|
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 ... |
81-1272 |
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: 593.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 81 MITHIVNQNFKSYAgEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK-IRSKKLSVLIHnSDEHKDIQSCTVE 159
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKsLRSERLSDLIH-SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 160 VHFqkiidKEGDDYEVLPNSNFYVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 239
Cdd:pfam02463 79 ITF-----DNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 240 GQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKNH 319
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 320 ICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVR 399
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 400 EKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQ 479
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 480 EKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKE 559
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 560 LQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDIAISSCCHALD 639
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 640 YIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRLfdlvkvkneeirqafyfalrdtlvaNNL 719
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL-------------------------AQL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 720 DQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQKVQHE 799
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 800 EAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVE 879
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 880 AEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTE 959
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 960 LKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISK 1039
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1040 IKLHPVEDNPVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSERDNFR 1119
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1120 QAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSL 1199
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVAL 1088
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789347 1200 ALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTKS 1272
Cdd:pfam02463 1089 ALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
82-1263 |
5.41e-125 |
|
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: 415.62 E-value: 5.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 82 ITHIVNQNFKSYAGEKVLgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGY-RAQKIRSKKLSVLIHNSDEHKDIQSCTVEV 160
Cdd:TIGR02169 2 IERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLsSSKAMRAERLSDLISNGKNGQSGNEAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 161 HFQKIIDKEGDDYEVLpnsnfyVSRTAYRD-STSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFlILQGEVEQIAMMKPK 239
Cdd:TIGR02169 81 TFKNDDGKFPDELEVV------RRLKVTDDgKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 240 GQTEhdegmleYLEDIIGCGRLNEPIKVLCRRVEILnehrGEKLNRVKMVEKEK----DALEGEKNIAIEFLTLENEMFK 315
Cdd:TIGR02169 154 ERRK-------IIDEIAGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKrqqlERLRREREKAERYQALLKEKRE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 316 KKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFiEQN--KEKFTQLDL 393
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLrvKEKIGELEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 394 EDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKklkeVMDSLKQETQGLQ 473
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----ELEDLRAELEEVD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 474 KEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEAL------ITASETLKERKAA-IKDINTKL 546
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagieakINELEEEKEDKALeIKKQEWKL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 547 PQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGrIPGIYGRLGDLGAIDEK 626
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS-IQGVHGTVAQLGSVGER 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 627 YDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRLFDLVKVkNEEIRQA 705
Cdd:TIGR02169 537 YATAIEVAAGNrLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-DPKYEPA 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 706 FYFALRDTLVANNLDQATRVAYQrdrrWRVVTLQGQIIEQSGTMSGGgSKVMRGRMGSSVIDEISVEEVNKMESQLERHS 785
Cdd:TIGR02169 616 FKYVFGDTLVVEDIEAARRLMGK----YRMVTLEGELFEKSGAMTGG-SRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 786 KQAMQ-IQEQKVQHEEAVVKLRHSER---DMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVltTAPDRKQQKLleenv 861
Cdd:TIGR02169 691 SSLQSeLRRIENRLDELSQELSDASRkigEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI--ENVKSELKEL----- 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 862 svfKKEYDAVAEKAGKVEAEI----KRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQD 937
Cdd:TIGR02169 764 ---EARIEELEEDLHKLEEALndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 938 SVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLE 1017
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1018 QIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAIKNPESItneialleaqcremkpNLGAIAEYKKK 1097
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV----------------NMLAIQEYEEV 984
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1098 EDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTlGGDAELELVDSLDPFSEGIMFSVR 1177
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAK 1063
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1178 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEIS 1257
Cdd:TIGR02169 1064 PKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYA 1143
|
....*.
gi 29789347 1258 DRLIGI 1263
Cdd:TIGR02169 1144 DRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
90-1263 |
7.29e-103 |
|
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: 354.36 E-value: 7.29e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 90 FKSYAgEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFqkiiD 167
Cdd:TIGR02168 10 FKSFA-DPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGeQSAKALRGGKMEDVIFNgSETRKPLSLAEVELVF----D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 168 KEGDDYEVLPNSNFYVSRTAYRDSTSVYHISGKKKTFKDVGNLL-------RSHGIdldhnrflILQGEVEQIAMMKPkg 240
Cdd:TIGR02168 85 NSDGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFldtglgkRSYSI--------IEQGKISEIIEAKP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 241 qtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILN--EHRGEKLNRV----KMVEKEKDALEGEKNIAIEFLTLENEMF 314
Cdd:TIGR02168 155 -----EERRAIFEEAAGISKYKE------RRKETERklERTRENLDRLedilNELERQLKSLERQAEKAERYKELKAELR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 315 KKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLE 394
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 395 DVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKErekeekklkevMDSLKQETQGLQK 474
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELES 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 475 EKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRhntaVSQLSKAKEALITASETLKER--KAAIKDINTKLPQTQQE 552
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR----LERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 553 LKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQE------------KKSGRIPGIYGRLGDL 620
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsegvkallKNQSGLSGILGVLSEL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 621 GAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPR----LFDLV 695
Cdd:TIGR02168 529 ISVDEGYEAAIEAALGGrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvAKDLV 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 696 KVKnEEIRQAFYFALRDTLVANNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSV-IDEISvEEV 774
Cdd:TIGR02168 609 KFD-PKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRReIEELE-EKI 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 775 NKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRntlekfaasiQGLSEQEEylcvQIKELEANVLTTAPDRKQQ 854
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----------RQISALRK----DLARLEAEVEQLEERIAQL 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 855 KLLEENVSVFKKEYDAVAEKAGKVEAEIKRlhntiidinnrKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKK 934
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEA-----------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 935 AQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKL 1014
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1015 KLEQIDGHISEHNSKIKYWQKEISKIKLHPVE-----DNPVETVAVLSQEELEAIKN--------PESITNEIALLEAQC 1081
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGlevriDNLQERLSEEYSLTLEEAEAlenkieddEEEARRRLKRLENKI 981
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1082 REMKP-NLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTLGGDAELE 1160
Cdd:TIGR02168 982 KELGPvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELR 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1161 LVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTK 1240
Cdd:TIGR02168 1062 LTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSK 1141
|
1210 1220
....*....|....*....|...
gi 29789347 1241 NAQFIIISLRNNMFEISDRLIGI 1263
Cdd:TIGR02168 1142 NTQFIVITHNKGTMEVADQLYGV 1164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
82-1263 |
8.28e-69 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 251.39 E-value: 8.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 82 ITHIVNQNFKSYAGEKVLgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG---YRAqkIRSKKLSVLIHN-SDEHKDIQSCT 157
Cdd:COG1196 3 LKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGeqsAKS--LRGGKMEDVIFAgSSSRKPLGRAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 158 VEVHF---QKIIDKEGDDYEvlpnsnfyVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLD-HNrfLILQGEVEQI 233
Cdd:COG1196 80 VSLTFdnsDGTLPIDYDEVT--------ITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPEsYS--IIGQGMIDRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 234 AMMKPkgqtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILNEHRG--EKLNRVK--MVEKEK--DALEGEKNIAIEFL 307
Cdd:COG1196 150 IEAKP-------EERRAIIEEAAGISKYKE------RKEEAERKLEAteENLERLEdiLGELERqlEPLERQAEKAERYR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 308 TLENEMFKKKNHICQYYIYDLQNRIAEITTQKEkihedtkEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEK 387
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELE-------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 388 FTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEV---MDS 464
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeeaLLE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 465 LKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINT 544
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 545 KLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSS----LAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDL 620
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARllllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 621 GAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVwAKKMSKIQTPENTPRLFDLVKVKN 699
Cdd:COG1196 530 IGVEAAYEAALEAALAAaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA-RAALAAALARGAIGAAVDLVASDL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 700 EEiRQAFYFALRDTLVANNLDQATRvayqRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEISVEEVNKMES 779
Cdd:COG1196 609 RE-ADARYYVLGDTLLGRTLVAARL----EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 780 QLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEAnvlttapdrkqqkLLEE 859
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE-------------LLEE 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 860 NVsvfkKEYDAVAEKAGKVEAEIKRLhntiidinnrklkaqqnkldtinkqldecasaitkaqvaiktadrnlkkaqdsv 939
Cdd:COG1196 751 EA----LEELPEPPDLEELERELERL------------------------------------------------------ 772
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 940 crtekeikdtEKEINDLktelkniedkaEEVinntktaetslpeiqkehrNL--LQELKVIQEnehalQKDALSiklklE 1017
Cdd:COG1196 773 ----------EREIEAL-----------GPV-------------------NLlaIEEYEELEE-----RYDFLS-----E 802
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1018 QIDghisehnskikywqkeiskiklhpveDnpvetvavlsqeeleaiknpesitneiaLLEAqcremkpnlgaiaeykkK 1097
Cdd:COG1196 803 QRE--------------------------D----------------------------LEEA-----------------R 811
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1098 EDLyLQRVAELDKITSERdnFRQAYEDLRKQrlnefmagfyvitnkLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVR 1177
Cdd:COG1196 812 ETL-EEAIEEIDRETRER--FLETFDAVNEN---------------FQELFPRLFGGGEAELLLTDPDDPLETGIEIMAQ 873
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1178 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEIS 1257
Cdd:COG1196 874 PPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAA 953
|
....*.
gi 29789347 1258 DRLIGI 1263
Cdd:COG1196 954 DRLYGV 959
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
80-239 |
6.61e-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: 227.56 E-value: 6.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 80 LMITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVE 159
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHPNLDSCSVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 160 VHFQKIIDKEgddyevlpnsnfyvsrtayrdstsvyhisgkkktfkdvgnLLRSHGIDLDHNRFLILQGEVEQIAMMkPK 239
Cdd:cd03274 81 VHFQEIIDKP----------------------------------------LLKSKGIDLDHNRFLILQGEVEQIAQM-PK 119
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1179-1273 |
3.25e-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: 219.86 E-value: 3.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1179 PKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISD 1258
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAD 197
|
90
....*....|....*
gi 29789347 1259 RLIGIYKTYNSTKSV 1273
Cdd:cd03274 198 RLVGIYKTNNCTKSV 212
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1189-1271 |
1.33e-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: 125.11 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1189 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKN-AQFIIISLRNNMFEISDRLIGIYKTY 1267
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 29789347 1268 NSTK 1271
Cdd:cd03239 175 GVST 178
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
611-725 |
2.84e-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: 121.95 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 611 PGIYGRLGDLGAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTV-----WAKKMSKIQT 684
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGrLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPrspagSKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 29789347 685 PENTPRLFDLVKVKnEEIRQAFYFALRDTLVANNLDQATRV 725
Cdd:smart00968 81 PGFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
88-240 |
3.60e-32 |
|
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: 126.15 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 88 QNFKSYAGEKVLGPFhKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFQKii 166
Cdd:cd03275 7 ENFKSYKGRHVIGPF-DRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRaRVGKPDSNSAYVTAVYED-- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789347 167 dkegDDYEVLpnsnfyVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKG 240
Cdd:cd03275 84 ----DDGEEK------TFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPPG 147
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1178-1265 |
1.29e-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: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1178 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEI 1256
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEFFSK 224
|
....*....
gi 29789347 1257 SDRLIGIYK 1265
Cdd:cd03275 225 ADALVGVYR 233
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
610-726 |
2.51e-28 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 110.43 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 610 IPGIYGRLGDLGAIDEKYDIAISSCC-HALDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTpENT 688
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALgGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLK-GGA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 29789347 689 PRLFDLVKVKnEEIRQAFYFALRDTLVANNLDQATRVA 726
Cdd:pfam06470 80 GPLLDLVEYD-DEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1184-1263 |
1.04e-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: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1184 KKIFN---LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRL 1260
Cdd:cd03278 106 KKVQRlslLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
...
gi 29789347 1261 IGI 1263
Cdd:cd03278 186 YGV 188
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
82-165 |
2.23e-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: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 82 ITHIVNQNFKSYAGEKVLGPFHkRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHnSDEHKDIQSCTVEVH 161
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSN-SFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAG-GGVKAGINSASVEIT 78
|
....
gi 29789347 162 FQKI 165
Cdd:cd03239 79 FDKS 82
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1186-1266 |
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 29789347 1186 IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEISDRLIGIY 1264
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIK 154
|
..
gi 29789347 1265 KT 1266
Cdd:cd03227 155 KV 156
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
82-162 |
6.69e-17 |
|
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: 80.59 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 82 ITHIVNQNFKSYAGEKVLgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHNSDEHKDIQS-CTVE 159
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGeQSAKSLRGEKMSDVIFAGSETRKPANfAEVT 79
|
...
gi 29789347 160 VHF 162
Cdd:cd03278 80 LTF 82
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1184-1263 |
1.06e-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: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1184 KKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1263
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1183-1268 |
1.98e-16 |
|
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: 80.42 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1183 WKK-IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLi 1261
Cdd:cd03273 160 WKEsLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVL- 238
|
....*..
gi 29789347 1262 giYKTYN 1268
Cdd:cd03273 239 --FRTRF 243
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
82-236 |
6.73e-16 |
|
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: 78.88 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 82 ITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRA-QKIRSKKLSVLIHNSDEhKDIQSCTVEV 160
Cdd:cd03273 3 IKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKRGQ-AGITKASVTI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789347 161 HFqKIIDKEGDD--YEVLPnsNFYVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMM 236
Cdd:cd03273 82 VF-DNSDKSQSPigFENYP--EITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNM 156
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
84-168 |
1.65e-14 |
|
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: 72.39 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 84 HIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKklsvlihnSDEHKDIQSCTVEVHFQ 163
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRR--------SGVKAGCIVAAVSAELI 72
|
....*
gi 29789347 164 KIIDK 168
Cdd:cd03227 73 FTRLQ 77
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
82-243 |
3.34e-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: 70.75 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 82 ITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIqSCTVEVH 161
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVM-SAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 162 FQKIidkegDDYEVLPNSNFYVSRT--AYRDStsvYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 239
Cdd:cd03272 80 FDNS-----DNRFPIDKEEVRLRRTigLKKDE---YFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQD 151
|
....
gi 29789347 240 GQTE 243
Cdd:cd03272 152 EQQE 155
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-587 |
2.94e-11 |
|
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: 68.12 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 328 LQNRIAEITTQKEKIHEDTKEITE---KSNVLSNE-----MKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVR 399
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQlksEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 400 EKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEvmdsLKQETQGLQKEKEIQ 479
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ----KDEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 480 EKE---LMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKakealitaseTLKERKAAIKDINTKLPQTQQELKEK 556
Cdd:TIGR04523 425 EKEierLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET----------QLKVLSRSINKIKQNLEQKQKELKSK 494
|
250 260 270
....*....|....*....|....*....|.
gi 29789347 557 EKELQKLTQEEINLKSLVHDLFQKVEEAKSS 587
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-588 |
2.26e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 88 QNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDSmLFVFGYRAQKIRSKKLSvlihNSDEHKDIQSCT-VEVHFqkii 166
Cdd:PRK03918 9 KNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEA-ILVGLYWGHGSKPKGLK----KDDFTRIGGSGTeIELKF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 167 DKEGDDYEVLPNSNFYVSRTAYRDSTSVYHiSGKKKTFKDVGNLLRSHgidLDHNRFLILQGEVEQIammkpkgqTEHDE 246
Cdd:PRK03918 78 EKNGRKYRIVRSFNRGESYLKYLDGSEVLE-EGDSSVREWVERLIPYH---VFLNAIYIRQGEIDAI--------LESDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 247 GMLEYLEDIIGCGR-------LNEPIKVLCRRVEILNE---HRGEKLNRVKMVEKEKDALEGE-KNIAIEFLTLENEMFK 315
Cdd:PRK03918 146 SREKVVRQILGLDDyenayknLGEVIKEIKRRIERLEKfikRTENIEELIKEKEKELEEVLREiNEISSELPELREELEK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 316 KKNHICQY-----YIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQ 390
Cdd:PRK03918 226 LEKEVKELeelkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 391 LDlEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKevMDSLKQETQ 470
Cdd:PRK03918 306 LD-ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--LERLKKRLT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 471 GLQKEKEIQE-KELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKE------ALITA---SETLKERKAAIK 540
Cdd:PRK03918 383 GLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgRELTEehrKELLEEYTAELK 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 29789347 541 DINTKLPQTQQELKEKEKELQKLTQEEINLKSLV--HDLFQKVEEAKSSL 588
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKL 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
259-586 |
2.06e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 259 GRLNEPIKVLCRRVEILNEHR---GEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEI 335
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 336 TTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKlnkvtkfieQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQ 415
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA---------KGKCPVCGRELTEEHRKELLEEYTAELKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 416 LQKDKEKVEELKSVPAKSKTVINETTTrnnslekerEKEEKKLKEVMDSLKQETQGLQKEK-EIQEKELMGFNKSVNEAR 494
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESE---------LIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 495 SKMEVAQSELDiylsrhntAVSQLSKAKEALITASETLKERKAAIKDINTKLP-QTQQELKEKEKELQKLTQEEINLKSL 573
Cdd:PRK03918 539 GEIKSLKKELE--------KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDA 610
|
330
....*....|...
gi 29789347 574 VHDLFQKVEEAKS 586
Cdd:PRK03918 611 EKELEREEKELKK 623
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1186-1265 |
2.41e-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: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1186 IFNLSGGEKTLSSLALVFALhhyKPtPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFE-ISDRLIGI 1263
Cdd:cd00267 78 VPQLSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVL 153
|
..
gi 29789347 1264 YK 1265
Cdd:cd00267 154 KD 155
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
347-1040 |
2.68e-08 |
|
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: 58.49 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 347 KEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQK-------D 419
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKinseiknD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 420 KEKVEELKSVPAKSKTVINETT---TRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSK 496
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKkniDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 497 ---MEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERkaaikdiNTKLPQTQQELKEKEKELQKLTQEEINLKSL 573
Cdd:TIGR04523 196 llkLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK-------QQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 574 VHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRL-GDLGAIDEKYDIAISSCCHAldyivVDSIDTAQEC 652
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN-----NKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 653 VNFLKKhnigiatfiglDKMTVWAKKMSK-IQTPENTPRLFDLVKVKNEEIRQAFYFALRDTLVANNLDQATRVAYQRDR 731
Cdd:TIGR04523 344 ISQLKK-----------ELTNSESENSEKqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 732 RWRVVTLQGQIIEQsgtmsgggskvmrgrmgssvideisveEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERD 811
Cdd:TIGR04523 413 QIKKLQQEKELLEK---------------------------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 812 MRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTapdRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIID 891
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL---NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 892 INNRKLKAQQN-KLDTINKQLDECASAITKaqvaIKTADRNLKKAQDSVcrtEKEIKDTEKEINDLKTELKNIEDKAEEV 970
Cdd:TIGR04523 543 LEDELNKDDFElKKENLEKEIDEKNKEIEE----LKQTQKSLKKKQEEK---QELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 971 inntktaETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKI 1040
Cdd:TIGR04523 616 -------EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
81-127 |
4.22e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.86 E-value: 4.22e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 29789347 81 MITHIVNQNFKSYAG-EKVLGPFHkrfsCIIGPNGSGKSNVIDSMLFV 127
Cdd:COG4637 1 MITRIRIKNFKSLRDlELPLGPLT----VLIGANGSGKSNLLDALRFL 44
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
81-175 |
4.37e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.02 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 81 MITHIVNQNFKSYAGEKVLgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKiRSKKLSVLIHNSDEhkdiqSCTVEV 160
Cdd:COG0419 1 KLLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSE-----EASVEL 73
|
90
....*....|....*
gi 29789347 161 HFQkiidKEGDDYEV 175
Cdd:COG0419 74 EFE----HGGKRYRI 84
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
330-608 |
2.10e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 330 NRIAE--ITTQKEKIHEDTKEITEksnVLSNEMKAKNSAVKDVEKKLNKvtkFIEQNKekFTQLDLEDVQVREKLKHATS 407
Cdd:COG3206 155 NALAEayLEQNLELRREEARKALE---FLEEQLPELRKELEEAEAALEE---FRQKNG--LVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 408 KAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTrnnslekerekeekklKEVMDSLKQETQGLQKEKEIQEKELMGFN 487
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------SPVIQQLRAQLAELEAELAELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 488 KSVNEARSKMEVAQSELDiylSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQkltqee 567
Cdd:COG3206 291 PDVIALRAQIAALRAQLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE------ 361
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 29789347 568 iNLKSLVHDLFQKVEEAKSSLAMNRSRGKVLD-AIIQEKKSG 608
Cdd:COG3206 362 -VARELYESLLQRLEEARLAEALTVGNVRVIDpAVVPLKPVS 402
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
771-1085 |
6.78e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 771 VEEVNKMESQLErHSKQAMQIQEQKVQHEEAVVKLRHSE-RDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTAP 849
Cdd:pfam15921 481 VEELTAKKMTLE-SSERTVSDLTASLQEKERAIEATNAEiTKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 850 DRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNtiiDINNRKLKAQQ-----NKLDTINKQLDECASAITKAQVA 924
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEfkilkDKKDAKIRELEARVSDLELEKVK 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 925 IKTAD-------RNLKKAQDSVCrteKEIKDTEKEINDLKTEL----KNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQ 993
Cdd:pfam15921 637 LVNAGserlravKDIKQERDQLL---NEVKTSRNELNSLSEDYevlkRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 994 ELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKI--KLHPVEdnpvETVAVLSQEELEAIKNPESIT 1071
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAnkEKHFLK----EEKNKLSQELSTVATEKNKMA 789
|
330
....*....|....
gi 29789347 1072 NEIALLEAQCREMK 1085
Cdd:pfam15921 790 GELEVLRSQERRLK 803
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
300-607 |
1.26e-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: 53.10 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 300 KNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSA----VKDVEKKLN 375
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEnsekQRELEEKQN 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 376 KVTKFIEQNKEKFTQLDLEDVQVREkLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEE 455
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 456 KKLKEVMDSLKqetqglqKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKER 535
Cdd:TIGR04523 450 SVKELIIKNLD-------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789347 536 KAAIKDINTKLPQTQQELKEKEKELQKLTQE--EINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKS 607
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
386-1205 |
1.61e-06 |
|
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: 52.66 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 386 EKFTQLDLEdvqVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETttrnnslekerekeekkLKEVMDSL 465
Cdd:TIGR00618 176 DQYTQLALM---EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKE-----------------LKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 466 KQETQGLQKEKEIQEKElmgfnksvnEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLK--ERKAAIKDIN 543
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQ---------EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 544 TKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLamnrsRGKVLDAIIQEKKSGRIPGIYGRLGDLGAI 623
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH-----SQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 624 dekydiaissccHALDYIvvdsIDTAQECVNFLKKHnigiatfigLDKMTVWAKKMSkIQTPENTPRLFDLVKVKNEEIR 703
Cdd:TIGR00618 382 ------------HTLQQQ----KTTLTQKLQSLCKE---------LDILQREQATID-TRTSAFRDLQGQLAHAKKQQEL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 704 QAFYFALRDTLVANNLDQAT-RVAYQRDRRWRVVTLqgqiIEQSGTMSGGGSKVMR-GRMGSSVIDEISVEE--VNKMES 779
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKlEKIHLQESAQSLKER----EQQLQTKEQIHLQETRkKAVVLARLLELQEEPcpLCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 780 QLERHSKQA----------MQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANV-LTTA 848
Cdd:TIGR00618 512 HPNPARQDIdnpgpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpNLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 849 PDRKQQKLLEENVSVFKKEydAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKL-------DTINKQLDECASAITKA 921
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDML--ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtalhalqLTLTQERVREHALSIRV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 922 QVAIKTADR-NLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVIN---------------NTKTAETSLPEIQ 985
Cdd:TIGR00618 670 LPKELLASRqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassslgsdlaaREDALNQSLKELM 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 986 KEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAiK 1065
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-Q 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1066 NPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLK 1145
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRL 908
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789347 1146 ENYQMLTLGGDAELELVDSLDPFSEGIMF------SVRPPKkswkkifNLSGGEKTLSSLALVFAL 1205
Cdd:TIGR00618 909 ANQSEGRFHGRYADSHVNARKYQGLALLVadaytgSVRPSA-------TLSGGETFLASLSLALAL 967
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
856-1135 |
6.00e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 856 LLEENVSVFKKEYDAVAEKAGKVEAEIKRLhNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKA 935
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQA-REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 936 QDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 1015
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1016 LEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYK 1095
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 29789347 1096 KKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMA 1135
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
381-604 |
6.90e-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: 49.76 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 381 IEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRnnslekerekeekklke 460
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 461 vMDSLKQETQGLQKEKEIQEKELMGFNKSV--NEARSKMEV---AQSELDIYlsRHNTAVSQLSKAKEALITA-SETLKE 534
Cdd:COG4942 85 -LAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALllsPEDFLDAV--RRLQYLKYLAPARREQAEElRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 535 RKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQE 604
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
837-1134 |
1.20e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 837 IKELEaNVLTTAPDrkQQKLLEENVSVFKKEYDavaEKAGKVEAEikrlhNTIIDINNRKLKAQQNKLDTINKQLDECAS 916
Cdd:TIGR00606 697 ISDLQ-SKLRLAPD--KLKSTESELKKKEKRRD---EMLGLAPGR-----QSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 917 AITKAQVAIKTADRNLKKAQDSVC------RTEKEIKDTEKEINDLKTELKNIE---------DKAEEVINNTKTAETSL 981
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVCLTdvtimeRFQMELKDVERKIAQQAAKLQGSDldrtvqqvnQEKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 982 PEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEEL 1061
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1062 EAIKNPESITNEIALLEAQcrEMKPNLGAIAEYKK---------KEDLYLQRVAELDKITSERDNFRQayedlRKQRLNE 1132
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVN--DIKEKVKNIHGYMKdienkiqdgKDDYLKQKETELNTVNAQLEECEK-----HQEKINE 998
|
..
gi 29789347 1133 FM 1134
Cdd:TIGR00606 999 DM 1000
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
896-1136 |
1.22e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 896 KLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEvinntk 975
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 976 tAETSLPEIQKEHRNLLQELKVIQENEHA---LQKDALSIKLKLEQIDGHISEHNskikywQKEISKIKlhpvednpvet 1052
Cdd:COG4942 95 -LRAELEAQKEELAELLRALYRLGRQPPLallLSPEDFLDAVRRLQYLKYLAPAR------REQAEELR----------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1053 vavLSQEELEAIKnpESITNEIALLEAQCREMKpnlgaiAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRK--QRL 1130
Cdd:COG4942 157 ---ADLAELAALR--AELEAERAELEALLAELE------EERAALEALKAERQKLLARLEKELAELAAELAELQQeaEEL 225
|
....*.
gi 29789347 1131 NEFMAG 1136
Cdd:COG4942 226 EALIAR 231
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1189-1265 |
1.82e-05 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 46.82 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1189 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTK---NAQFIIISLRNNMFEISDRLIGIYK 1265
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKkqpGRQFIFITPQDISGLASSDDVKVFR 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
772-1018 |
2.40e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 772 EEVNKMESQLERHSKQAM---QIQEQKVQHEEAVVKLRHSERdMRNTLEKFAAsiqglseqeeylcvqikELEANVLtta 848
Cdd:COG4913 235 DDLERAHEALEDAREQIEllePIRELAERYAAARERLAELEY-LRAALRLWFA-----------------QRRLELL--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 849 pdRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTA 928
Cdd:COG4913 294 --EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 929 DRnlkkaqdSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETslpEIQKEHRNLLQELKVIQENEHALQKD 1008
Cdd:COG4913 372 GL-------PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRKSNIPAR 441
|
250
....*....|
gi 29789347 1009 ALSIKLKLEQ 1018
Cdd:COG4913 442 LLALRDALAE 451
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
82-168 |
2.43e-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: 48.07 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 82 ITHIVNQNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRaqkiRSKKLSVL-IHNSDEHKDIqSCTVEV 160
Cdd:COG3593 3 LEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPS----SSRKFDEEdFYLGDDPDLP-EIEIEL 75
|
....*...
gi 29789347 161 HFQKIIDK 168
Cdd:COG3593 76 TFGSLLSR 83
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
334-593 |
2.84e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.56 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 334 EITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHatsKAKKLE 413
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVK 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 414 KQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKlkevMDSLKQETQGLQKEKEIQEKELMGFNKSVNEA 493
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN----IEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 494 RSKMEVAQSELDIYLSRHNTAVSQ--------LSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQ 565
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDkkiseeklLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE 721
|
250 260
....*....|....*....|....*...
gi 29789347 566 EEINLKSLVHDLFQKVEEAKSSLAMNRS 593
Cdd:pfam05483 722 ERDSELGLYKNKEQEQSSAKAALEIELS 749
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
902-1096 |
3.02e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 902 NKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNtktaetsl 981
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 982 peiqKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKlhpvednpvetvavlsqEEL 1061
Cdd:COG1579 89 ----KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK-----------------AEL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 29789347 1062 EAIKnpESITNEIALLEAQCREMKPNLGA--IAEYKK 1096
Cdd:COG1579 148 DEEL--AELEAELEELEAEREELAAKIPPelLALYER 182
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
813-1131 |
3.34e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 813 RNTLEKFAA--SIQGLSEQEEYLCVQIKE-LEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTI 889
Cdd:pfam12128 305 ELNGELSAAdaAVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 890 IDINNRKL----KAQQNKLDTINKQLDECASA------------------ITKAQVAIKTADRNLKKAQDSVCRTEKEIK 947
Cdd:pfam12128 385 KEQNNRDIagikDKLAKIREARDRQLAVAEDDlqaleselreqleagkleFNEEEYRLKSRLGELKLRLNQATATPELLL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 948 DTE---KEINDLKTEL----KNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQID 1020
Cdd:pfam12128 465 QLEnfdERIERAREEQeaanAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEA 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1021 GHISEHNSKIkywqkeISKIKLHPVEDNPVETVAVLSQE--------ELEAIKNPESITNEIAlLEAQCREMKPNLGAIA 1092
Cdd:pfam12128 545 PDWEQSIGKV------ISPELLHRTDLDPEVWDGSVGGElnlygvklDLKRIDVPEWAASEEE-LRERLDKAEEALQSAR 617
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 29789347 1093 EYKKKEDLYL-QRVAELDKITSERDNFRQAYE--DLRKQRLN 1131
Cdd:pfam12128 618 EKQAAAEEQLvQANGELEKASREETFARTALKnaRLDLRRLF 659
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
823-1271 |
3.46e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 823 IQGLSEQEEYLCVQIKELEANVLttapdrKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINnRKLKAQQN 902
Cdd:PHA02562 183 IQTLDMKIDHIQQQIKTYNKNIE------EQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLV-MDIEDPSA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 903 KLDTINkqldecaSAITKAQVAIKTADRNLKKAQD-SVCRTEKE-IKDTEKEINDLKTELKNIEDKAEEVinntktaets 980
Cdd:PHA02562 256 ALNKLN-------TAAAKIKSKIEQFQKVIKMYEKgGVCPTCTQqISEGPDRITKIKDKLKELQHSLEKL---------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 981 lpeiqKEHRnllQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDnpvetvavlsqee 1060
Cdd:PHA02562 319 -----DTAI---DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN------------- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1061 leaiknpesiTNEIALLEAQCREMKPNLGAIaeykKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMagfyvi 1140
Cdd:PHA02562 378 ----------AEELAKLQDELDKIVKTKSEL----VKEKYHRGIVTDLLKDSGIKASIIKKYIPYFNKQINHYL------ 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1141 tnKLKENYQMLTLggDAElelvdsldpFSEGImfsvrppKKSWKKIF---NLSGGEKTLSSLALVFA------LHHYKPT 1211
Cdd:PHA02562 438 --QIMEADYNFTL--DEE---------FNETI-------KSRGREDFsyaSFSQGEKARIDLALLFTwrdvasKVSGVDT 497
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789347 1212 PLYFMDEI-DAALDFKNVSIVaFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTK 1271
Cdd:PHA02562 498 NLLILDEVfDGALDAEGTKAL-LSILDSLKDTNVFVISHKDHDPQKFDRHLKMEKVGRFSV 557
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1127 |
6.75e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 851 RKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTI--IDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTA 928
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIneISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 929 DRNLKKAQDSVCRTEKEIKDTEKEINDLKT---ELKNIEDKAEEVInntktaetslpEIQKEHRNLLQELKVIQENEHAL 1005
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEkvkELKELKEKAEEYI-----------KLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1006 QKDALSIKLKLEQidghISEHNSKIKYWQKEISKIklhpvednpvetvavlsQEELEAIKNPESITNEIALLEAQCREMK 1085
Cdd:PRK03918 320 EEEINGIEERIKE----LEEKEERLEELKKKLKEL-----------------EKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 29789347 1086 PNLG------AIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRK 1127
Cdd:PRK03918 379 KRLTgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
870-1117 |
1.15e-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: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 870 AVAEKAGKVEAEIKRLhntiidinNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDT 949
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 950 EKEINDLKTELKNIEDKAEEVINNT-KTAETSLPEI---QKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISE 1025
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALyRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1026 HNSKIKYWQKEISKIKlhpvednpvETVAVLSQEELEAIKNPESITNEIALLEAQcremkpnlgaIAEYKKKEDLYLQRV 1105
Cdd:COG4942 169 LEAERAELEALLAELE---------EERAALEALKAERQKLLARLEKELAELAAE----------LAELQQEAEELEALI 229
|
250
....*....|..
gi 29789347 1106 AELDKITSERDN 1117
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
836-1031 |
1.21e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.39 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 836 QIKELEANVlttapdrkqQKLLEENvsvFKKEYDAVAEKAGKVEaeiKRLHNTIIDINNRKLKAQQNKLDTINKQLDECA 915
Cdd:pfam06160 212 QLEELKEGY---------REMEEEG---YALEHLNVDKEIQQLE---EQLEENLALLENLELDEAEEALEEIEERIDQLY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 916 SAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEI-----------------NDLKTELKNIEDKAEEVINNTKTAE 978
Cdd:pfam06160 277 DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELervqqsytlnenelervRGLEKQLEELEKRYDEIVERLEEKE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 979 TSLPEIQKEHRNLLQELKVIQENE-------HALQKDALSIKLKLEQIDGHISEHNSKIK 1031
Cdd:pfam06160 357 VAYSELQEELEEILEQLEEIEEEQeefkeslQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
88-575 |
1.23e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 88 QNFKSYAGEKVL--GPFHKRFsCIIGPNGSGKSNVIDSMLF-VFGyraqKIRSKKLSVLIHNSDEHKDIQSCTVEVHFQk 164
Cdd:TIGR00618 9 KNFGSYKGTHTIdfTALGPIF-LICGKTGAGKTTLLDAITYaLYG----KLPRRSEVIRSLNSLYAAPSEAAFAELEFS- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 165 iidKEGDDYEVLPNsnfYVSRTAYRDSTSVYHI-------------SGKKKTFKDVGNLLRshgidLDHNRF----LILQ 227
Cdd:TIGR00618 83 ---LGTKIYRVHRT---LRCTRSHRKTEQPEQLyleqkkgrgrilaAKKSETEEVIHDLLK-----LDYKTFtrvvLLPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 228 GEVEQIAMMKPKGQTEHDEGMLEY-------LEDIIGCGRLNEPIKVLCRRVEIL----NEHRGEKLNRVKMVEKEKDAL 296
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLdqytqlaLMEFAKKKSLHGKAELLTLRSQLLtlctPCMPDTYHERKQVLEKELKHL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 297 E---GEKNIAIEFLTLENEMFKKKNHIcQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKnsAVKDVEKK 373
Cdd:TIGR00618 232 RealQQTQQSHAYLTQKREAQEEQLKK-QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK--AVTQIEQQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 374 LNKVTKFIEQNKEKFTQLdLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREK 453
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKL-LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 454 EEKKLKEvMDSLKQETQGLQKEKEIQEKELMGFN--KSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKE-ALITASE 530
Cdd:TIGR00618 388 KTTLTQK-LQSLCKELDILQREQATIDTRTSAFRdlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQ 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 29789347 531 TLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINL-KSLVH 575
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLcGSCIH 512
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
836-981 |
1.29e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 836 QIKELEaNVLTTAPDRKQQklLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQnKLDTI--NKQLDE 913
Cdd:COG1579 18 ELDRLE-HRLKELPAELAE--LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVrnNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789347 914 CASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSL 981
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
880-1132 |
1.38e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 880 AEIKRLHNTIIDI---NNRKLKAQQNK--LDTINKQLDECASAITKAQVAIktadRNLKKAQDSVcRTEKEIKDTEKEIN 954
Cdd:COG3206 148 ELAAAVANALAEAyleQNLELRREEARkaLEFLEEQLPELRKELEEAEAAL----EEFRQKNGLV-DLSEEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 955 DLKTELKNIEDKAEEvinntktAETSLPEIQKEHRNLLQELKVIQENEH--ALQKDALSIKLKLEQIDGHISEHNSKIKY 1032
Cdd:COG3206 223 ELESQLAEARAELAE-------AEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1033 WQKEISKIKlhpvednpvetvAVLSQEELEAIknpESITNEIALLEAQCREMKpnlGAIAEYKKKEDLYLQRVAELDKIT 1112
Cdd:COG3206 296 LRAQIAALR------------AQLQQEAQRIL---ASLEAELEALQAREASLQ---AQLAQLEARLAELPELEAELRRLE 357
|
250 260
....*....|....*....|
gi 29789347 1113 SERDNFRQAYEDLRkQRLNE 1132
Cdd:COG3206 358 REVEVARELYESLL-QRLEE 376
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
221-606 |
1.95e-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: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 221 NRFLILQGEVEQIAMMKPKGQT---------EHDEGMLEYLEDIIGCGRlNEPIKVLCRRVEILnehRGEKLNRVKMVEK 291
Cdd:TIGR00606 444 LKKEILEKKQEELKFVIKELQQlegssdrilELDQELRKAERELSKAEK-NSLTETLKKEVKSL---QNEKADLDRKLRK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 292 EKDALEgEKNIAIEFLTlENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVE 371
Cdd:TIGR00606 520 LDQEME-QLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLN 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 372 KKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHAT------SKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNN 445
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYEDKLFDVCgsqdeeSDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 446 S---LEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIY----------LSRHN 512
Cdd:TIGR00606 678 SccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKekeipelrnkLQKVN 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 513 TAV----SQLSKAKEALITASETLKERKAAIKDInTKLPQTQQELKEKEKELQKLTQE--EINLKSLVHDLFQKVEEAKS 586
Cdd:TIGR00606 758 RDIqrlkNDIEEQETLLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKIAQQAAKlqGSDLDRTVQQVNQEKQEKQH 836
|
410 420
....*....|....*....|
gi 29789347 587 SLAMNRSRGKVLDAIIQEKK 606
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQ 856
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
781-1041 |
2.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 781 LERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQglseqEEYLCVQIKELEanvlttapdRKQQKLLEEN 860
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELE---------EKLKKYNLEE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 861 VSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDIN--NRKLKAQQNKLDTINKQLDECASAITKAQV-AIKTADRNLKKAQD 937
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEP 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 938 ------SVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQK-----EHRNlLQELKVIQENEHAlq 1006
Cdd:PRK03918 600 fyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEE-LREEYLELSRELA-- 676
|
250 260 270
....*....|....*....|....*....|....*
gi 29789347 1007 kdalSIKLKLEQIDGHISEHNSKIKYWQKEISKIK 1041
Cdd:PRK03918 677 ----GLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
260-1061 |
2.78e-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: 45.42 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 260 RLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEgEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAeITTQK 339
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQ-EHIRARDSLIQSLATRLELDGFERGPFSERQIKNF-HTLVI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 340 EKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLekqLQKD 419
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI---LELD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 420 KEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDslkQETQGLQKEKEIQEKELMgfnksvnEARSKMEV 499
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD---QEMEQLNHHTTTRTQMEM-------LTKDKMDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 500 AQSELDIYLSRHNTAVSQL------SKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSL 573
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 574 VHD-------------LFQKVEEAKSSLAMNRSRGKVLDAIIQE---KKSGRIPgiygrlgdLGAIDEKYDIAISSCCHA 637
Cdd:TIGR00606 628 LFDvcgsqdeesdlerLKEEIEKSSKQRAMLAGATAVYSQFITQltdENQSCCP--------VCQRVFQTEAELQEFISD 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 638 LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRL----FDLVKVKNEEIRQAFYFALRDT 713
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqkvnRDIQRLKNDIEEQETLLGTIMP 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 714 LVANNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEisVEEVNKMESQLERHSKqAMQIQE 793
Cdd:TIGR00606 780 EEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEK--QHELDTVVSKIELNRK-LIQDQQ 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 794 QKVQHEEAVVKLRHSERdmrNTLEKFAASIQGLSEQEEYLCVQIKEL---------EANVLTTAPDRKQQKLLE------ 858
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEK---LQIGTNLQRRQQFEEQLVELSTEVQSLireikdakeQDSPLETFLEKDQQEKEElisske 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 859 ENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNL--KKAQ 936
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtQKIQ 1013
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 937 DSVCRTEKEIKDTEKEINDLKTELKNiedkaeeviNNTKTAETSLPEIQKEHRNLLQELKVIQENEhalqkdalsiklkl 1016
Cdd:TIGR00606 1014 ERWLQDNLTLRKRENELKEVEEELKQ---------HLKEMGQMQVLQMKQEHQKLEENIDLIKRNH-------------- 1070
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 29789347 1017 EQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEEL 1061
Cdd:TIGR00606 1071 VLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTEL 1115
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
771-1160 |
2.83e-04 |
|
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: 45.49 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 771 VEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSE-RDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVlttAP 849
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL---SL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 850 DRKQQKLLEE-------NVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKqldecASAITkAQ 922
Cdd:pfam15921 396 EKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEK-----VSSLT-AQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 923 vaIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEdKAEEVINNTKTAETSLPEIQKEHrnlLQELKVIQENE 1002
Cdd:pfam15921 470 --LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-RAIEATNAEITKLRSRVDLKLQE---LQHLKNEGDHL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1003 HALQKDALSIKLKLEQIDGHISEHNSKIKYWQK------------EISKIKLHP-VEDNPVE--TVAVLSQEELEAIKNP 1067
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKeINDRRLElqEFKILKDKKDAKIREL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1068 ESITNEIALLEAQ-CREMKPNLGAIAEYKKKEDlylQRVAELDKITSERDNFRQAYEDLRKQRLNEfMAGFYVITNKLKe 1146
Cdd:pfam15921 624 EARVSDLELEKVKlVNAGSERLRAVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRNFRNK-SEEMETTTNKLK- 698
|
410
....*....|....
gi 29789347 1147 nyqMLTLGGDAELE 1160
Cdd:pfam15921 699 ---MQLKSAQSELE 709
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
824-1006 |
2.89e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 824 QGLSEQEEYLCVQIKEL---EANVLTTAPDRKQQKLLEENVSVfKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKL-KA 899
Cdd:pfam07111 59 QALSQQAELISRQLQELrrlEEEVRLLRETSLQQKMRLEAQAM-ELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLeEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 900 QQNKLDTINKQLDECASAITKAQ----VAIKTADRNLKKAQDSV----CRTEKEIKDTEKEINDLKTELKNIEDKAEEVI 971
Cdd:pfam07111 138 SQRELEEIQRLHQEQLSSLTQAHeealSSLTSKAEGLEKSLNSLetkrAGEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29789347 972 NNTKT-----AETSLPEIQK-----EHRNLLQELKVIQENEHALQ 1006
Cdd:pfam07111 218 TLVESlrkyvGEQVPPEVHSqtwelERQELLDTMQHLQEDRADLQ 262
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
82-123 |
3.31e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 44.38 E-value: 3.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 29789347 82 ITHIVNQNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDS 123
Cdd:COG1195 2 LKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEA 41
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
885-1102 |
3.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 885 LHNTIIDINNRKLKAQQNKLDTINKQLDE-CASAITKAQVAIKTAD---RNLKKAQDSVCRTEKEIKDTEKEINDLKTEL 960
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 961 KNIED--KAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHalqkdalsiklKLEQIDGHISEHNSKIKYWQKEIS 1038
Cdd:COG4717 119 EKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789347 1039 KIKLHPVEDNpVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYL 1102
Cdd:COG4717 188 LATEEELQDL-AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
102-236 |
3.97e-04 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 43.73 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 102 FHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK--IRSKKLSVLIH----NSDEHKdiqsctvevHFQKIIDKEGDDYEV 175
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGGRASAdlIRSGAEKAVVEgvfdISDEEE---------AKALLLELGIEDDDD 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789347 176 LpnsnfYVSRTAYRDSTSVYHISGK---KKTFKDVGNLL------RSHGIDLDHNRFL-ILQGEVEQIAMM 236
Cdd:cd03241 90 L-----IIRREISRKGRSRYFINGQsvtLKLLRELGSLLvdihgqHDHQNLLNPERQLdLLDGGLDDVEFL 155
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
288-575 |
4.10e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 288 MVEKEKDALEGEKNIAIEFLTLENEMFKKKNHIcqyyiydLQNRIAEITTQKEKIHEDTKEIteksnvlsnEMKAKNSAV 367
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKRLNEN-------ANNLIKQFENTKEKIAEYTKSI---------DIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 368 KDVEKKLNKVTKFIEQNKEKFTQLDledvQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSL 447
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETETGIQ----NLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 448 EKEREKEEKKLKEVMDSLKQetqgLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD-----IYLSRHNTAVSQLSKAK 522
Cdd:COG5185 391 ESLDEIPQNQRGYAQEILAT----LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNeliseLNKVMREADEESQSRLE 466
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 29789347 523 EALITASETLKERKAAIKDINTKLPQTQQELKEK-EKELQKLTQEEINLKSLVH 575
Cdd:COG5185 467 EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATlEKLRAKLERQLEGVRSKLD 520
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
678-1072 |
4.64e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.83 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 678 KMSKIQTPENTPRLFDLVKVK-NEEIRQAFYFALRDTLVANN----LDQATRV--AYQRDRRWRVVTLQGQIIEQSGTMS 750
Cdd:NF012221 1438 RVSELDTYTNTSLYQDLSNLTaGEVIALSFDFARRAGLSTNNgievLWNGEVVfaSSGDASAWQQKTLKLTAKAGSNRLE 1517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 751 GGGSKVMRGrMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASiqglseqe 830
Cdd:NF012221 1518 FKGTGHNDG-LGYILDNVVATSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGS-------- 1588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 831 eylcvQiKELEANvlttapdrkQQKLLEENVSVfkkEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNK------- 903
Cdd:NF012221 1589 -----Q-SQLEST---------DQNALETNGQA---QRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGdqwrnpf 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 904 ----LDTINKQLDECASAITKAQVAIKTA-DRNLKKAQDSVC-------RTEKEIKDTEKEINDLKTELKNIEDKAEEVI 971
Cdd:NF012221 1651 agglLDRVQEQLDDAKKISGKQLADAKQRhVDNQQKVKDAVAkseagvaQGEQNQANAEQDIDDAKADAEKRKDDALAKQ 1730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 972 NNTKTAET-SLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIK---YWQKEISKIKLHPVED 1047
Cdd:NF012221 1731 NEAQQAESdANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNRQGAAGSGLSgkaYSVEGVAEPGSHINPD 1810
|
410 420
....*....|....*....|....*....
gi 29789347 1048 NPVET----VAVLSQEELEAIKNPESITN 1072
Cdd:NF012221 1811 SPAAAdgrfSEGLTEQEQEALEGATNAVN 1839
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
350-603 |
5.13e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 350 TEKSNVL----SNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVqvrEKLKHATSKAKKLEKQLQKDKEKVEE 425
Cdd:PRK01156 464 EEKSNHIinhyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEI---NKSINEYNKIESARADLEDIKIKINE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 426 LKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETqgLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD 505
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIET--NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 506 IYLSRHNTAVSQLSKAK---EALITASETL--------------KERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEI 568
Cdd:PRK01156 619 KSIREIENEANNLNNKYneiQENKILIEKLrgkidnykkqiaeiDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698
|
250 260 270
....*....|....*....|....*....|....*
gi 29789347 569 NLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQ 603
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
81-127 |
5.79e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.49 E-value: 5.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 29789347 81 MITHIVNQNFKSYAGEKVL-----GPFHKRFSCIIGPNGSGKSNVIDSMLFV 127
Cdd:COG1106 1 MLISFSIENFRSFKDELTLsmvasGLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
779-1021 |
7.85e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 779 SQLERHSKQamQIQEQKVQHEEAVVKLRHSERDMRNTLEK---FAASIQGLSEQEEylcvqikELEANVLTTAPDRKQQK 855
Cdd:pfam05557 12 SQLQNEKKQ--MELEHKRARIELEKKASALKRQLDRESDRnqeLQKRIRLLEKREA-------EAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 856 LLEENVSVFKKEYDAVAEKAGKVEAEIK---RLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKtadrNL 932
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKnelSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 933 KKAQDSVCRTEKEIKDTEKEI---NDLKTELKNIEDKAEevinntktaetSLPEIQKEHRNLLQE---LKVIQENEHALQ 1006
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELEFEIqsqEQDSEIVKNSKSELA-----------RIPELEKELERLREHnkhLNENIENKLLLK 227
|
250
....*....|....*
gi 29789347 1007 KDALSIKLKLEQIDG 1021
Cdd:pfam05557 228 EEVEDLKRKLEREEK 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-566 |
8.44e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 327 DLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEkftqldledvqvreklkhat 406
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 407 sKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEiqekelmgf 486
Cdd:COG4942 91 -EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 487 nkSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKealitasetlKERKAAIKDINTKLPQTQQELKEKEKELQKLTQE 566
Cdd:COG4942 161 --ELAALRAELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
768-1126 |
8.96e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 768 EISVEEVNKMESQLERHSKQAMQIQEQkvqhEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTT 847
Cdd:PRK02224 230 EQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 848 APDRK----QQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQqNKLDTINKQLDECASAITKAQV 923
Cdd:PRK02224 306 DADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR-EEAAELESELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 924 AIKTadrnlkkaqdsvcrTEKEIKDTEKEINDLKTELKNIEDKAEEVINN-------TKTAETSLPEIQK---EHRNLLQ 993
Cdd:PRK02224 385 EIEE--------------LEEEIEELRERFGDAPVDLGNAEDFLEELREErdelrerEAELEATLRTARErveEAEALLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 994 ELKV------IQENEHA------------LQKDALSIKLKLEQIDGHIsEHNSKIKYWQKEISKIKlhpvedNPVETVav 1055
Cdd:PRK02224 451 AGKCpecgqpVEGSPHVetieedrerveeLEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLE------ERREDL-- 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789347 1056 lsqEELEAIKnpESITNEIALLEAQCREMKPNLGAIAEYKKKE--------DLYLQRVAELDKITSERDNFRQAYEDLR 1126
Cdd:PRK02224 522 ---EELIAER--RETIEEKRERAEELRERAAELEAEAEEKREAaaeaeeeaEEAREEVAELNSKLAELKERIESLERIR 595
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
779-987 |
9.44e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 779 SQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTapdRKQQKLLE 858
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 859 ENVSVFKKEYD---AVAEKAGKVEAEIKRLHNTIIDINNRKL-------KAQQNKLDTINKQLDECASAITKAQVAIKTA 928
Cdd:COG4942 97 AELEAQKEELAellRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789347 929 DRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKE 987
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
763-1114 |
1.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 763 SSVIDEISvEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKfaasIQGLSEQEEYLCVQIKELEA 842
Cdd:PRK03918 206 LREINEIS-SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK----IRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 843 NVL---TTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINN--RKLKAQQNKLDTINKQLDECASA 917
Cdd:PRK03918 281 KVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 918 IT---------------KAQVAIKTADRnLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLP 982
Cdd:PRK03918 361 HElyeeakakkeelerlKKRLTGLTPEK-LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 983 ----EIQKEHR------------NLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHN--SKIKYWQKEISKIKLHP 1044
Cdd:PRK03918 440 vcgrELTEEHRkelleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEE 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1045 VEDNpvetvavlsQEELEAIKnpesitNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSE 1114
Cdd:PRK03918 520 LEKK---------AEEYEKLK------EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
88-256 |
1.20e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.33 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 88 QNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNS--DEHKDIQSCTVEVHFQKI 165
Cdd:pfam13476 4 ENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDirIGLEGKGKAYVEITFENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 166 IDKEGDDYEVLPNSNFYVSRTAYRDSTSVYHISGKKKTFKDvgnllrSHGIDLDHNRFLILQGEvEQIAMMKPKGQTEHD 245
Cdd:pfam13476 82 DGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISE------LLKSDKIILPLLVFLGQ-EREEEFERKEKKERL 154
|
170
....*....|.
gi 29789347 246 EGMLEYLEDII 256
Cdd:pfam13476 155 EELEKALEEKE 165
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
888-962 |
1.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789347 888 TIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKN 962
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
817-1271 |
1.38e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 817 EKFAASIQGLSEQEEYLCVQIKELEANVLTTAPDRKQQKLLEENVSVFK-KEYDAVAEKAGKVEAEIKRLHNTIIDINNR 895
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELKDK 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 896 KLKAQQnkldtinkqLDECASAITKAQVAIKTADRNLKKAQdsvcRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTK 975
Cdd:PRK01156 545 HDKYEE---------IKNRYKSLKLEDLDSKRTSWLNALAV----ISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFP 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 976 TAET----SLPEIQKEHRNLLQELKVIQENehalqkdalsiKLKLEQIDGhisehnsKIKYWQKEISKIKlhPVEDNPVE 1051
Cdd:PRK01156 612 DDKSyidkSIREIENEANNLNNKYNEIQEN-----------KILIEKLRG-------KIDNYKKQIAEID--SIIPDLKE 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1052 TVAVLSQeeleaiknpesITNEIALLEAQCREMKPNLgaiAEYKKKEDLYLQRVAELDKITSERD-------NFRQAYED 1124
Cdd:PRK01156 672 ITSRIND-----------IEDNLKKSRKALDDAKANR---ARLESTIEILRTRINELSDRINDINetlesmkKIKKAIGD 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1125 LRKQRLNEFMAGFYVITNKLKENYqMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSW-KKIFNLSGGEKTLSSLALVF 1203
Cdd:PRK01156 738 LKRLREAFDKSGVPAMIRKSASQA-MTSLTRKYLFEFNLDFDDIDVDQDFNITVSRGGMvEGIDSLSGGEKTAVAFALRV 816
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789347 1204 ALHHY--KPTPLYFMDEIDAALDFKNVS----IVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTK 1271
Cdd:PRK01156 817 AVAQFlnNDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSK 890
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
766-1129 |
1.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 766 IDEISVEEVNKMESQLerhsKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVL 845
Cdd:COG4717 65 KPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 846 TTAPDRKQQKLLEEnvsvfKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAI 925
Cdd:COG4717 141 LAELPERLEELEER-----LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 926 KTADRNLKKAQDSVCRTEKE--IKDTEKEINDLKTEL-------------KNIEDKAEEVIN-------------NTKTA 977
Cdd:COG4717 216 EEAQEELEELEEELEQLENEleAAALEERLKEARLLLliaaallallglgGSLLSLILTIAGvlflvlgllallfLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 978 ETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQID-----GHISEHNSKIKYWQKEISKIKLHPVED---NP 1049
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllellDRIEELQELLREAEELEEELQLEELEQeiaAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1050 VETVAVLSQEELEAI----KNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYlqrvAELDKITSERDNFRQAYEDL 1125
Cdd:COG4717 376 LAEAGVEDEEELRAAleqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELE----EELEELEEELEELEEELEEL 451
|
....
gi 29789347 1126 RKQR 1129
Cdd:COG4717 452 REEL 455
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
404-589 |
1.81e-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: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 404 HATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRnnslekerekeekklkevMDSLKQETQGLQKEKEIQEKEL 483
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE------------------YNELQAELEALQAEIDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 484 MGFNKSVNEARSKME----------VAQSELDIYLSRHN--------TAVSQLSKAKEALI----TASETLKERKAAIKD 541
Cdd:COG3883 75 AEAEAEIEERREELGeraralyrsgGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLeelkADKAELEAKKAELEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29789347 542 INTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLA 589
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
779-1122 |
1.99e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 779 SQLERHSKQAMQIQEQKVQHEEAVVKLRHSERD---------MRNTLEKFAASIQGLSEQEEYLCVQIKELeANVLTTAP 849
Cdd:pfam05667 207 SLLERNAAELAAAQEWEEEWNSQGLASRLTPEEyrkrkrtklLKRIAEQLRSAALAGTEATSGASRSAQDL-AELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 850 DRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIkrLHNTIIDINNRKLKaQQNKLDTINKQLDECASAITKAqvaiktad 929
Cdd:pfam05667 286 GSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSS--PPTKVETEEELQQQ-REEELEELQEQLEDLESSIQEL-------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 930 rnlkkaqdsvcrtekeikdtEKEINDLKTELKNIEDKAEEvinnTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDA 1009
Cdd:pfam05667 355 --------------------EKEIKKLESSIKQVEEELEE----LKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1010 LSIKLKLEQIDGHISEHNSKIkywqkeISKIKLHPVEdnpvetvavLSQEELEAiknpESITNEIALLEAQCREMkpnlg 1089
Cdd:pfam05667 411 DASAQRLVELAGQWEKHRVPL------IEEYRALKEA---------KSNKEDES----QRKLEEIKELREKIKEV----- 466
|
330 340 350
....*....|....*....|....*....|...
gi 29789347 1090 aIAEYKKKEDLYLQRVAELDKITseRDNFRQAY 1122
Cdd:pfam05667 467 -AEEAKQKEELYKQLVAEYERLP--KDVSRSAY 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
873-1041 |
2.39e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 873 EKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKE 952
Cdd:TIGR04523 60 DKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 953 INDLKTELKNIEDKAEEVINNTKtaetslpEIQKEHRNLLQELKVIQENEHALQKDALSIK---LKLEQIDGHISEHNSK 1029
Cdd:TIGR04523 140 IDKFLTEIKKKEKELEKLNNKYN-------DLKKQKEELENELNLLEKEKLNIQKNIDKIKnklLKLELLLSNLKKKIQK 212
|
170
....*....|..
gi 29789347 1030 IKYWQKEISKIK 1041
Cdd:TIGR04523 213 NKSLESQISELK 224
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
82-164 |
2.63e-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: 41.57 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 82 ITHIVNQNFKSYagEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQkiRSKKLSVLIHNSDEHkdiqsCTVEVH 161
Cdd:TIGR00611 3 LSRLELTDFRNY--DAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSH--RTSRDKPLIRFGAEA-----FVIEGR 73
|
...
gi 29789347 162 FQK 164
Cdd:TIGR00611 74 VSK 76
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
312-566 |
2.67e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 312 EMFKKKNHICQYYIYDLQNRIAEIT------TQKEKIHEDT----KEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFI 381
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEINDKEKQVSllliqiTEKENKMKDLtfllEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 382 EQNKEKFTQldleDVQVREKLKHATSKAKKLEKQLQKDKE-KVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKE 460
Cdd:pfam05483 299 EDIKMSLQR----SMSTQKALEEDLQIATKTICQLTEEKEaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 461 VMDSLKQETQGLQKE-KEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITAseTLKERKAAI 539
Cdd:pfam05483 375 NEDQLKIITMELQKKsSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIF--LLQAREKEI 452
|
250 260
....*....|....*....|....*..
gi 29789347 540 KDINTKLPQTQQELKEKEKELQKLTQE 566
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
242-610 |
2.72e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 242 TEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKL-NRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKnhi 320
Cdd:COG5022 806 LGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLiQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAER--- 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 321 cqyYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMkaknsaVKDVEKKLNKVTKfIEQNKEKftqLDLEDVQVRE 400
Cdd:COG5022 883 ---QLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDL------IENLEFKTELIAR-LKKLLNN---IDLEEGPSIE 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 401 klKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSlekerekeekklkevMDSLKQETQGLQKEKEIQE 480
Cdd:COG5022 950 --YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSE---------------LKNFKKELAELSKQYGALQ 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 481 KELmgfnKSVNEARSKMEVAQSELDIYLSRHnTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEK-E 559
Cdd:COG5022 1013 EST----KQLKELPVEVAELQSASKIISSES-TELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQlE 1087
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 29789347 560 LQKLTQEEINLKSLvhdLFQKVEEAKSS--LAMNRSRGKVLDAIIQEKKSGRI 610
Cdd:COG5022 1088 STENLLKTINVKDL---EVTNRNLVKPAnvLQFIVAQMIKLNLLQEISKFLSQ 1137
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
771-1066 |
2.76e-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: 41.93 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 771 VEEVNKMESQLERHSKQ-AMQIQEQKVQHEEAVVKLRHSE--------RDMRNTLEKFAASIQGLSEQEEYLCVQIKELE 841
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQlKSEISDLNNQKEQDWNKELKSElknqekklEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 842 ANVLTtapdrKQQKLLEEN--VSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINN------RKLKAQQNKLDTINKQLDE 913
Cdd:TIGR04523 356 SENSE-----KQRELEEKQneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlnqqkdEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 914 CASAITKAQVAIKtadrNLKKaQDSVcrTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQ 993
Cdd:TIGR04523 431 LKETIIKNNSEIK----DLTN-QDSV--KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789347 994 ELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNpVETVAVLSQEELEAIKN 1066
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN-LEKEIDEKNKEIEELKQ 575
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
850-1041 |
3.06e-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: 41.93 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 850 DRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINN--RKLKAQ------------------QNKLDTINK 909
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNkyNDLKKQkeelenelnllekeklniQKNIDKIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 910 QL-----------------DECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVIN 972
Cdd:TIGR04523 195 KLlklelllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789347 973 NTKTAETSLPEIQKEHRNLLQELKVI-----QENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIK 1041
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
270-559 |
3.16e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 270 RRVEILNEHRGEKLNRVKMVEKEKDAL--EGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITtqKEKIHEDTK 347
Cdd:PTZ00108 1032 KKKDLVKELKKLGYVRFKDIIKKKSEKitAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLT--KEKVEKLNA 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 348 EITEKSNVLSnemKAKNSAVKDVEKK-LNKVTKFIEQNKEKftqlDLEDVQVREKLKHATS-KAKKLEKQLQKDKEKVEE 425
Cdd:PTZ00108 1110 ELEKKEKELE---KLKNTTPKDMWLEdLDKFEEALEEQEEV----EEKEIAKEQRLKSKTKgKASKLRKPKLKKKEKKKK 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 426 LKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD 505
Cdd:PTZ00108 1183 KSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSS 1262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789347 506 IYLSRHN---TAVSQLSKAKEALITASETLKERK-------AAIKDINTKLPQTQQELKEKEKE 559
Cdd:PTZ00108 1263 DDLSKEGkpkNAPKRVSAVQYSPPPPSKRPDGESnggskpsSPTKKKVKKRLEGSLAALKKKKK 1326
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
106-206 |
3.48e-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: 41.22 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 106 FSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSK-KLSVLIHNSDEHKDIQSCTVEVHFQKIIDKEGDDyEVLPNSNFYVS 184
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTdERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLED-GVRYRYGLDLE 79
|
90 100
....*....|....*....|..
gi 29789347 185 RTAYRDSTSVYHISGKKKTFKD 206
Cdd:pfam13304 80 REDVEEKLSSKPTLLEKRLLLR 101
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
865-1018 |
3.75e-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: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 865 KKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQnKLDTINKQLDECASAITKAQVAIKTADRNLKKA--------- 935
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 936 --------------QDSVCRTE-------------KEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEH 988
Cdd:COG3883 101 svsyldvllgsesfSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190
....*....|....*....|....*....|
gi 29789347 989 RNLLQELKViQENEHALQKDALSIKLKLEQ 1018
Cdd:COG3883 181 EALLAQLSA-EEAAAEAQLAELEAELAAAE 209
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
82-126 |
3.83e-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: 40.74 E-value: 3.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 29789347 82 ITHIVNQNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDSMLF 126
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
81-152 |
4.17e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 4.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789347 81 MITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKD 152
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGD 73
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-606 |
4.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 268 LCRRvEILNEHRGEKLNR----VKMVEKE-KDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYD----LQNRIAEITTQ 338
Cdd:PRK03918 440 VCGR-ELTEEHRKELLEEytaeLKRIEKElKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeLEEKLKKYNLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 339 K-EKIHEDTKEITEKSNVLSNEMKAKNSAVK---DVEKKLNKVTKFIEQNKEKFTQL----------DLEDVQVREK--- 401
Cdd:PRK03918 519 ElEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEELAELlkeleelgfeSVEELEERLKele 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 402 --------LKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREkeekklkevmdslKQETQGLQ 473
Cdd:PRK03918 599 pfyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS-------------EEEYEELR 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 474 KEKEIQEKELMGFNKSVNEARSKMEVAQSELDiylsrhntavsqlsKAKEALitasETLKERKAAIKDINTKLPQTqQEL 553
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLE--------------KLKEEL----EEREKAKKELEKLEKALERV-EEL 726
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 29789347 554 KEKEKELQKLTQEEInlkslvhdlFQKVEEAKSSLAMNRSRGKVLDAIIQEKK 606
Cdd:PRK03918 727 REKVKKYKALLKERA---------LSKVGEIASEIFEELTEGKYSGVRVKAEE 770
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
903-1137 |
4.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 903 KLDTINKQLDECASAITKAQVAIktadrnlkkaqdsvcrteKEIKDTEKEINDLKTELKNIEDKAEEVInNTKTAETSLP 982
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERL------------------EALEAELDALQERREALQRLAEYSWDEI-DVASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 983 EIQKEHRNLLQ---ELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEI--SKIKLHPVEDNPVETVAVLS 1057
Cdd:COG4913 672 ELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdeLQDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 1058 QEELEAIKNP-------ESITNEIALLEAQCREMKPNL-GAIAEYKKKEDLYLQRV-----------AELDKITSER-DN 1117
Cdd:COG4913 752 EERFAAALGDaverelrENLEERIDALRARLNRAEEELeRAMRAFNREWPAETADLdadleslpeylALLDRLEEDGlPE 831
|
250 260
....*....|....*....|
gi 29789347 1118 FRQAYEDLRKQRLNEFMAGF 1137
Cdd:COG4913 832 YEERFKELLNENSIEFVADL 851
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
692-1048 |
4.64e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 692 FDLVKVKNEEIRQAFYFALR-DTLVANNLDQAtrvaYQR---DRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVID 767
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKeDHEKIQHLEEE----YKKeinDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 768 EISVEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMR-------NTLEKFAASIQGLSEQEEYLCVQIKEL 840
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEF 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 841 EANVLTTAPD-RKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINN-RKLKAQQNKLDTINKQLDECASAI 918
Cdd:pfam05483 355 EATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElKKILAEDEKLLDEKKQFEKIAEEL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 919 TKAQVAI----KTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQE 994
Cdd:pfam05483 435 KGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLE 514
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 995 LKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEIS------KIKLHPVEDN 1048
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevKCKLDKSEEN 574
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
836-969 |
5.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 836 QIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAE------KAGKVEAEIKRLHNTIidinnRKLKAQQNKLDTINK 909
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAEL-----ERLDASSDDLAALEE 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 910 QLDEcasaitkAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEE 969
Cdd:COG4913 693 QLEE-------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
271-586 |
6.04e-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: 40.87 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 271 RVE-ILNEHRGEKlnrVKMVEKEKDALEGEKNIAIEfLTLENEMFKKKNHICQYYIYDLQNRIAEITTQ---KEKIHEDT 346
Cdd:pfam15921 268 RIEqLISEHEVEI---TGLTEKASSARSQANSIQSQ-LEIIQEQARNQNSMYMRQLSDLESTVSQLRSElreAKRMYEDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 347 KEITEKSNVLSNemkaknsavkdvekklnkvTKFIEQNKEKfTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEL 426
Cdd:pfam15921 344 IEELEKQLVLAN-------------------SELTEARTER-DQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 427 KSVPAKSKTVIN----ETTTRNnslekereKEEKKLKEVMDSLKQETQGlqkEKEIQEKELMGFNKSvnearskmevaqs 502
Cdd:pfam15921 404 WDRDTGNSITIDhlrrELDDRN--------MEVQRLEALLKAMKSECQG---QMERQMAAIQGKNES------------- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 503 eldiyLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVE 582
Cdd:pfam15921 460 -----LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
....
gi 29789347 583 EAKS 586
Cdd:pfam15921 535 HLKN 538
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
381-560 |
6.08e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 381 IEQNKEKFTQLDLEDVQVREKL-----KHATSK-AKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRnnslekereke 454
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVeeveeRLERAEdLVEAEDRIERLEERREDLEELIAERRETIEEKRER----------- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 455 ekklkevMDSLKQETQGLQKEKEIQEK---ELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAkEALITASET 531
Cdd:PRK02224 539 -------AEELRERAAELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAI-ADAEDEIER 610
|
170 180
....*....|....*....|....*....
gi 29789347 532 LKERKAAIKDINTKLPQTQQELKEKEKEL 560
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKREL 639
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
270-587 |
6.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 270 RRVEilNEHRGEKLNRVKMVEK-EKDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIH--EDT 346
Cdd:PTZ00121 1218 RKAE--DAKKAEAVKKAEEAKKdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 347 KEITEKSNVLSNEMKAKNS--------AVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQK 418
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAkkadeakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 419 DKEKVEEL-KSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGfnKSVNEARSKM 497
Cdd:PTZ00121 1376 AKKKADAAkKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKA 1453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 498 EVAQSELDIylsrhNTAVSQLSKAKEALITASETLKERKAAIKDINTKlpQTQQELKEKEKELQKLTQEEINLKSLVHDL 577
Cdd:PTZ00121 1454 EEAKKAEEA-----KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
330
....*....|
gi 29789347 578 FQKVEEAKSS 587
Cdd:PTZ00121 1527 AKKAEEAKKA 1536
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
331-590 |
6.30e-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: 40.87 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 331 RIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLE-DVQVREkLKHAtska 409
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRvDLKLQE-LQHL---- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 410 KKLEKQLQKDKEKVEELKSVPAKSKTVINetttrnnslekEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKElmgfnks 489
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIE-----------ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 490 VNEARSKME---VAQSELDIYLSRHNTAVSQLSKAKEALITASEtlkERKAAIKDINTKLPQTQQELKEKEKELQKLTQE 566
Cdd:pfam15921 599 INDRRLELQefkILKDKKDAKIRELEARVSDLELEKVKLVNAGS---ERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
250 260
....*....|....*....|....
gi 29789347 567 EINLKSLVHDLFQKVEEAKSSLAM 590
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKM 699
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
88-181 |
8.02e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.17 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 88 QNFKSYAGEKVLG--PFHKR-FSCIIGPNGSGKSNVIDSMLF-VFGYRAQKIRSKKLSVLIHNSDehkdiqsCTVEVHFQ 163
Cdd:cd03279 9 KNFGPFREEQVIDftGLDNNgLFLICGPTGAGKSTILDAITYaLYGKTPRYGRQENLRSVFAPGE-------DTAEVSFT 81
|
90 100 110
....*....|....*....|....*....|..
gi 29789347 164 --------KIIDKEGDDYE------VLPNSNF 181
Cdd:cd03279 82 fqlggkkyRVERSRGLDYDqftrivLLPQGEF 113
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
352-569 |
9.47e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 352 KSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPA 431
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 432 KSKTVIN--------ETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELmgfnKSVNEARSKMEVAQSE 503
Cdd:COG3883 97 RSGGSVSyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL----AELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789347 504 LDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEIN 569
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
764-1063 |
9.83e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 764 SVIDEISvEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTL----EKFAASIQGLSEQEEYLCVQIKE 839
Cdd:PRK04778 105 HEINEIE-SLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLlanrFSFGPALDELEKQLENLEEEFSQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 840 LEAnvLTTAPD----RKQQKLLEENVSVFKKEYDavaekagKVEAEIKRLHNTIID-INN-----RKLKAQQNKLDT--I 907
Cdd:PRK04778 184 FVE--LTESGDyveaREILDQLEEELAALEQIME-------EIPELLKELQTELPDqLQElkagyRELVEEGYHLDHldI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 908 NKQLDECASAITKAQVAIKTADrnLKKAQDSVCRTEKEIKDT----EKEI---NDLKTELKNIEDKAEEVINNTKTAETS 980
Cdd:PRK04778 255 EKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQLydilEREVkarKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789347 981 LPEIQKEHR---NLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNpvETVAVLS 1057
Cdd:PRK04778 333 IDRVKQSYTlneSELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLS--EMLQGLR 410
|
....*.
gi 29789347 1058 QEELEA 1063
Cdd:PRK04778 411 KDELEA 416
|
|
| |
