|
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 ... |
83-1274 |
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: 607.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 83 MITHIVNQNFKSYAgEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK-IRSKKLSVLIHnSDEHKDIQSCTVE 161
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKsLRSERLSDLIH-SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 162 VHFqkiidKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 241
Cdd:pfam02463 79 ITF-----DNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 242 GQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNH 321
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 322 VCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVR 401
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 402 EKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKESR 481
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 482 EKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLPQTEQELKEKEKE 561
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 562 LQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDVAISSCCHALD 641
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 642 YIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFdlvkvkdekirqafyfalrdtlvadNL 721
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA-------------------------QL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 722 DQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLE 801
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 802 ERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVE 881
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 882 AEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAE 961
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 962 LKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISK 1041
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1042 ISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYLQRVAELDKITYERDSFR 1121
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1122 QAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSL 1201
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVAL 1088
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50658063 1202 ALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNITKS 1274
Cdd:pfam02463 1089 ALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
84-1265 |
5.40e-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: 407.53 E-value: 5.40e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 84 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGY-RAQKIRSKKLSVLIHNSDEHKDIQSCTVEV 162
Cdd:TIGR02169 2 IERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLsSSKAMRAERLSDLISNGKNGQSGNEAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 163 HFQKIIDKEGDDYEVIpnsnfyVSRTACRDN-TSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFlILQGEVEQIAMMKPK 241
Cdd:TIGR02169 81 TFKNDDGKFPDELEVV------RRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 242 GQTEhdegmleYLEDIIGCGRLNEPIKVLCRRVEILnehrGEKLNRVKMVEKEK----DALEGEKNIAIEFLTLENEIFr 317
Cdd:TIGR02169 154 ERRK-------IIDEIAGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKrqqlERLRREREKAERYQALLKEKR- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 318 kknhvcQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEEN--------KEK 389
Cdd:TIGR02169 222 ------EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 390 FTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKsnniINETTTRNNALEKEKEKEEKKLKEVMDSLKQ 469
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE----LEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 470 ETQGLQK-------EKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIR 542
Cdd:TIGR02169 372 ELEEVDKefaetrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 543 DIEGKLPQTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGrIPGIYGRLGDL 622
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS-IQGVHGTVAQL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 623 GAIDEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFDLVKVkD 701
Cdd:TIGR02169 531 GSVGERYATAIEVAAGNrLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-D 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 702 EKIRQAFYFALRDTLVADNLDQATRVAYQkdrrWRVVTLQGQIIEQSGTMTGGgSKVMKGRMGSSLVIEISEEEVNKMES 781
Cdd:TIGR02169 610 PKYEPAFKYVFGDTLVVEDIEAARRLMGK----YRMVTLEGELFEKSGAMTGG-SRAPRGGILFSRSEPAELQRLRERLE 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 782 QLQNDSKKAMQ-IQEQKVQLEERVVKLRHSEREMRnTLEKftaSIQRLIEQEEYLNVQVKELEANVlatapDKKKQKLle 860
Cdd:TIGR02169 685 GLKRELSSLQSeLRRIENRLDELSQELSDASRKIG-EIEK---EIEQLEQEEEKLKERLEELEEDL-----SSLEQEI-- 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 861 ENVSAFKTEYDAV----AEKAGKVEAEVKRL-----HNTIVEINNHkLKAQQDKLDKINKQLDECASAITKAQVAIKTAD 931
Cdd:TIGR02169 754 ENVKSELKELEARieelEEDLHKLEEALNDLearlsHSRIPEIQAE-LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 932 RNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHalqkda 1011
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE------ 906
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1012 lSIKLKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEiSVLSPEDLEAiknpdsitnQIALLEARCHEMKP-NL 1090
Cdd:TIGR02169 907 -ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQA---------ELQRVEEEIRALEPvNM 975
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1091 GAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTlGGDAELELVDSLDPF 1170
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELILENPDDPF 1054
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1171 SEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIIS 1250
Cdd:TIGR02169 1055 AGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVS 1134
|
1210
....*....|....*
gi 50658063 1251 LRNNMFEISDRLIGI 1265
Cdd:TIGR02169 1135 LRSPMIEYADRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-1265 |
2.24e-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: 344.35 E-value: 2.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 92 FKSYAgEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFqkiiD 169
Cdd:TIGR02168 10 FKSFA-DPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGeQSAKALRGGKMEDVIFNgSETRKPLSLAEVELVF----D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 170 KEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLL-------RSHGIdldhnrflILQGEVEQIAMMKPkg 242
Cdd:TIGR02168 85 NSDGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFldtglgkRSYSI--------IEQGKISEIIEAKP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 243 qtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILN--EHRGEKLNRV----KMVEKEKDALEGEKNIAIEFLTLENEIF 316
Cdd:TIGR02168 155 -----EERRAIFEEAAGISKYKE------RRKETERklERTRENLDRLedilNELERQLKSLERQAEKAERYKELKAELR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 317 RKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLE 396
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 397 DVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEkekeekklkevMDSLKQETQGLQK 476
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELES 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 477 EKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKErkAAIRDIEGKLPQTEQELK 556
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 557 EKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQE------------KKSGRIPGIYGRLGDLGA 624
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsegvkallKNQSGLSGILGVLSELIS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 625 IDEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPR----LFDLVKV 699
Cdd:TIGR02168 531 VDEGYEAAIEAALGGrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvAKDLVKF 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 700 kDEKIRQAFYFALRDTLVADNLDQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKM 779
Cdd:TIGR02168 611 -DPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 780 ESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlatapdkkkqkll 859
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL------------- 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 860 eENVSAFKTEYDAVAEKAGKVEAEVKRlhntiveinnhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQD 939
Cdd:TIGR02168 757 -TELEAEIEELEERLEEAEEELAEAEA-----------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 940 SVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLE 1019
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1020 QIDGHIAEHNSKIKYWHKEISKISLHPIE-----DNPIEEISVLSPEDLE-AIKNPDSITNQIALLEARCHEMKP----- 1088
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGlevriDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENkikel 984
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1089 ---NLGAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVD 1165
Cdd:TIGR02168 985 gpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTD 1064
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1166 SLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQ 1245
Cdd:TIGR02168 1065 PEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQ 1144
|
1210 1220
....*....|....*....|
gi 50658063 1246 FIIISLRNNMFEISDRLIGI 1265
Cdd:TIGR02168 1145 FIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
82-241 |
8.38e-68 |
|
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: 227.18 E-value: 8.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 82 LMITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVE 161
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHPNLDSCSVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 162 VHFQKIIDKEgddyevipnsnfyvsrtacrdntsvyhisgkkktfkdvgnLLRSHGIDLDHNRFLILQGEVEQIAMMkPK 241
Cdd:cd03274 81 VHFQEIIDKP----------------------------------------LLKSKGIDLDHNRFLILQGEVEQIAQM-PK 119
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
84-1265 |
9.46e-67 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 245.23 E-value: 9.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 84 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG---YRAqkIRSKKLSVLIHN-SDEHKDIQSCT 159
Cdd:COG1196 3 LKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGeqsAKS--LRGGKMEDVIFAgSSSRKPLGRAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 160 VEVHF---QKIIDkeGDDYEVIpnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLD-HNrfLILQGEVEQI 235
Cdd:COG1196 80 VSLTFdnsDGTLP--IDYDEVT------ITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPEsYS--IIGQGMIDRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 236 AMMKPkgqtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILNEHRG--EKLNRVK--MVEKEK--DALEGEKNIAIEFL 309
Cdd:COG1196 150 IEAKP-------EERRAIIEEAAGISKYKE------RKEEAERKLEAteENLERLEdiLGELERqlEPLERQAEKAERYR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 310 TLENEIFRKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEK 389
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 390 FTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLkevmDSLKQ 469
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL----LEAEA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 470 ETQGLQKEKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLP 549
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 550 QTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSS----LAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAI 625
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARllllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 626 DEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVwAKKMTEIQTPENTPRLFDLVKVkDEKI 704
Cdd:COG1196 533 EAAYEAALEAALAAaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA-RAALAAALARGAIGAAVDLVAS-DLRE 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 705 RQAFYFALRDTLV-----ADNLDQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKvmKGRMGSSLVIEISEEEVNKM 779
Cdd:COG1196 611 ADARYYVLGDTLLgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR--ELLAALLEAEAELEELAERL 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 780 ESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEkftasiQRLIEQEEYLNVQVKELEANVLATAPDkkkqkll 859
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE------QLEAEREELLEELLEEEELLEEEALEE------- 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 860 eenvsafkteydavaekagkveaevkrlhntiveinnhklkaqqdkldkinkqldecasaitkaqvaiktadrnlqkaqd 939
Cdd:COG1196 --------------------------------------------------------------------------------
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 940 svLRTEKEIKDTEKEVDDLTAELKSLEDkaaeVvkNTNAAEEsLPEIQKEHRNLLQELkviqenehalqkdalsiklkle 1019
Cdd:COG1196 756 --LPEPPDLEELERELERLEREIEALGP----V--NLLAIEE-YEELEERYDFLSEQR---------------------- 804
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1020 qidghiaehnskikywhkeiskislhpiednpieeisvlspEDLEaiknpdsitnqiallEARchemkpnlgaiaeykkk 1099
Cdd:COG1196 805 -----------------------------------------EDLE---------------EAR----------------- 811
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1100 EELyLQRVAELDKITYERdsFRQAYEDLRKQrlnefmagfyiitnkLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVR 1179
Cdd:COG1196 812 ETL-EEAIEEIDRETRER--FLETFDAVNEN---------------FQELFPRLFGGGEAELLLTDPDDPLETGIEIMAQ 873
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1180 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEIS 1259
Cdd:COG1196 874 PPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAA 953
|
....*.
gi 50658063 1260 DRLIGI 1265
Cdd:COG1196 954 DRLYGV 959
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1181-1275 |
1.25e-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: 221.02 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1181 PKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISD 1260
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAD 197
|
90
....*....|....*
gi 50658063 1261 RLIGIYKTYNITKSV 1275
Cdd:cd03274 198 RLVGIYKTNNCTKSV 212
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
613-727 |
1.36e-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: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 613 PGIYGRLGDLGAIDEKYDVAISSCCHA-LDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAV-----WAKKMTEIQT 686
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGrLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPrspagSKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 50658063 687 PENTPRLFDLVKVkDEKIRQAFYFALRDTLVADNLDQATRV 727
Cdd:smart00968 81 PGFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1191-1273 |
1.81e-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: 124.73 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1191 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKN-AQFIIISLRNNMFEISDRLIGIYKTY 1269
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 50658063 1270 NITK 1273
Cdd:cd03239 175 GVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
90-242 |
2.12e-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: 123.84 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 90 QNFKSYAGEKILGPFhKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFQkii 168
Cdd:cd03275 7 ENFKSYKGRHVIGPF-DRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRaRVGKPDSNSAYVTAVYE--- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50658063 169 dkegDDYEVIPnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKG 242
Cdd:cd03275 83 ----DDDGEEK-----TFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPPG 147
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1180-1267 |
1.33e-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: 118.83 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1180 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEI 1258
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEFFSK 224
|
....*....
gi 50658063 1259 SDRLIGIYK 1267
Cdd:cd03275 225 ADALVGVYR 233
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
612-728 |
9.07e-29 |
|
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: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 612 IPGIYGRLGDLGAIDEKYDVAISSCC-HALDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTpENT 690
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALgGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLK-GGA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 50658063 691 PRLFDLVKVKDEkIRQAFYFALRDTLVADNLDQATRVA 728
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 ... |
1186-1265 |
1.13e-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: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1186 KKIFN---LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRL 1262
Cdd:cd03278 106 KKVQRlslLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
...
gi 50658063 1263 IGI 1265
Cdd:cd03278 186 YGV 188
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
84-167 |
1.97e-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: 110.09 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 84 ITHIVNQNFKSYAGEKILGPFHkRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHnSDEHKDIQSCTVEVH 163
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSN-SFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAG-GGVKAGINSASVEIT 78
|
....
gi 50658063 164 FQKI 167
Cdd:cd03239 79 FDKS 82
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1188-1268 |
1.14e-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: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1188 IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEISDRLIGIY 1266
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIK 154
|
..
gi 50658063 1267 KT 1268
Cdd:cd03227 155 KV 156
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1185-1271 |
7.01e-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: 81.96 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1185 WKK-IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLi 1263
Cdd:cd03273 160 WKEsLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVL- 238
|
....*...
gi 50658063 1264 giYKTYNI 1271
Cdd:cd03273 239 --FRTRFV 244
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1186-1265 |
1.02e-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: 81.15 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1186 KKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1265
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 ... |
84-164 |
2.82e-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: 78.66 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 84 ITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHNSDEHKDIQS-CTVE 161
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGeQSAKSLRGEKMSDVIFAGSETRKPANfAEVT 79
|
...
gi 50658063 162 VHF 164
Cdd:cd03278 80 LTF 82
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
84-238 |
1.41e-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: 78.11 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 84 ITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRA-QKIRSKKLSVLIHNSDEhKDIQSCTVEV 162
Cdd:cd03273 3 IKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKRGQ-AGITKASVTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 163 HFqKIIDKEG-----DDYEVIPnsnfyVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAM 237
Cdd:cd03273 82 VF-DNSDKSQspigfENYPEIT-----VTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLN 155
|
.
gi 50658063 238 M 238
Cdd:cd03273 156 M 156
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
86-170 |
8.11e-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: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 86 HIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKklsvlihnSDEHKDIQSCTVEVHFQ 165
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRR--------SGVKAGCIVAAVSAELI 72
|
....*
gi 50658063 166 KIIDK 170
Cdd:cd03227 73 FTRLQ 77
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
84-245 |
7.44e-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: 69.60 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 84 ITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIqSCTVEVH 163
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVM-SAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 164 FQKIidkegDDYEVIPNSNFYVSRT--ACRDNtsvYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 241
Cdd:cd03272 80 FDNS-----DNRFPIDKEEVRLRRTigLKKDE---YFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQD 151
|
....
gi 50658063 242 GQTE 245
Cdd:cd03272 152 EQQE 155
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1188-1267 |
2.46e-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: 54.56 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1188 IFNLSGGEKTLSSLALVFALhhyKPtPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFE-ISDRLIGI 1265
Cdd:cd00267 78 VPQLSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVL 153
|
..
gi 50658063 1266 YK 1267
Cdd:cd00267 154 KD 155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
852-1032 |
2.66e-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: 56.09 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 852 DKKKQKLLEEnVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKtad 931
Cdd:COG1579 2 MPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 932 rNLQKAQDSVlRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQEnehALQKDA 1011
Cdd:COG1579 77 -KYEEQLGNV-RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEEL 151
|
170 180
....*....|....*....|.
gi 50658063 1012 LSIKLKLEQIDGHIAEHNSKI 1032
Cdd:COG1579 152 AELEAELEELEAEREELAAKI 172
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
766-1133 |
5.05e-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: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 766 SLVIEISEEEVNKMESQLQNDSKKAMQiQEQKVQLEERVVKLRHSEREMRN--TLEKFTA--SIQRLIEQEEYLNVQVKE 841
Cdd:pfam12128 255 SAELRLSHLHFGYKSDETLIASRQEER-QETSAELNQLLRTLDDQWKEKRDelNGELSAAdaAVAKDRSELEALEDQHGA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 842 -LEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKI----------- 909
Cdd:pfam12128 334 fLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIreardrqlava 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 910 -----------NKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVD-------DLTAELKSLEDKAAE 971
Cdd:pfam12128 414 eddlqaleselREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDErierareEQEAANAEVERLQSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 972 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIklkleqidghIAEHNSKIKYWHKEISKI--------- 1042
Cdd:pfam12128 494 LRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL----------LHFLRKEAPDWEQSIGKVispellhrt 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1043 SLHPI--EDNPIEEISVLSPE-DLEAIKNPDSITNQIAlLEARCHEMKPNLGAIAE-YKKKEELYLQRVAELDKITYERD 1118
Cdd:pfam12128 564 DLDPEvwDGSVGGELNLYGVKlDLKRIDVPEWAASEEE-LRERLDKAEEALQSAREkQAAAEEQLVQANGELEKASREET 642
|
410
....*....|....*..
gi 50658063 1119 SFRQAYE--DLRKQRLN 1133
Cdd:pfam12128 643 FARTALKnaRLDLRRLF 659
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
83-178 |
6.31e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 54.25 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 83 MITHIVNQNFKSYAGEKILgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKiRSKKLSVLIHNSDEhkdiqSCTVEV 162
Cdd:COG0419 1 KLLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSE-----EASVEL 73
|
90
....*....|....*.
gi 50658063 163 HFQkiidKEGDDYEVI 178
Cdd:COG0419 74 EFE----HGGKRYRIE 85
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
83-129 |
6.56e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.48 E-value: 6.56e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 50658063 83 MITHIVNQNFKSYAGEKI-LGPFHkrfsCIIGPNGSGKSNVIDSMLFV 129
Cdd:COG4637 1 MITRIRIKNFKSLRDLELpLGPLT----VLIGANGSGKSNLLDALRFL 44
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
781-1027 |
1.95e-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: 55.52 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 781 SQLQNDSK-KAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKE-LEANVLATAPDKKKQKL 858
Cdd:pfam05557 12 SQLQNEKKqMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREqAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 859 LEENVSAFKTEYDAVAEKAGKVeAEVKRlhntIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKtadrNLQKAQ 938
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNEL-SELRR----QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 939 DSVLRTEKEIKDTEKEVddltaelkSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQE---LKVIQENEHALQKDALSIK 1015
Cdd:pfam05557 163 SSLAEAEQRIKELEFEI--------QSQEQDSEIVKNSKSELARIPELEKELERLREHnkhLNENIENKLLLKEEVEDLK 234
|
250
....*....|..
gi 50658063 1016 LKLEQIDGHIAE 1027
Cdd:pfam05557 235 RKLEREEKYREE 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
773-1207 |
2.66e-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: 55.36 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 773 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKL---RHSEREMRNTLEKFTASIQRLIEQEEYLNVQVK-ELEANVLA 848
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAcEQHALLRK 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 849 TAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRlhntivEINNHKLKAQQDKLDKINKQLdecaSAITKAQVAIK 928
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE------RVREHALSIRVLPKELLASRQ----LALQKMQSEKE 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 929 --TADRNLQKAQDSVLRTEKE-IKDTEKEVDDLTAELKSLEdkaAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEH 1005
Cdd:TIGR00618 691 qlTYWKEMLAQCQTLLRELEThIEEYDREFNEIENASSSLG---SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1006 ALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEIsKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHE 1085
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL-KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1086 MKPNLGAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVD 1165
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVN 926
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 50658063 1166 SLDPFSEGIMF------SVRPPKkswkkifNLSGGEKTLSSLALVFAL 1207
Cdd:TIGR00618 927 ARKYQGLALLVadaytgSVRPSA-------TLSGGETFLASLSLALAL 967
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
799-1028 |
4.82e-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: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 799 QLEERVVKLRhserEMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATApdKKKQKLLEENVSAFKTEYDAVAEKAG 878
Cdd:COG4913 239 RAHEALEDAR----EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 879 KVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDEcasaitkAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDL 958
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLEREIER-------LERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 959 TAELKSLEDKAAEVVKntnAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEH 1028
Cdd:COG4913 386 RAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
858-1081 |
1.30e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 858 LLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKA 937
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE-ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 938 QDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 1017
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50658063 1018 -LEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEA 1081
Cdd:COG4372 187 eLLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
773-984 |
1.45e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 773 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELE---ANVLAT 849
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 850 APDKKKQKLLEENVSAfktEYDAVAEKAGKVEAEVKRLHNTIVEinnhKLKAQQDKLDKINKQLDECASAITKAQVAIKT 929
Cdd:COG4942 113 LYRLGRQPPLALLLSP---EDFLDAVRRLQYLKYLAPARREQAE----ELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 50658063 930 ADRNLQKAQDS----VLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLP 984
Cdd:COG4942 186 ERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
773-1033 |
1.68e-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: 52.72 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 773 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA-------- 844
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNtresletq 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 845 --------NVLATAPDKKKQKL----------------LEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLK 900
Cdd:TIGR04523 470 lkvlsrsiNKIKQNLEQKQKELkskekelkklneekkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 901 AQQD-KLDKINKQLDECASAITKaqvaIKTADRNLQKAQDSVlrtEKEIKDTEKEVDDLTAELKSLEDKAAEVvkntnaa 979
Cdd:TIGR04523 550 DDFElKKENLEKEIDEKNKEIEE----LKQTQKSLKKKQEEK---QELIDQKEKEKKDLIKEIEEKEKKISSL------- 615
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 50658063 980 EESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIK 1033
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
90-548 |
2.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 90 QNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSmLFVFGYRAQKIRSKKLSvlihNSDEHKDIQSCT-VEVHFqkii 168
Cdd:PRK03918 9 KNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEA-ILVGLYWGHGSKPKGLK----KDDFTRIGGSGTeIELKF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 169 DKEGDDYEVIPNSNFYVSRTACRDNTSVYHiSGKKKTFKDVGNLLRSHgidLDHNRFLILQGEVEQIammkpkgqTEHDE 248
Cdd:PRK03918 78 EKNGRKYRIVRSFNRGESYLKYLDGSEVLE-EGDSSVREWVERLIPYH---VFLNAIYIRQGEIDAI--------LESDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 249 GMLEYLEDIIGCGRLnepikvlcrrveilnEHRGEKLNRV-KMVEKEKDALEgekniaiEFLTLENEIfrkknhvcqyyi 327
Cdd:PRK03918 146 SREKVVRQILGLDDY---------------ENAYKNLGEViKEIKRRIERLE-------KFIKRTENI------------ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 328 yelQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDtekklnkitkfIEENKEKFTQLDLEDVQVREKLKHA 407
Cdd:PRK03918 192 ---EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-----------LEELKEEIEELEKELESLEGSKRKL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 408 TSKAKKLEKQLQKDKEKVEEFKSIPAKSNNI--INETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQK------EKE 479
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEErikeleEKE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 480 SR-----------EKELMGFSKSV---NEARSKMDVAQ---SELDIY-LSRHNTAVSQLTKAKEALIAASETLKERKAAI 541
Cdd:PRK03918 338 ERleelkkklkelEKRLEELEERHelyEEAKAKKEELErlkKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
....*..
gi 50658063 542 RDIEGKL 548
Cdd:PRK03918 418 KKEIKEL 424
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
309-1045 |
4.92e-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: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 309 LTLENEIFRKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMK-----------AKNKDVKDTEKKLN 377
Cdd:pfam15921 94 LNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvheleaakcLKEDMLEDSNTQIE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 378 KITKFIEENKEKFTQLDLEDVQVREklkhatSKAKKLEKQlqkDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEE 457
Cdd:pfam15921 174 QLRKMMLSHEGVLQEIRSILVDFEE------ASGKKIYEH---DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 458 KKlkevMDSLKQETQG-----LQKEKESREK-------ELMGFSKSVNEARSKMDVAQSELDI--------------YLS 511
Cdd:pfam15921 245 DQ----LEALKSESQNkiellLQQHQDRIEQlisehevEITGLTEKASSARSQANSIQSQLEIiqeqarnqnsmymrQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 512 RHNTAVSQLtkaKEALIAASETLKERkaaIRDIEGKLPQTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLA 591
Cdd:pfam15921 321 DLESTVSQL---RSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 592 MNRSRGKVLdaiiQEKKSGR---IPGIYGRLGDLGAIDEKYDV---AISSCCHA---LDYIVVDSIDIAQECVNFLKRQN 662
Cdd:pfam15921 395 LEKEQNKRL----WDRDTGNsitIDHLRRELDDRNMEVQRLEAllkAMKSECQGqmeRQMAAIQGKNESLEKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 663 IGVATFIGLDKMAVWAKKMTeIQTPENTprLFDLVKVKDEKIRQAfyfalrdtlvadnldQATRVAYQKDRRWRVVTLQG 742
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMT-LESSERT--VSDLTASLQEKERAI---------------EATNAEITKLRSRVDLKLQE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 743 -QIIEQSGTM---TGGGSKVMKGRM-GSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNT 817
Cdd:pfam15921 533 lQHLKNEGDHlrnVQTECEALKLQMaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 818 LEKFTASIQRL---IEQEEYLNVQVKELEANVLATAPDKKKQK--LLEEnVSAFKTEYDAVAEkagkvEAEVKRlhntiv 892
Cdd:pfam15921 613 KDKKDAKIRELearVSDLELEKVKLVNAGSERLRAVKDIKQERdqLLNE-VKTSRNELNSLSE-----DYEVLK------ 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 893 eiNNHKLKAQQDKL--DKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAA 970
Cdd:pfam15921 681 --RNFRNKSEEMETttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 971 EVVK-------NTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISKIS 1043
Cdd:pfam15921 759 NANKekhflkeEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
..
gi 50658063 1044 LH 1045
Cdd:pfam15921 839 LQ 840
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
785-1022 |
8.65e-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: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 785 NDSKKAMQIQEQKVQLEERVvklrhseREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLatapdKKKQKLLEENVS 864
Cdd:COG4913 238 ERAHEALEDAREQIELLEPI-------RELAERYAAARERLAELEYLRAALRLWFAQRRLELL-----EAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 865 AFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRT 944
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50658063 945 EKEIKDTekeVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALqKDALSIKLKLEQID 1022
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 ... |
769-1042 |
8.69e-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: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 769 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA--NV 846
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESqiND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 847 LATAPDKKKQ--KLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINN--HKLKAQQDKLDKINKQLDECASAITK 922
Cdd:TIGR04523 396 LESKIQNQEKlnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdSVKELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 923 aqvAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQE 1002
Cdd:TIGR04523 476 ---SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 50658063 1003 NehalqkdalsikLKLEQIDGHIAEHNSKIKYWHKEISKI 1042
Cdd:TIGR04523 553 E------------LKKENLEKEIDEKNKEIEELKQTQKSL 580
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
769-989 |
1.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 769 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQvkeLEANVLA 848
Cdd:COG3883 39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL---LGSESFS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 849 TAPDkkkqklleeNVSAFKTEYDAVAEKAGKVEAEVKrlhntiveinnhKLKAQQDKLDkinKQLDECASAITKAQVAIK 928
Cdd:COG3883 116 DFLD---------RLSALSKIADADADLLEELKADKA------------ELEAKKAELE---AKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50658063 929 TADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKE 989
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
84-170 |
1.44e-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: 48.85 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 84 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRaqkiRSKKLSVL-IHNSDEHKDIqSCTVEV 162
Cdd:COG3593 3 LEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPS----SSRKFDEEdFYLGDDPDLP-EIEIEL 75
|
....*...
gi 50658063 163 HFQKIIDK 170
Cdd:COG3593 76 TFGSLLSR 83
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1191-1267 |
1.76e-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: 47.21 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1191 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTK---NAQFIIISLRNNMFEISDRLIGIYK 1267
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKkqpGRQFIFITPQDISGLASSDDVKVFR 189
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
916-1010 |
1.82e-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: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 916 CASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQ 995
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|....*
gi 50658063 996 ELKVIQENEHALQKD 1010
Cdd:COG4942 91 EIAELRAELEAQKEE 105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
792-970 |
1.89e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 792 QIQEQKVQLEERVVKLRHSeREMRNTLEKFTASIQRLIEQEEYLNVQVKELEAnVLATAPDKKKQKLLEENVSAFKTEYD 871
Cdd:COG4717 72 ELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 872 avaekagKVEAEVKRLHNTIVEInnhklKAQQDKLDKINKQLDECASAIT-KAQVAIKTADRNLQKAQDSVLRTEKEIKD 950
Cdd:COG4717 150 -------ELEERLEELRELEEEL-----EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|
gi 50658063 951 TEKEVDDLTAELKSLEDKAA 970
Cdd:COG4717 218 AQEELEELEEELEQLENELE 237
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
773-1148 |
2.15e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 773 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKEL--EANVLATA 850
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELreEAAELESE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 851 pdkkkqklLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEinnhkLKAQQDKLDKINKQLDECASAITKAQVAIKTA 930
Cdd:PRK02224 372 --------LEEAREAVEDRREEIEELEEEIEELRERFGDAPVD-----LGNAEDFLEELREERDELREREAELEATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 931 DRNLQKAQDsvLRTE----------------KEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAE-----ESLPEIQKE 989
Cdd:PRK02224 439 RERVEEAEA--LLEAgkcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaEDRIERLEE 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 990 HRNLLQELkvIQENEHALQKDAlsikLKLEQIDGHIAEHNSKIKYWHKEISKisLHPIEDNPIEEISVLS------PEDL 1063
Cdd:PRK02224 517 RREDLEEL--IAERRETIEEKR----ERAEELRERAAELEAEAEEKREAAAE--AEEEAEEAREEVAELNsklaelKERI 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1064 EAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYLQ----RVAELDKiTYERDSFRQAYEDlrKQRLNEFMAGf 1139
Cdd:PRK02224 589 ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekreRKRELEA-EFDEARIEEARED--KERAEEYLEQ- 664
|
....*....
gi 50658063 1140 yiITNKLKE 1148
Cdd:PRK02224 665 --VEEKLDE 671
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
285-535 |
2.30e-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: 48.95 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 285 LNRVKMVEKEKDALEGEKNIAIEFL-TLENEIFRKKNHVC------QYYIYELQKRIAEMETQKEKIHE----------D 347
Cdd:pfam05483 421 LDEKKQFEKIAEELKGKEQELIFLLqAREKEIHDLEIQLTaiktseEHYLKEVEDLKTELEKEKLKNIEltahcdklllE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 348 TKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAK-KLEKQLQKDK---- 422
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARsiey 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 423 ---EKVEEFKSIPAKSNNIINETTTRNNAlekekekeekklkevMDSLKQETQGLQKEKESREKELMGFSKSVNEARSKM 499
Cdd:pfam05483 581 evlKKEKQMKILENKCNNLKKQIENKNKN---------------IEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
250 260 270
....*....|....*....|....*....|....*.
gi 50658063 500 DVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLK 535
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-548 |
2.59e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 261 GRLNEPIKVLCRRVEILNEHR---GEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNHVCQYYIYELQKRIAEM 337
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 338 ETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEK--------------------------KLNKITKFIEENKEKFT 391
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 392 QLDLEDVQVREKLKHAT--SKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQ 469
Cdd:PRK03918 477 KLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 470 ETQGLQKEKESREKEL---------MGFSkSVNEARSKMdvaqSELDIYLSRHNTAVS----------QLTKAKEALIAA 530
Cdd:PRK03918 557 KLAELEKKLDELEEELaellkeleeLGFE-SVEELEERL----KELEPFYNEYLELKDaekelereekELKKLEEELDKA 631
|
330
....*....|....*...
gi 50658063 531 SETLKERKAAIRDIEGKL 548
Cdd:PRK03918 632 FEELAETEKRLEELRKEL 649
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
826-1008 |
3.26e-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: 48.21 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 826 QRLIEQEEYLNVQVKEL---EANVLATAPDKKKQKLLEEnVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKL-KA 901
Cdd:pfam07111 59 QALSQQAELISRQLQELrrlEEEVRLLRETSLQQKMRLE-AQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLeEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 902 QQDKLDKINKQLDECASAITKAQ----VAIKTADRNLQKAQDSvLRTE-----KEIKDTEKEVDDLTAEL-KSLEDKAAE 971
Cdd:pfam07111 138 SQRELEEIQRLHQEQLSSLTQAHeealSSLTSKAEGLEKSLNS-LETKrageaKQLAEAQKEAELLRKQLsKTQEELEAQ 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50658063 972 VVKNTN----AAEESLPEIQK-----EHRNLLQELKVIQENEHALQ 1008
Cdd:pfam07111 217 VTLVESlrkyVGEQVPPEVHSqtwelERQELLDTMQHLQEDRADLQ 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-548 |
4.49e-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: 47.45 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 331 QKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLdledvqvREKLKHATSK 410
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-------EAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 411 AKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKE---SREKELMG 487
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAelaALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50658063 488 FSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKL 548
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
829-996 |
4.99e-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: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 829 IEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAgKVEAEVKRLHNTIVEinnhkLKAQQDKLDK 908
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS-WDEIDVASAEREIAE-----LEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 909 INKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVkNTNAAEESLPEIQK 988
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL-RALLEERFAAALGD 761
|
....*...
gi 50658063 989 EHRNLLQE 996
Cdd:COG4913 762 AVERELRE 769
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
770-1192 |
5.10e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 770 EISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELeanvlat 849
Cdd:COG5022 929 LIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL------- 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 850 apdkkkqklleenvSAFKTEYDAVAEKagkvEAEVKRLHNTIVEINNH-KLKAQQDKLDKINKQLDECASAITKAQVAIK 928
Cdd:COG5022 1002 --------------AELSKQYGALQES----TKQLKELPVEVAELQSAsKIISSESTELSILKPLQKLKGLLLLENNQLQ 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 929 TADRNLQKAQDSVLRTEKEIKDTEK-EVDDLTAELKSLEDKAAEVVKNTN------AAEESLPEIQKEHRNLLQELKVIQ 1001
Cdd:COG5022 1064 ARYKALKLRRENSLLDDKQLYQLEStENLLKTINVKDLEVTNRNLVKPANvlqfivAQMIKLNLLQEISKFLSQLVNTLE 1143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1002 ENEHALQKDalsiKLKLEQIDGHIAEHNSKIKYWHKEISKISlhPIEDNPIEEISVLSPEDLEAIKNP-DSITNQIALLE 1080
Cdd:COG5022 1144 PVFQKLSVL----QLELDGLFWEANLEALPSPPPFAALSEKR--LYQSALYDEKSKLSSSEVNDLKNElIALFSKIFSGW 1217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1081 ARCHEMKPNLGAIAEYKKKEELYlqrvaeldKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAE 1160
Cdd:COG5022 1218 PRGDKLKKLISEGWVPTEYSTSL--------KGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSL 1289
|
410 420 430
....*....|....*....|....*....|..
gi 50658063 1161 LELVDSLDpFSEGIMfsvRPPKKSWKKIFNLS 1192
Cdd:COG5022 1290 LQYINVGL-FNALRT---KASSLRWKSATEVN 1317
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
778-1033 |
5.31e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 778 KMESQLQNdskkamqIQEQKVQLEERVVKLRHSE-REMRNTLEKFTASIQRLIEQ--------EEYLNVQVKELEANVla 848
Cdd:pfam06160 150 ELEKQLAE-------IEEEFSQFEELTESGDYLEaREVLEKLEEETDALEELMEDipplyeelKTELPDQLEELKEGY-- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 849 tapdkkkQKLLEENvsaFKTEYDAVAEKAGKVEaevKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIK 928
Cdd:pfam06160 221 -------REMEEEG---YALEHLNVDKEIQQLE---EQLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKK 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 929 TADRNLQKAQDSVLRTEKEIKDTEKEVD-----------------DLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHR 991
Cdd:pfam06160 288 YVEKNLPEIEDYLEHAEEQNKELKEELErvqqsytlnenelervrGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELE 367
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 50658063 992 NLLQELKVIQENE-------HALQKDALSIKLKLEQIDGHIAEHNSKIK 1033
Cdd:pfam06160 368 EILEQLEEIEEEQeefkeslQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
898-997 |
5.34e-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: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 898 KLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEvvkntn 977
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE------ 94
|
90 100
....*....|....*....|
gi 50658063 978 aAEESLPEIQKEHRNLLQEL 997
Cdd:COG4942 95 -LRAELEAQKEELAELLRAL 113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
793-1004 |
6.76e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 793 IQEQKVQLEERVVKLRHSEREMRNTLEKftasIQRLIEQEEYLNvQVKELEanvlatapdKKKQKLLEENVSAFKTEYDA 872
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKK----ESELIKLKELAE-QLKELE---------EKLKKYNLEELEKKAEEYEK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 873 VAEKAGKVEAEVKRLHNTIVEIN--NHKLKAQQDKLDKINKQLDECASAITKAQV-AIKTADRNLQKAQdSVLRTEKEIK 949
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELE-PFYNEYLELK 608
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50658063 950 DTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEhrnlLQELKVIQENE 1004
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE----LEELEKKYSEE 659
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
329-542 |
9.00e-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: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 329 ELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHAT 408
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 409 SKAKKLEKQlqkdkekveEFKSIPAKSNNIinETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKESREKELMGF 488
Cdd:COG4942 111 RALYRLGRQ---------PPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 50658063 489 SKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIR 542
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
905-1033 |
1.06e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 905 KLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEvvkntnaAEESLP 984
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-------YEEQLG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 50658063 985 EI--QKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIK 1033
Cdd:COG1579 84 NVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
842-1020 |
1.09e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 842 LEANVLATAPDKKKQKllEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAIT 921
Cdd:COG3883 6 LAAPTPAFADPQIQAK--QKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 922 KAQVAIKTADRNLQKAQDSVLRTE--------------------------KEIKDTEKEVDDLTAELKSLEDKAAEVVKN 975
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLDvllgsesfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 50658063 976 TNAAEESLPEIQK---EHRNLLQELKViQENEHALQKDALSIKLKLEQ 1020
Cdd:COG3883 163 KAELEAAKAELEAqqaEQEALLAQLSA-EEAAAEAQLAELEAELAAAE 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
872-1020 |
1.24e-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: 45.91 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 872 AVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDT 951
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 952 EKEVDDLTAELKSL---------EDKAAEVVKNTNAAE-----ESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 1017
Cdd:COG4942 96 RAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
...
gi 50658063 1018 LEQ 1020
Cdd:COG4942 176 LEA 178
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
772-989 |
1.58e-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: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 772 SEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEA--NVLAT 849
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKeiAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 850 APDKKKQKLLEENVSAFKT---EYDAVAEKAGKVEAEVKRLhntivEINNHKLKAQQDKLDKINKQLDECASAITKAQVA 926
Cdd:COG4942 98 ELEAQKEELAELLRALYRLgrqPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50658063 927 IKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKE 989
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
738-1113 |
1.65e-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: 46.20 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 738 VTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDS--KKAMQIQEQKV---QLEERVVKL--RHS 810
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEadKNAKAIEKNKElfeQYKKDVTELlnKYS 1531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 811 EREMRNTLEKFTASIQRLIEQeeylnvqVKELEANVLATApDKKKQKLLEENVSAFKTEYDAVA-EKAGK----VEAEVK 885
Cdd:TIGR01612 1532 ALAIKNKFAKTKKDSEIIIKE-------IKDAHKKFILEA-EKSEQKIKEIKKEKFRIEDDAAKnDKSNKaaidIQLSLE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 886 RLHNTIVEINNHKLKAQQ--DKLDKINKQLDECASAITKAQVAIKTADRN-LQKAQDSVLRTEKEIKDTEKEVDDLTAEL 962
Cdd:TIGR01612 1604 NFENKFLKISDIKKKINDclKETESIEKKISSFSIDSQDTELKENGDNLNsLQEFLESLKDQKKNIEDKKKELDELDSEI 1683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 963 KSLEDKAAEVVKNTN-AAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKlKLEQIDGH--IAEHNSKIKYWHKEI 1039
Cdd:TIGR01612 1684 EKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTN-DLEGIDPNekLEEYNTEIGDIYEEF 1762
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50658063 1040 skISLHPIEDNPIEEISVlSPEDLEAIKNpDSITNQIALLEarchemkpnlgaIAEYKKKEELYLQRVA--ELDKI 1113
Cdd:TIGR01612 1763 --IELYNIIAGCLETVSK-EPITYDEIKN-TRINAQNEFLK------------IIEIEKKSKSYLDDIEakEFDRI 1822
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
937-1131 |
1.73e-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: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 937 AQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKL 1016
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1017 KLEQIDGHIAEHNSKIkYWHKEISKISLhpiednpieeisVLSPED-LEAIKNPDSITNQIALLEARCHEMKPNLGAIAE 1095
Cdd:COG4942 98 ELEAQKEELAELLRAL-YRLGRQPPLAL------------LLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 50658063 1096 ykKKEELYLQRvAELDKITYERDSFRQAYEDLRKQR 1131
Cdd:COG4942 165 --LRAELEAER-AELEALLAELEEERAALEALKAER 197
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
917-1124 |
1.75e-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: 45.79 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 917 ASAITKAQVAIKTADRNLQKAQDSVLRT-EKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRN--- 992
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEElQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVkkk 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 993 LLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIkywhkeiskislhpiednpIEEISVLspEDLEAIKNPDS- 1071
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPL-------------------IEEYRAL--KEAKSNKEDESq 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 50658063 1072 -ITNQIALLEARCHEMkpnlgaIAEYKKKEELYLQRVAELDKITyeRDSFRQAY 1124
Cdd:pfam05667 451 rKLEEIKELREKIKEV------AEEAKQKEELYKQLVAEYERLP--KDVSRSAY 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
736-1039 |
2.14e-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: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 736 RVVTLQGQIiEQSGTMtggGSKVMKGRMGSSLV--------IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERvvKL 807
Cdd:COG4913 575 RAITRAGQV-KGNGTR---HEKDDRRRIRSRYVlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQER--RE 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 808 RHSEREMRNTLEKFTASIQRLIEQeeyLNVQVKELEAN--VLATApdKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVK 885
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAE---LEAELERLDASsdDLAAL--EEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 886 RLhntiveinnhklkaqQDKLDKINKQLDEcASAITKAQVAIKTADRNLQKAQDSVLRTEKEikDTEKEVDDLTAELKSL 965
Cdd:COG4913 724 QA---------------EEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELRE--NLEERIDALRARLNRA 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 966 EDKAAEV-----------VKNTNAAEESLPEIQKEHRNLlqelkvIQENEHALQKDALsiKLKLEQIDGHIAEHNSKIKY 1034
Cdd:COG4913 786 EEELERAmrafnrewpaeTADLDADLESLPEYLALLDRL------EEDGLPEYEERFK--ELLNENSIEFVADLLSKLRR 857
|
....*
gi 50658063 1035 WHKEI 1039
Cdd:COG4913 858 AIREI 862
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
769-1024 |
2.28e-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: 45.81 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 769 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRliEQEEYLNVQVKELEANVLA 848
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR--EKERELVDCQRELEKLNKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 849 TAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRL----------HNTIVEI---NNHKLK--AQQDKLDKINKQL 913
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLatrleldgfeRGPFSERqikNFHTLVieRQEDEAKTAAQLC 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 914 DECAS-------AITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKntnaAEESLPEI 986
Cdd:TIGR00606 415 ADLQSkerlkqeQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK----AERELSKA 490
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 50658063 987 QKEH--RNLLQELKVIQENEHALQKDALSIKLKLEQIDGH 1024
Cdd:TIGR00606 491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
769-979 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 769 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLiEQEEYLNVqvkeleanvla 848
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLAL----------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 849 tapdkkkqKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKlKAQQDKLDKINKQLDECASAITKAQVAIK 928
Cdd:COG4942 125 --------LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR-AELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 50658063 929 TADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA 979
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
84-125 |
3.04e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 44.76 E-value: 3.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 50658063 84 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDS 125
Cdd:COG1195 2 LKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEA 41
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
947-1043 |
3.15e-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: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 947 EIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA-EESLPEIQKEHRNL---LQELKVIQENEHALQKDALSIKLKLEQID 1022
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELeeeLEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100
....*....|....*....|.
gi 50658063 1023 GHIAEHNSKIKYWHKEISKIS 1043
Cdd:COG0542 485 GKIPELEKELAELEEELAELA 505
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
898-1104 |
3.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 898 KLKAQQDKLDKINKQLDE-CASAITKAQVAIKTAD---RNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLED--KAAE 971
Cdd:COG4717 50 RLEKEADELFKPQGRKPElNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 972 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHalqkdalsiklKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNp 1051
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLSLATEEELQDL- 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50658063 1052 IEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYL 1104
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
327-485 |
4.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 327 IYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQL------------- 393
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 394 --------DLED-VQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVM 464
Cdd:COG3883 105 ldvllgseSFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180
....*....|....*....|.
gi 50658063 465 DSLKQETQGLQKEKESREKEL 485
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAEL 205
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
769-979 |
4.35e-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: 43.56 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 769 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLN-----VQVKELE 843
Cdd:pfam06008 42 IEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGendfaLPSSDLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 844 aNVLATApdkkkQKLLEE----NVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASA 919
Cdd:pfam06008 122 -RMLAEA-----QRMLGEirsrDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLREL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 920 ITKAQVAIKTADRNLQKAQdsvlRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAA 979
Cdd:pfam06008 196 LREAAAKTRDANRLNLANQ----ANLREFQRKKEEVSEQKNQLEETLKTARDSLDAANLL 251
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
90-258 |
4.78e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 42.87 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 90 QNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNS--DEHKDIQSCTVEVHFQKI 167
Cdd:pfam13476 4 ENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDirIGLEGKGKAYVEITFENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 168 IDKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDvgnllrSHGIDLDHNRFLILQGEvEQIAMMKPKGQTEHD 247
Cdd:pfam13476 82 DGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISE------LLKSDKIILPLLVFLGQ-EREEEFERKEKKERL 154
|
170
....*....|.
gi 50658063 248 EGMLEYLEDII 258
Cdd:pfam13476 155 EELEKALEEKE 165
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
329-589 |
6.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 329 ELQKRIAEMETQKEKIHEDTKEINE---KSNILSNE-----MKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQV 400
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQlksEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 401 REKLKHATSKAKKLEKQLQKDKEKVEEFKS-IPAKSNNIINETTTRNNALEKEKEKEEKKLKevmdsLKQETQGLQKEKE 479
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQINDLESKIQNQEKLNQQ-----KDEQIKKLQQEKE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 480 SREKELMGFSKSVNEARSKMdvaqSELDIYLSRHNTAVSQLTKAKEALiaaSETLKERKAAIRDIEGKLPQTEQELKEKE 559
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEI----KDLTNQDSVKELIIKNLDNTRESL---ETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
250 260 270
....*....|....*....|....*....|
gi 50658063 560 KELQKLTQEETNFKSLVHDLFQKVEEAKSS 589
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
773-1022 |
6.83e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 773 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATapd 852
Cdd:COG4372 58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 853 KKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADR 932
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 933 NlQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDAL 1012
Cdd:COG4372 215 E-LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250
....*....|
gi 50658063 1013 SIKLKLEQID 1022
Cdd:COG4372 294 ELKLLALLLN 303
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
104-238 |
6.90e-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: 42.96 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 104 FHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK--IRSKKLSVLIH----NSDEHKdiqsctvevHFQKIIDKEGDDYEV 177
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGGRASAdlIRSGAEKAVVEgvfdISDEEE---------AKALLLELGIEDDDD 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50658063 178 IpnsnfYVSRTACRDNTSVYHISGK---KKTFKDVGNLL------RSHGIDLDHNRFL-ILQGEVEQIAMM 238
Cdd:cd03241 90 L-----IIRREISRKGRSRYFINGQsvtLKLLRELGSLLvdihgqHDHQNLLNPERQLdLLDGGLDDVEFL 155
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
694-1039 |
7.18e-04 |
|
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: 43.94 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 694 FDLVKVKDEKIRQAFYFALR-DTLVADNLDQAtrvaYQK---DRRWRVVTLQGQIIEQSGTMTGggskvmkgrmgSSLVI 769
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKeDHEKIQHLEEE----YKKeinDKEKQVSLLLIQITEKENKMKD-----------LTFLL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 770 EISEEEVNKMESQLQNDSKKAMQIQEQK----VQLEERVVKLRHS---EREMRNTLEKFTASIQRLIEQEEYL------- 835
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSmstQKALEEDLQIATKTICQLTEEKEAQmeelnka 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 836 ----NVQVKELEANVLATAPD-KKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINN-HKLKAQQDKLDKI 909
Cdd:pfam05483 344 kaahSFVVTEFEATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 910 NKQLDECASAITKAQVAI----KTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPE 985
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 50658063 986 IQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEI 1039
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
327-441 |
8.79e-04 |
|
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: 43.02 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 327 IYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDV------KDTEKKLN--KITKFIEENKEKFTQLDLEDV 398
Cdd:pfam09728 112 LKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFekllktKELEVQLAeaKLQQATEEEEKKAQEKEVAKA 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 50658063 399 -QVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINE 441
Cdd:pfam09728 192 rELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTT 235
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
788-974 |
9.16e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 788 KKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANvlATAPDKKKQklleenvsaFK 867
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG--GVCPTCTQQ---------IS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 868 TEYDAVAEkagkveaevkrLHNTIVEINnHKLKAQQDKLDKINKQLDECASAITKA---QVAIKTADRNLQKAQDSVLRT 944
Cdd:PHA02562 296 EGPDRITK-----------IKDKLKELQ-HSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKAKKV 363
|
170 180 190
....*....|....*....|....*....|
gi 50658063 945 EKEIKDTEKEVDDLTAELKSLEDKAAEVVK 974
Cdd:PHA02562 364 KAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
83-129 |
1.24e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.72 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 50658063 83 MITHIVNQNFKSYAGEKIL-----GPFHKRFSCIIGPNGSGKSNVIDSMLFV 129
Cdd:COG1106 1 MLISFSIENFRSFKDELTLsmvasGLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-427 |
1.28e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 279 EHRGEKLN-RVKMVEKEKDALEGE-KNIAIEFLTLENEIFRKKNHVCQyyiyeLQKRIAEMETQKEKIhEDTKEINeksn 356
Cdd:COG1579 23 EHRLKELPaELAELEDELAALEARlEAAKTELEDLEKEIKRLELEIEE-----VEARIKKYEEQLGNV-RNNKEYE---- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50658063 357 ILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEE 427
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
83-154 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50658063 83 MITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKD 154
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGD 73
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
769-1004 |
1.83e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 769 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLA 848
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 849 TAPDkkkqklleenVSAFKTEYDAVAEKAGKVEAEVKRLHntiveinnhklkaqqDKLDKINKQLDECASAITKAQVAIK 928
Cdd:PRK02224 333 CRVA----------AQAHNEEAESLREDADDLEERAEELR---------------EEAAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50658063 929 TadrnlqkaqdsvlrTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLlqeLKVIQENE 1004
Cdd:PRK02224 388 E--------------LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA---RERVEEAE 446
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
831-1011 |
1.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 831 QEEYLNVQVKELEANVLATapdKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKIN 910
Cdd:COG3883 17 QIQAKQKELSELQAELEAA---QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA-EIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 911 KQL----------------DECASAITKAQV--AIKTADRN-LQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAE 971
Cdd:COG3883 93 RALyrsggsvsyldvllgsESFSDFLDRLSAlsKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 50658063 972 VVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDA 1011
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
329-531 |
2.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 329 ELQKRIAEMETQKEKIHEDTKEINEksniLSNEMKAKNKDVKDTEKKLNKITKFIEenkekFTQLDLEDVQVREKLKHAT 408
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 409 SKAKKLEKQLQKDKEKVEEfksIPAKSNNIINETTTRNNALEKEKEKEEKKlkevMDSLKQETQGLQKEKESREKELMGF 488
Cdd:COG4717 146 ERLEELEERLEELRELEEE---LEELEAELAELQEELEELLEQLSLATEEE----LQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50658063 489 SKSVNEARSKMDVAQSELdiylsRHNTAVSQLTKAKEALIAAS 531
Cdd:COG4717 219 QEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIAA 256
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
853-1129 |
2.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 853 KKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNH--KLKAQQDKLDKINKQLDECASAITKAQVAIKTA 930
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSElpELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 931 DRNLQKAQDSVLRTEKEIKDTEKEVDDL---TAELKSLEDKAAE---VVKNTNAAEESLPEIQKEHRNLLQELKVIQEne 1004
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELeekVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEE-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1005 haLQKDALSIKLKLEQIDGHIAE---HNSKIKYWHKEISKISLHPIEDNPIE-EISVLSPEDLEAI-----KNPDSITNQ 1075
Cdd:PRK03918 329 --RIKELEEKEERLEELKKKLKElekRLEELEERHELYEEAKAKKEELERLKkRLTGLTPEKLEKEleeleKAKEEIEEE 406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50658063 1076 IALLEARCHEMKPNLG----AIAEYKK----------------KEELYLQRVAELDKITYERDSFRQAYEDLRK 1129
Cdd:PRK03918 407 ISKITARIGELKKEIKelkkAIEELKKakgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
772-1153 |
2.80e-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: 42.03 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 772 SEEEVNKMESQL-----QNDSKKAMQIQeQKVQLEERVVKLRHSEREMRNTLEKFTASIQR--LIEQEEYLNVQVKELEA 844
Cdd:pfam15921 290 ARSQANSIQSQLeiiqeQARNQNSMYMR-QLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 845 NVLATAPDKKKQKLLEEnvsAFKTEYDAVAEKAGKVEAEVKRLHNTIV------EINNHKLKAQqdKLDKINKQL-DECA 917
Cdd:pfam15921 369 SQESGNLDDQLQKLLAD---LHKREKELSLEKEQNKRLWDRDTGNSITidhlrrELDDRNMEVQ--RLEALLKAMkSECQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 918 SAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEEslpeiqKEhrnllqel 997
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE------KE-------- 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 998 KVIQENEHALQKDALSIKLKLEQIDgHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAI-----KNPDSI 1072
Cdd:pfam15921 510 RAIEATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgRTAGAM 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1073 TNQIALLEARCHEMKPNLGAIAEYKKKEELYLQ----RVAELD----KITYERDSFRQAYEDLRKQR---LNEFMAGFYI 1141
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIReleaRVSDLElekvKLVNAGSERLRAVKDIKQERdqlLNEVKTSRNE 668
|
410
....*....|..
gi 50658063 1142 ItNKLKENYQML 1153
Cdd:pfam15921 669 L-NSLSEDYEVL 679
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
898-970 |
3.21e-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: 41.25 E-value: 3.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50658063 898 KLKAQQDKLDKINKQLDECASAITKAQ-VAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAA 970
Cdd:TIGR04320 283 ALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
881-1033 |
3.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 881 EAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTA 960
Cdd:COG3883 15 DPQIQAKQKELSELQA-ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 961 EL----------------KSLED--KAAEVVKNTNAAEESLPEIQKEHRNLLQELKV-IQENEHALQKDALSIKLKLEQI 1021
Cdd:COG3883 94 ALyrsggsvsyldvllgsESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAeLEAKLAELEALKAELEAAKAEL 173
|
170
....*....|..
gi 50658063 1022 DGHIAEHNSKIK 1033
Cdd:COG3883 174 EAQQAEQEALLA 185
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
774-1080 |
3.51e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 774 EEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSE----------REMRNTLEKFTASIQRLIEQEEYLNVQVKELe 843
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniqknidkiKNKLLKLELLLSNLKKKIQKNKSLESQISEL- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 844 anvlatapdKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNhKLKAQQDKLDKINKQLDECASAITKA 923
Cdd:TIGR04523 224 ---------KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK-QLSEKQKELEQNNKKIKELEKQLNQL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 924 QVAIKtaDRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQEN 1003
Cdd:TIGR04523 294 KSEIS--DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1004 EHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEI----SKISLHPIEDNPIE-EISVLSPEDLEAIKNPDSITNQIAL 1078
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdEQIKKLQQEKELLEkEIERLKETIIKNNSEIKDLTNQDSV 451
|
..
gi 50658063 1079 LE 1080
Cdd:TIGR04523 452 KE 453
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
773-1129 |
3.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 773 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSERE---MRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlAT 849
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELEELKEEIEELEKElesLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 850 APDKKKQKLLEENVSAFKTEYDA----VAEKAGKVEAEVKRLHNTIVEINN---------HKLKAQQDKLDKINK--QLD 914
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDelreIEKRLSRLEEEINGIEERIKELEEkeerleelkKKLKELEKRLEELEErhELY 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 915 ECASAITKAQVAIKT--ADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNA---AEESLP----E 985
Cdd:PRK03918 365 EEAKAKKEELERLKKrlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkAKGKCPvcgrE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 986 IQKEHR------------NLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHN--SKIKYWHKEISKISLHPIEDNP 1051
Cdd:PRK03918 445 LTEEHRkelleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1052 IE-------------EISVLSpEDLEAIKnpdSITNQIALLEARCHEMKPNLGAIaeYKKKEELYLQRVAELDKITYERD 1118
Cdd:PRK03918 525 EEyeklkekliklkgEIKSLK-KELEKLE---ELKKKLAELEKKLDELEEELAEL--LKELEELGFESVEELEERLKELE 598
|
410
....*....|.
gi 50658063 1119 SFRQAYEDLRK 1129
Cdd:PRK03918 599 PFYNEYLELKD 609
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
782-974 |
3.57e-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: 40.68 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 782 QLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVlatapDKKKQKLleE 861
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-----KKYEEQL--G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 862 NVSAFKtEYDAVaekagkveaevkrlhntiveinNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSV 941
Cdd:COG1579 84 NVRNNK-EYEAL----------------------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|...
gi 50658063 942 LRTEKEIkdtEKEVDDLTAELKSLEDKAAEVVK 974
Cdd:COG1579 141 EEKKAEL---DEELAELEAELEELEAEREELAA 170
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
773-1041 |
4.28e-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: 41.75 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 773 EEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKEleanvlatapd 852
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNK----------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 853 kkkqklleenvsAFKTEYDAVAEKAGKVEAEVKRLhntiveinnhkLKAQQDKLDKINKQLDECASAITKAQVAIKTAdr 932
Cdd:pfam12128 672 ------------ALAERKDSANERLNSLEAQLKQL-----------DKKHQAWLEEQKEQKREARTEKQAYWQVVEGA-- 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 933 nlQKAQDSVLRTEKEikdteKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHA------ 1006
Cdd:pfam12128 727 --LDAQLALLKAAIA-----ARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfd 799
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 50658063 1007 -------LQKDALSIKL-----KLEQIDGHIAEHNSKIKYWHKEISK 1041
Cdd:pfam12128 800 wyqetwlQRRPRLATQLsnierAISELQQQLARLIADTKLRRAKLEM 846
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
769-998 |
4.76e-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: 41.57 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 769 IEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEK---FTASIQRLIEQEEYLNVQVKELEAN 845
Cdd:TIGR00606 831 KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqqFEEQLVELSTEVQSLIREIKDAKEQ 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 846 VLATAPDKKK-QKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLH-------NTIVEINNHKLKAQQDKLDKINKQLDECA 917
Cdd:TIGR00606 911 DSPLETFLEKdQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdieNKIQDGKDDYLKQKETELNTVNAQLEECE 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 918 SAITKAQVAIKTADRNL--QKAQDSVLRTEKEIKDTEKEVDDLTAELKSL-----EDKAAEVVKNTNAAEESLPEIQKEH 990
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVLQMKQEHQKLEENIDLIKRNH 1070
|
....*...
gi 50658063 991 RNLLQELK 998
Cdd:TIGR00606 1071 VLALGRQK 1078
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
700-886 |
5.47e-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: 41.26 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 700 KDEKIRQafyfalrdtlvadNLDQATRVAYQKDRRWRvvtlqgQIIEQSGTMTGGGSKVMKGRMGSSLVIEisEEEVNKM 779
Cdd:pfam17380 390 KNERVRQ-------------ELEAARKVKILEEERQR------KIQQQKVEMEQIRAEQEEARQREVRRLE--EERAREM 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 780 ESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNtlekftasiQRLIEQEEYLNVQvKELEANVLATAPDKKKQKLL 859
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD---------RKRAEEQRRKILE-KELEERKQAMIEEERKRKLL 518
|
170 180
....*....|....*....|....*..
gi 50658063 860 EENVSAFKTeydAVAEKAGKVEAEVKR 886
Cdd:pfam17380 519 EKEMEERQK---AIYEEERRREAEEER 542
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
274-429 |
5.77e-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: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 274 VEILNEHRgEKLNRVKM-VEKEKDALEGE-KNIAIEFLTL-----ENEIFRKKNHVcqyYIYELQKRIAEMETQK----E 342
Cdd:pfam01576 358 LEELTEQL-EQAKRNKAnLEKAKQALESEnAELQAELRTLqqakqDSEHKRKKLEG---QLQELQARLSESERQRaelaE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 343 KIHEDTKEINEKSNILsNEMKAKN----KDVKDTEKKLNKITKFI-EENKEKFT------QLDLEDVQVREKLKHATSKA 411
Cdd:pfam01576 434 KLSKLQSELESVSSLL-NEAEGKNiklsKDVSSLESQLQDTQELLqEETRQKLNlstrlrQLEDERNSLQEQLEEEEEAK 512
|
170
....*....|....*...
gi 50658063 412 KKLEKQLQKDKEKVEEFK 429
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMK 530
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
812-1009 |
5.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 812 REMRNTLEKFTASIQRL-IEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAeVKRLHNT 890
Cdd:COG4717 52 EKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 891 IVEIN--NHKLKAQQDKLDKINKQLDEcasaITKAQVAIKTADRNLQKAQDSVLRTEKEIK-DTEKEVDDLTAELKSLED 967
Cdd:COG4717 131 YQELEalEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 50658063 968 KAAEvvkntnaAEESLPEIQKEHRNLLQELKVIQENEHALQK 1009
Cdd:COG4717 207 RLAE-------LEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
108-140 |
6.01e-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: 40.45 E-value: 6.01e-03
10 20 30
....*....|....*....|....*....|...
gi 50658063 108 FSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSK 140
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLT 33
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
770-1013 |
6.28e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 770 EISEEEVNKMESQLQN-------DSKKAMQIQeQKVQLEERVVKLRHSereMRNTLEKFTASIQRLIEQEEYLNVQVKEL 842
Cdd:PRK04863 386 EAAEEEVDELKSQLADyqqaldvQQTRAIQYQ-QAVQALERAKQLCGL---PDLTADNAEDWLEEFQAKEQEATEELLSL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 843 EanvlatapdkkkQKLleeNVS-AFKTEYDAVAEKAGKVEAEVKRL--HNTIVE-INNH-KLKAQQDKLDKINKQLDECA 917
Cdd:PRK04863 462 E------------QKL---SVAqAAHSQFEQAYQLVRKIAGEVSRSeaWDVARElLRRLrEQRHLAEQLQQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 918 SAITKAQVAIKTADRNLQKAQDSVLRTEkeikDTEKEVDDLTAELKSLEDKAAEVVkntnAAEESLPEIQKEHRNLLQEL 997
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDED----ELEQLQEELEARLESLSESVSEAR----ERRMALRQQLEQLQARIQRL 598
|
250
....*....|....*.
gi 50658063 998 KVIQENEHALQkDALS 1013
Cdd:PRK04863 599 AARAPAWLAAQ-DALA 613
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
84-128 |
6.60e-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: 6.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 50658063 84 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLF 128
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
778-1095 |
6.99e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 778 KMESQLQNDSKKAMQIQEQKVQLEervvKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQK 857
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEIN----SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 858 LLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEIN--NHKLKAQQDKLDKINKQLDECASaitkaqvaikTADRNLQ 935
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNryESEIKTAESDLSMELEKNNYYKE----------LEERHMK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 936 KAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKnTNAAEESLPEIQKEHRNLLQELKVIQEnehaLQKDALSIK 1015
Cdd:PRK01156 285 IINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK-YHAIIKKLSVLQKDYNDYIKKKSRYDD----LNNQILELE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1016 LKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAIKNP-----DSITNQIALLEARCHEMKPNL 1090
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEinvklQDISSKVSSLNQRIRALRENL 439
|
....*
gi 50658063 1091 GAIAE 1095
Cdd:PRK01156 440 DELSR 444
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
334-571 |
7.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 334 IAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEkftqlDLEDVQvrEKLKHATSKAKK 413
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA-----EIAEAE--AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 414 LEKQLQKDKEKVEEFKSIpAKSNNiINETTTRNNAlekeKEKEEKKLKEVMDSLKQETQGLQKEKESREKELmgfsKSVN 493
Cdd:COG3883 91 RARALYRSGGSVSYLDVL-LGSES-FSDFLDRLSA----LSKIADADADLLEELKADKAELEAKKAELEAKL----AELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50658063 494 EARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLPQTEQELKEKEKELQKLTQEETN 571
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
270-545 |
7.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 270 LCRRvEILNEHRGEKLNR----VKMVEKE-KDALEGEKNIAIEFLTLENEIFRKKNHVCQYYIYElqkriaemetQKEKI 344
Cdd:PRK03918 440 VCGR-ELTEEHRKELLEEytaeLKRIEKElKEIEEKERKLRKELRELEKVLKKESELIKLKELAE----------QLKEL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 345 HEDTKEINEKsnilsnEMKAKNKDVKDTEKKLNKITKFI---EENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKD 421
Cdd:PRK03918 509 EEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIkslKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 422 K-EKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKklkevMDSLKQETQGLQKEKESREKELMGFSKSVNEARSKMD 500
Cdd:PRK03918 583 GfESVEELEERLKELEPFYNEYLELKDAEKELEREEKE-----LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 50658063 501 VAQ--------SELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIE 545
Cdd:PRK03918 658 EEEyeelreeyLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
84-166 |
8.65e-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: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 84 ITHIVNQNFKSYAGEKIlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQkiRSKKLSVLIHNSDEHkdiqsCTVEVH 163
Cdd:TIGR00611 3 LSRLELTDFRNYDAVDL--ELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSH--RTSRDKPLIRFGAEA-----FVIEGR 73
|
...
gi 50658063 164 FQK 166
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 ... |
773-998 |
9.11e-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: 40.54 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 773 EEEVNKMESQLQNDSKKAMQiqeqkvQLEERVVKLRHSEReMRNTLEKftaSIQRLIEQEEYLNVQVKELEANVLATAPD 852
Cdd:pfam01576 337 EEETRSHEAQLQEMRQKHTQ------ALEELTEQLEQAKR-NKANLEK---AKQALESENAELQAELRTLQQAKQDSEHK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 853 KKK--QKLLEENVSAFKTEY--DAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDkLDKINKQL---DECASAITKAQV 925
Cdd:pfam01576 407 RKKleGQLQELQARLSESERqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD-VSSLESQLqdtQELLQEETRQKL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50658063 926 AIKTADRNLQKAQDSV---LRTEKEIKDT-EKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELK 998
Cdd:pfam01576 486 NLSTRLRQLEDERNSLqeqLEEEEEAKRNvERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
147-500 |
9.32e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.41 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 147 HNSDEHKDIqscTVEVHFQKIIDKEGDDYEvipnSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLLRSH---GIDLDHN 223
Cdd:PTZ00108 923 YSTANTVHF---TVKLNDGVLEQWEEEGIE----KVFKLKSTISTTNMVLFDENGKIKKYSDALDILKEFylvRLDLYKK 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 224 R--FLI--LQGEVEQIammkpkgqtehdEGMLEYLEDIIgcgrlNEPIKVLCR-RVEILNEHRGEKLNRVKMVEKEKDAL 298
Cdd:PTZ00108 996 RkeYLLgkLERELARL------------SNKVRFIKHVI-----NGELVITNAkKKDLVKELKKLGYVRFKDIIKKKSEK 1058
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 299 --EGEKNIAIEFLTLENEIFRKKNHVCQYYIYELQKRIAEMetQKEKIHEDTKEINEKSNILSnemKAKNKDVKDTEKK- 375
Cdd:PTZ00108 1059 itAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSL--TKEKVEKLNAELEKKEKELE---KLKNTTPKDMWLEd 1133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 376 LNKITKFIE--ENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETT--TRNNALEK 451
Cdd:PTZ00108 1134 LDKFEEALEeqEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSdeKRKLDDKP 1213
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 50658063 452 EKEKEEKKLKEVMDSLKQETQGLQKEKESREKELMGFSKSVNEARSKMD 500
Cdd:PTZ00108 1214 DNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSS 1262
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
896-1273 |
9.43e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 896 NHKLKAQQDKLDKINKQLDEcasAITKAQVAIktaDRNLQKAQD---SVLRTEKEIKDTEKEVDDLTAELKSLEDKAA-- 970
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGE---NIARKQNKY---DELVEEAKTikaEIEELTDELLNLVMDIEDPSAALNKLNTAAAki 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 971 ----------------------------EVVKNTNAAEESLPEIQKEHRNLL---QELKVIQENEHALQKDALSIKLKLE 1019
Cdd:PHA02562 268 kskieqfqkvikmyekggvcptctqqisEGPDRITKIKDKLKELQHSLEKLDtaiDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1020 QIDGHIAEHNSKIKYWHKEISKISLHPIEDNpiEEISVLSpEDLEAIKNPDSitnqiallearchemkpnlgaiaeYKKK 1099
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNA--EELAKLQ-DELDKIVKTKS------------------------ELVK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1100 EELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMagfyiitnKLKENYQMLTLggDAElelvdsldpFSEGImfsvr 1179
Cdd:PHA02562 401 EKYHRGIVTDLLKDSGIKASIIKKYIPYFNKQINHYL--------QIMEADYNFTL--DEE---------FNETI----- 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50658063 1180 ppKKSWKKIF---NLSGGEKTLSSLALVFA------LHHYKPTPLYFMDEI-DAALDFKNVSIVaFYIYEQTKNAQFIII 1249
Cdd:PHA02562 457 --KSRGREDFsyaSFSQGEKARIDLALLFTwrdvasKVSGVDTNLLILDEVfDGALDAEGTKAL-LSILDSLKDTNVFVI 533
|
410 420
....*....|....*....|....
gi 50658063 1250 SLRNNMFEISDRLIGIYKTYNITK 1273
Cdd:PHA02562 534 SHKDHDPQKFDRHLKMEKVGRFSV 557
|
|
| |
