cdd:PRK04863 462 E------------QKL---SVAqAAHSQFEQAYQLVRKIAGEVSRSeaWDVARELLRRlrEQRHLAEQLQQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 846 SAITKAQVAIKTADRNLQKAQDSVLRTEkeikDTEKEVDDLTAELKSLEDKAAEVVkntnAAEESLPEIQKEHRNLLQEL 925
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDED----ELEQLQEELEARLESLSESVSEAR----ERRMALRQQLEQLQARIQRL 598
|
250
....*....|....*.
gi 767925443 926 KVIQENEHALQkDALS 941
Cdd:PRK04863 599 AARAPAWLAAQ-DALA 613
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
12-56 |
6.19e-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: 39.97 E-value: 6.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 767925443 12 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLF 56
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
36-68 |
6.32e-03 |
|
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: 40.07 E-value: 6.32e-03
10 20 30
....*....|....*....|....*....|...
gi 767925443 36 FSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSK 68
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLT 33
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
202-357 |
6.56e-03 |
|
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: 40.93 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 202 VEILNEHRgEKLNRVKM-VEKEKDALEGE-KNIAIEFLTL-----ENEIFRKKNHVcqyYIYELQKRIAEMETQK----E 270
Cdd:pfam01576 358 LEELTEQL-EQAKRNKAnLEKAKQALESEnAELQAELRTLqqakqDSEHKRKKLEG---QLQELQARLSESERQRaelaE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 271 KIHEDTKEINEKSNILsNEMKAKN----KDVKDTEKKLNKITKFI-EENKEKFT------QLDLEDVQVREKLKHATSKA 339
Cdd:pfam01576 434 KLSKLQSELESVSSLL-NEAEGKNiklsKDVSSLESQLQDTQELLqEETRQKLNlstrlrQLEDERNSLQEQLEEEEEAK 512
|
170
....*....|....*...
gi 767925443 340 KKLEKQLQKDKEKVEEFK 357
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMK 530
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
697-926 |
6.58e-03 |
|
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: 40.80 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 697 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEK---FTASIQRLIEQEEYLNVQVKELEAN 773
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqqFEEQLVELSTEVQSLIREIKDAKEQ 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 774 VLATAPDKKK-QKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLH-------NTIVEINNHKLKAQQDKLDKINKQLDECA 845
Cdd:TIGR00606 911 DSPLETFLEKdQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdieNKIQDGKDDYLKQKETELNTVNAQLEECE 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 846 SAITKAQVAIKTADRNL--QKAQDSVLRTEKEIKDTEKEVDDLTAELKSL-----EDKAAEVVKNTNAAEESLPEIQKEH 918
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVLQMKQEHQKLEENIDLIKRNH 1070
|
....*...
gi 767925443 919 RNLLQELK 926
Cdd:TIGR00606 1071 VLALGRQK 1078
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
701-1057 |
7.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 701 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSERE---MRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlAT 777
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELEELKEEIEELEKElesLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 778 APDKKKQKLLEENVSAFKTEYDA----VAEKAGKVEAEVKRLHNTIVEINN---------HKLKAQQDKLDKINK--QLD 842
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDelreIEKRLSRLEEEINGIEERIKELEEkeerleelkKKLKELEKRLEELEErhELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 843 ECASAITKAQVAIKT--ADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNA---AEESLP----E 913
Cdd:PRK03918 365 EEAKAKKEELERLKKrlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkAKGKCPvcgrE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 914 IQKEHR------------NLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHN--SKIKYWHKEISKISLHPIEDNP 979
Cdd:PRK03918 445 LTEEHRkelleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 980 IE-------------EISVLSpEDLEAIKnpdSITNQIALLEARCHEMKPNLGAIaeYKKKEELYLQRVAELDKITYERD 1046
Cdd:PRK03918 525 EEyeklkekliklkgEIKSLK-KELEKLE---ELKKKLAELEKKLDELEEELAEL--LKELEELGFESVEELEERLKELE 598
|
410
....*....|.
gi 767925443 1047 SFRQAYEDLRK 1057
Cdd:PRK03918 599 PFYNEYLELKD 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
740-937 |
8.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 740 REMRNTLEKFTASIQRL-IEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAeVKRLHNT 818
Cdd:COG4717 52 EKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 819 IVEIN--NHKLKAQQDKLDKINKQLDEcasaITKAQVAIKTADRNLQKAQDSVLRTEKEIK-DTEKEVDDLTAELKSLED 895
Cdd:COG4717 131 YQELEalEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767925443 896 KAAEvvkntnaAEESLPEIQKEHRNLLQELKVIQENEHALQK 937
Cdd:COG4717 207 RLAE-------LEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
12-94 |
8.62e-03 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain] Cd Length: 365 Bit Score: 40.03 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 12 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQkiRSKKLSVLIHNSDEHkdiqsCTVEVH 91
Cdd:TIGR00611 3 LSRLELTDFRNYDAVDL--ELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSH--RTSRDKPLIRFGAEA-----FVIEGR 73
|
...
gi 767925443 92 FQK 94
Cdd:TIGR00611 74 VSK 76
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
701-926 |
9.60e-03 |
|
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: 40.16 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 701 EEEVNKMESQLQNDSKKAMQiqeqkvQLEERVVKLRHSEReMRNTLEKftaSIQRLIEQEEYLNVQVKELEANVLATAPD 780
Cdd:pfam01576 337 EEETRSHEAQLQEMRQKHTQ------ALEELTEQLEQAKR-NKANLEK---AKQALESENAELQAELRTLQQAKQDSEHK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767925443 781 KKK--QKLLEENVSAFKTEY--DAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDkLDKINKQL---DECASAITKAQV 853
Cdd:pfam01576 407 RKKleGQLQELQARLSESERqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD-VSSLESQLqdtQELLQEETRQKL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767925443 854 AIKTADRNLQKAQDSV---LRTEKEIKDT-EKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELK 926
Cdd:pfam01576 486 NLSTRLRQLEDERNSLqeqLEEEEEAKRNvERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
|
| |
