|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
11-1202 |
0e+00 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 586.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 11 MITHIVNQNFKSYAgEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK-IRSKKLSVLIHnSDEHKDIQSCTVE 89
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKsLRSERLSDLIH-SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 90 VHFqkiidKEGDDYEVLPNSNFYVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 169
Cdd:pfam02463 79 ITF-----DNEDHELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 170 GQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKNH 249
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 250 ICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVR 329
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 330 EKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQ 409
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 410 EKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKE 489
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 490 LQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDIAISSCCHALD 569
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 570 YIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRLfdlvkvkneeirqafyfalrdtlvaNNL 649
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL-------------------------AQL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 650 DQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQKVQHE 729
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 730 EAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVE 809
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 810 AEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTE 889
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 890 LKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISK 969
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 970 IKLHPVEDNPVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSERDNFR 1049
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1050 QAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSL 1129
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVAL 1088
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720405097 1130 ALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTKS 1202
Cdd:pfam02463 1089 ALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
12-1193 |
2.64e-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: 414.85 E-value: 2.64e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 12 ITHIVNQNFKSYAGEKVLgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGY-RAQKIRSKKLSVLIHNSDEHKDIQSCTVEV 90
Cdd:TIGR02169 2 IERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLsSSKAMRAERLSDLISNGKNGQSGNEAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 91 HFQKIIDKEGDDYEVLpnsnfyVSRTAYRD-STSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFlILQGEVEQIAMMKPK 169
Cdd:TIGR02169 81 TFKNDDGKFPDELEVV------RRLKVTDDgKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 170 GQTEhdegmleYLEDIIGCGRLNEPIKVLCRRVEILnehrGEKLNRVKMVEKEK----DALEGEKNIAIEFLTLENEMFK 245
Cdd:TIGR02169 154 ERRK-------IIDEIAGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKrqqlERLRREREKAERYQALLKEKRE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 246 KKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFiEQN--KEKFTQLDL 323
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-EQLrvKEKIGELEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 324 EDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKklkeVMDSLKQETQGLQ 403
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----ELEDLRAELEEVD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 404 KEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEAL------ITASETLKERKAA-IKDINTKL 476
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagieakINELEEEKEDKALeIKKQEWKL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 477 PQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGrIPGIYGRLGDLGAIDEK 556
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS-IQGVHGTVAQLGSVGER 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 557 YDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRLFDLVKVkNEEIRQA 635
Cdd:TIGR02169 537 YATAIEVAAGNrLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-DPKYEPA 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 636 FYFALRDTLVANNLDQATRVAYQrdrrWRVVTLQGQIIEQSGTMSGGgSKVMRGRMGSSVIDEISVEEVNKMESQLERHS 715
Cdd:TIGR02169 616 FKYVFGDTLVVEDIEAARRLMGK----YRMVTLEGELFEKSGAMTGG-SRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 716 KQAMQ-IQEQKVQHEEAVVKLRHSER---DMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVltTAPDRKQQKLleenv 791
Cdd:TIGR02169 691 SSLQSeLRRIENRLDELSQELSDASRkigEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI--ENVKSELKEL----- 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 792 svfKKEYDAVAEKAGKVEAEI----KRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQD 867
Cdd:TIGR02169 764 ---EARIEELEEDLHKLEEALndleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 868 SVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLE 947
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 948 QIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAIKNPESItneialleaqcremkpNLGAIAEYKKK 1027
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV----------------NMLAIQEYEEV 984
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1028 EDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTlGGDAELELVDSLDPFSEGIMFSVR 1107
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELILENPDDPFAGGLELSAK 1063
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1108 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEIS 1187
Cdd:TIGR02169 1064 PKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYA 1143
|
....*.
gi 1720405097 1188 DRLIGI 1193
Cdd:TIGR02169 1144 DRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-1193 |
7.13e-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: 353.21 E-value: 7.13e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 20 FKSYAgEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFqkiiD 97
Cdd:TIGR02168 10 FKSFA-DPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGeQSAKALRGGKMEDVIFNgSETRKPLSLAEVELVF----D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 98 KEGDDYEVLPNSNFYVSRTAYRDSTSVYHISGKKKTFKDVGNLL-------RSHGIdldhnrflILQGEVEQIAMMKPkg 170
Cdd:TIGR02168 85 NSDGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFldtglgkRSYSI--------IEQGKISEIIEAKP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 171 qtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILN--EHRGEKLNRV----KMVEKEKDALEGEKNIAIEFLTLENEMF 244
Cdd:TIGR02168 155 -----EERRAIFEEAAGISKYKE------RRKETERklERTRENLDRLedilNELERQLKSLERQAEKAERYKELKAELR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 245 KKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLE 324
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 325 DVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKErekeekklkevMDSLKQETQGLQK 404
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAELEELES 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 405 EKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRhntaVSQLSKAKEALITASETLKER--KAAIKDINTKLPQTQQE 482
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR----LERLEDRRERLQQEIEELLKKleEAELKELQAELEELEEE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 483 LKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQE------------KKSGRIPGIYGRLGDL 550
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsegvkallKNQSGLSGILGVLSEL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 551 GAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPR----LFDLV 625
Cdd:TIGR02168 529 ISVDEGYEAAIEAALGGrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvAKDLV 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 626 KVKnEEIRQAFYFALRDTLVANNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSV-IDEISvEEV 704
Cdd:TIGR02168 609 KFD-PKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRReIEELE-EKI 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 705 NKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRntlekfaasiQGLSEQEEylcvQIKELEANVLTTAPDRKQQ 784
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----------RQISALRK----DLARLEAEVEQLEERIAQL 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 785 KLLEENVSVFKKEYDAVAEKAGKVEAEIKRlhntiidinnrKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKK 864
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEA-----------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 865 AQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKL 944
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 945 KLEQIDGHISEHNSKIKYWQKEISKIKLHPVE-----DNPVETVAVLSQEELEAIKN--------PESITNEIALLEAQC 1011
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGlevriDNLQERLSEEYSLTLEEAEAlenkieddEEEARRRLKRLENKI 981
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1012 REMKP-NLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLKENYQMLTLGGDAELE 1090
Cdd:TIGR02168 982 KELGPvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELR 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1091 LVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTK 1170
Cdd:TIGR02168 1062 LTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSK 1141
|
1210 1220
....*....|....*....|...
gi 1720405097 1171 NAQFIIISLRNNMFEISDRLIGI 1193
Cdd:TIGR02168 1142 NTQFIVITHNKGTMEVADQLYGV 1164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-1193 |
4.61e-69 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 251.78 E-value: 4.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 12 ITHIVNQNFKSYAGEKVLgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG---YRAqkIRSKKLSVLIHN-SDEHKDIQSCT 87
Cdd:COG1196 3 LKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGeqsAKS--LRGGKMEDVIFAgSSSRKPLGRAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 88 VEVHF---QKIIDKEGDDYEvlpnsnfyVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLD-HNrfLILQGEVEQI 163
Cdd:COG1196 80 VSLTFdnsDGTLPIDYDEVT--------ITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPEsYS--IIGQGMIDRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 164 AMMKPkgqtehdEGMLEYLEDIIGCGRLNEpikvlcRRVEILNEHRG--EKLNRVK--MVEKEK--DALEGEKNIAIEFL 237
Cdd:COG1196 150 IEAKP-------EERRAIIEEAAGISKYKE------RKEEAERKLEAteENLERLEdiLGELERqlEPLERQAEKAERYR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 238 TLENEMFKKKNHICQYYIYDLQNRIAEITTQKEkihedtkEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEK 317
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELE-------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 318 FTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEV---MDS 394
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeeaLLE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 395 LKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINT 474
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 475 KLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSS----LAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDL 550
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARllllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 551 GAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVwAKKMSKIQTPENTPRLFDLVKVKN 629
Cdd:COG1196 530 IGVEAAYEAALEAALAAaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA-RAALAAALARGAIGAAVDLVASDL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 630 EEiRQAFYFALRDTLVANNLDQATRvayqRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEISVEEVNKMES 709
Cdd:COG1196 609 RE-ADARYYVLGDTLLGRTLVAARL----EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 710 QLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEAnvlttapdrkqqkLLEE 789
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE-------------LLEE 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 790 NVsvfkKEYDAVAEKAGKVEAEIKRLhntiidinnrklkaqqnkldtinkqldecasaitkaqvaiktadrnlkkaqdsv 869
Cdd:COG1196 751 EA----LEELPEPPDLEELERELERL------------------------------------------------------ 772
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 870 crtekeikdtEKEINDLktelkniedkaEEVinntktaetslpeiqkehrNL--LQELKVIQEnehalQKDALSiklklE 947
Cdd:COG1196 773 ----------EREIEAL-----------GPV-------------------NLlaIEEYEELEE-----RYDFLS-----E 802
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 948 QIDghisehnskikywqkeiskiklhpveDnpvetvavlsqeeleaiknpesitneiaLLEAqcremkpnlgaiaeykkK 1027
Cdd:COG1196 803 QRE--------------------------D----------------------------LEEA-----------------R 811
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1028 EDLyLQRVAELDKITSERdnFRQAYEDLRKQrlnefmagfyvitnkLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVR 1107
Cdd:COG1196 812 ETL-EEAIEEIDRETRER--FLETFDAVNEN---------------FQELFPRLFGGGEAELLLTDPDDPLETGIEIMAQ 873
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1108 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEIS 1187
Cdd:COG1196 874 PPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITHNKRTMEAA 953
|
....*.
gi 1720405097 1188 DRLIGI 1193
Cdd:COG1196 954 DRLYGV 959
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
10-169 |
1.67e-67 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 226.02 E-value: 1.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 10 LMITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVE 89
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHPNLDSCSVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 90 VHFQKIIDKEgddyevlpnsnfyvsrtayrdstsvyhisgkkktfkdvgnLLRSHGIDLDHNRFLILQGEVEQIAMMkPK 169
Cdd:cd03274 81 VHFQEIIDKP----------------------------------------LLKSKGIDLDHNRFLILQGEVEQIAQM-PK 119
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1109-1203 |
7.05e-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: 218.70 E-value: 7.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1109 PKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISD 1188
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAD 197
|
90
....*....|....*
gi 1720405097 1189 RLIGIYKTYNSTKSV 1203
Cdd:cd03274 198 RLVGIYKTNNCTKSV 212
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1119-1201 |
1.94e-32 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 124.34 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1119 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKN-AQFIIISLRNNMFEISDRLIGIYKTY 1197
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
....
gi 1720405097 1198 NSTK 1201
Cdd:cd03239 175 GVST 178
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
541-655 |
3.26e-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: 121.57 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 541 PGIYGRLGDLGAIDEKYDIAISSCCHA-LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTV-----WAKKMSKIQT 614
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGrLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPrspagSKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720405097 615 PENTPRLFDLVKVKnEEIRQAFYFALRDTLVANNLDQATRV 655
Cdd:smart00968 81 PGFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
18-170 |
5.34e-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: 125.38 E-value: 5.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 18 QNFKSYAGEKVLGPFhKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHN-SDEHKDIQSCTVEVHFQKii 96
Cdd:cd03275 7 ENFKSYKGRHVIGPF-DRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRaRVGKPDSNSAYVTAVYED-- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720405097 97 dkegDDYEVLpnsnfyVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKG 170
Cdd:cd03275 84 ----DDGEEK------TFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPPG 147
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1108-1195 |
1.71e-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: 118.44 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1108 PPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEI 1186
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEFFSK 224
|
....*....
gi 1720405097 1187 SDRLIGIYK 1195
Cdd:cd03275 225 ADALVGVYR 233
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
540-656 |
2.96e-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: 110.04 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 540 IPGIYGRLGDLGAIDEKYDIAISSCC-HALDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTpENT 618
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALgGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLK-GGA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720405097 619 PRLFDLVKVKnEEIRQAFYFALRDTLVANNLDQATRVA 656
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 ... |
1114-1193 |
1.14e-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: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1114 KKIFN---LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRL 1190
Cdd:cd03278 106 KKVQRlslLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
...
gi 1720405097 1191 IGI 1193
Cdd:cd03278 186 YGV 188
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
12-95 |
3.15e-27 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 109.32 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 12 ITHIVNQNFKSYAGEKVLGPFHkRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHnSDEHKDIQSCTVEVH 91
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSN-SFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAG-GGVKAGINSASVEIT 78
|
....
gi 1720405097 92 FQKI 95
Cdd:cd03239 79 FDKS 82
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1116-1196 |
1.07e-23 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 98.97 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1116 IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFEISDRLIGIY 1194
Cdd:cd03227 75 RLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIK 154
|
..
gi 1720405097 1195 KT 1196
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 ... |
12-92 |
7.84e-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: 80.20 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 12 ITHIVNQNFKSYAGEKVLgPFHKRFSCIIGPNGSGKSNVIDSMLFVFG-YRAQKIRSKKLSVLIHNSDEHKDIQS-CTVE 89
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGeQSAKSLRGEKMSDVIFAGSETRKPANfAEVT 79
|
...
gi 1720405097 90 VHF 92
Cdd:cd03278 80 LTF 82
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1114-1193 |
1.37e-16 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 80.77 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1114 KKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGI 1193
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGV 233
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1113-1198 |
2.46e-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: 80.03 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1113 WKK-IFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLi 1191
Cdd:cd03273 160 WKEsLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVL- 238
|
....*..
gi 1720405097 1192 giYKTYN 1198
Cdd:cd03273 239 --FRTRF 243
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
12-166 |
9.83e-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: 78.49 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 12 ITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRA-QKIRSKKLSVLIHNSDEhKDIQSCTVEV 90
Cdd:cd03273 3 IKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKRGQ-AGITKASVTI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720405097 91 HFqKIIDKEGDD--YEVLPnsNFYVSRTAYRDSTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMM 166
Cdd:cd03273 82 VF-DNSDKSQSPigFENYP--EITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVLNM 156
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-98 |
1.55e-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: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 14 HIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKklsvlihnSDEHKDIQSCTVEVHFQ 93
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRR--------SGVKAGCIVAAVSAELI 72
|
....*
gi 1720405097 94 KIIDK 98
Cdd:cd03227 73 FTRLQ 77
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
12-173 |
4.15e-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: 70.37 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 12 ITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIqSCTVEVH 91
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVM-SAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 92 FQKIidkegDDYEVLPNSNFYVSRT--AYRDStsvYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPK 169
Cdd:cd03272 80 FDNS-----DNRFPIDKEEVRLRRTigLKKDE---YFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQD 151
|
....
gi 1720405097 170 GQTE 173
Cdd:cd03272 152 EQQE 155
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
258-517 |
8.15e-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: 66.58 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 258 LQNRIAEITTQKEKIHEDTKEITE---KSNVLSNE-----MKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVR 329
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQlksEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 330 EKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEvmdsLKQETQGLQKEKEIQ 409
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ----KDEQIKKLQQEKELL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 410 EKE---LMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKakealitaseTLKERKAAIKDINTKLPQTQQELKEK 486
Cdd:TIGR04523 425 EKEierLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET----------QLKVLSRSINKIKQNLEQKQKELKSK 494
|
250 260 270
....*....|....*....|....*....|.
gi 1720405097 487 EKELQKLTQEEINLKSLVHDLFQKVEEAKSS 517
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
18-518 |
4.02e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 18 QNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDSmLFVFGYRAQKIRSKKLSvlihNSDEHKDIQSCT-VEVHFqkii 96
Cdd:PRK03918 9 KNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEA-ILVGLYWGHGSKPKGLK----KDDFTRIGGSGTeIELKF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 97 DKEGDDYEVLPNSNFYVSRTAYRDSTSVYHiSGKKKTFKDVGNLLRSHgidLDHNRFLILQGEVEQIammkpkgqTEHDE 176
Cdd:PRK03918 78 EKNGRKYRIVRSFNRGESYLKYLDGSEVLE-EGDSSVREWVERLIPYH---VFLNAIYIRQGEIDAI--------LESDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 177 GMLEYLEDIIGCGR-------LNEPIKVLCRRVEILNE---HRGEKLNRVKMVEKEKDALEGE-KNIAIEFLTLENEMFK 245
Cdd:PRK03918 146 SREKVVRQILGLDDyenayknLGEVIKEIKRRIERLEKfikRTENIEELIKEKEKELEEVLREiNEISSELPELREELEK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 246 KKNHICQY-----YIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQ 320
Cdd:PRK03918 226 LEKEVKELeelkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 321 LDlEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKevMDSLKQETQ 400
Cdd:PRK03918 306 LD-ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--LERLKKRLT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 401 GLQKEKEIQE-KELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKE------ALITA---SETLKERKAAIK 470
Cdd:PRK03918 383 GLTPEKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgRELTEehrKELLEEYTAELK 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1720405097 471 DINTKLPQTQQELKEKEKELQKLTQEEINLKSLV--HDLFQKVEEAKSSL 518
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKL 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
189-516 |
2.61e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 189 GRLNEPIKVLCRRVEILNEHR---GEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEI 265
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 266 TTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKlnkvtkfieQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQ 345
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA---------KGKCPVCGRELTEEHRKELLEEYTAELKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 346 LQKDKEKVEELKSVPAKSKTVINETTTrnnslekerEKEEKKLKEVMDSLKQETQGLQKEK-EIQEKELMGFNKSVNEAR 424
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESE---------LIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 425 SKMEVAQSELDiylsrhntAVSQLSKAKEALITASETLKERKAAIKDINTKLP-QTQQELKEKEKELQKLTQEEINLKSL 503
Cdd:PRK03918 539 GEIKSLKKELE--------KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDA 610
|
330
....*....|...
gi 1720405097 504 VHDLFQKVEEAKS 516
Cdd:PRK03918 611 EKELEREEKELKK 623
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1116-1195 |
2.83e-08 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 54.17 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1116 IFNLSGGEKTLSSLALVFALhhyKPtPLYFMDEIDAALDFKNVSIVAFYIYEQT-KNAQFIIISLRNNMFE-ISDRLIGI 1193
Cdd:cd00267 78 VPQLSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVL 153
|
..
gi 1720405097 1194 YK 1195
Cdd:cd00267 154 KD 155
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
11-57 |
3.94e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.86 E-value: 3.94e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1720405097 11 MITHIVNQNFKSYAG-EKVLGPFHkrfsCIIGPNGSGKSNVIDSMLFV 57
Cdd:COG4637 1 MITRIRIKNFKSLRDlELPLGPLT----VLIGANGSGKSNLLDALRFL 44
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
11-105 |
5.34e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 54.63 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 11 MITHIVNQNFKSYAGEKVLgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKiRSKKLSVLIHNSDEhkdiqSCTVEV 90
Cdd:COG0419 1 KLLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVGSE-----EASVEL 73
|
90
....*....|....*
gi 1720405097 91 HFQkiidKEGDDYEV 105
Cdd:COG0419 74 EFE----HGGKRYRI 84
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
277-970 |
1.42e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 277 KEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQK-------D 349
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKinseiknD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 350 KEKVEELKSVPAKSKTVINETT---TRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSK 426
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKkniDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 427 ---MEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKERkaaikdiNTKLPQTQQELKEKEKELQKLTQEEINLKSL 503
Cdd:TIGR04523 196 llkLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK-------QQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 504 VHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRL-GDLGAIDEKYDIAISSCCHAldyivVDSIDTAQEC 582
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN-----NKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 583 VNFLKKhnigiatfiglDKMTVWAKKMSK-IQTPENTPRLFDLVKVKNEEIRQAFYFALRDTLVANNLDQATRVAYQRDR 661
Cdd:TIGR04523 344 ISQLKK-----------ELTNSESENSEKqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 662 RWRVVTLQGQIIEQsgtmsgggskvmrgrmgssvideisveEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERD 741
Cdd:TIGR04523 413 QIKKLQQEKELLEK---------------------------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 742 MRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTapdRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIID 821
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL---NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 822 INNRKLKAQQN-KLDTINKQLDECASAITKaqvaIKTADRNLKKAQDSVcrtEKEIKDTEKEINDLKTELKNIEDKAEEV 900
Cdd:TIGR04523 543 LEDELNKDDFElKKENLEKEIDEKNKEIEE----LKQTQKSLKKKQEEK---QELIDQKEKEKKDLIKEIEEKEKKISSL 615
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 901 inntktaETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKI 970
Cdd:TIGR04523 616 -------EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
260-538 |
2.31e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 260 NRIAE--ITTQKEKIHEDTKEITEksnVLSNEMKAKNSAVKDVEKKLNKvtkFIEQNKekFTQLDLEDVQVREKLKHATS 337
Cdd:COG3206 155 NALAEayLEQNLELRREEARKALE---FLEEQLPELRKELEEAEAALEE---FRQKNG--LVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 338 KAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTrnnslekerekeekklKEVMDSLKQETQGLQKEKEIQEKELMGFN 417
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------SPVIQQLRAQLAELEAELAELSARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 418 KSVNEARSKMEVAQSELDiylSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQkltqee 497
Cdd:COG3206 291 PDVIALRAQIAALRAQLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE------ 361
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720405097 498 iNLKSLVHDLFQKVEEAKSSLAMNRSRGKVLD-AIIQEKKSG 538
Cdd:COG3206 362 -VARELYESLLQRLEEARLAEALTVGNVRVIDpAVVPLKPVS 402
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
701-1015 |
6.28e-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: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 701 VEEVNKMESQLErHSKQAMQIQEQKVQHEEAVVKLRHSE-RDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTAP 779
Cdd:pfam15921 481 VEELTAKKMTLE-SSERTVSDLTASLQEKERAIEATNAEiTKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 780 DRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNtiiDINNRKLKAQQ-----NKLDTINKQLDECASAITKAQVA 854
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEK---EINDRRLELQEfkilkDKKDAKIRELEARVSDLELEKVK 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 855 IKTAD-------RNLKKAQDSVCrteKEIKDTEKEINDLKTEL----KNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQ 923
Cdd:pfam15921 637 LVNAGserlravKDIKQERDQLL---NEVKTSRNELNSLSEDYevlkRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 924 ELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKI--KLHPVEdnpvETVAVLSQEELEAIKNPESIT 1001
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAnkEKHFLK----EEKNKLSQELSTVATEKNKMA 789
|
330
....*....|....
gi 1720405097 1002 NEIALLEAQCREMK 1015
Cdd:pfam15921 790 GELEVLRSQERRLK 803
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
316-1135 |
1.76e-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: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 316 EKFTQLDLEdvqVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETttrnnslekerekeekkLKEVMDSL 395
Cdd:TIGR00618 176 DQYTQLALM---EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKE-----------------LKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 396 KQETQGLQKEKEIQEKElmgfnksvnEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLK--ERKAAIKDIN 473
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQ---------EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 474 TKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLamnrsRGKVLDAIIQEKKSGRIPGIYGRLGDLGAI 553
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH-----SQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 554 dekydiaissccHALDYIvvdsIDTAQECVNFLKKHnigiatfigLDKMTVWAKKMSkIQTPENTPRLFDLVKVKNEEIR 633
Cdd:TIGR00618 382 ------------HTLQQQ----KTTLTQKLQSLCKE---------LDILQREQATID-TRTSAFRDLQGQLAHAKKQQEL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 634 QAFYFALRDTLVANNLDQAT-RVAYQRDRRWRVVTLqgqiIEQSGTMSGGGSKVMR-GRMGSSVIDEISVEE--VNKMES 709
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKlEKIHLQESAQSLKER----EQQLQTKEQIHLQETRkKAVVLARLLELQEEPcpLCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 710 QLERHSKQA----------MQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANV-LTTA 778
Cdd:TIGR00618 512 HPNPARQDIdnpgpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpNLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 779 PDRKQQKLLEENVSVFKKEydAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKL-------DTINKQLDECASAITKA 851
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDML--ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtalhalqLTLTQERVREHALSIRV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 852 QVAIKTADR-NLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVIN---------------NTKTAETSLPEIQ 915
Cdd:TIGR00618 670 LPKELLASRqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNeienassslgsdlaaREDALNQSLKELM 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 916 KEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAiK 995
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-Q 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 996 NPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMAGFYVITNKLK 1075
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRL 908
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720405097 1076 ENYQMLTLGGDAELELVDSLDPFSEGIMF------SVRPPKkswkkifNLSGGEKTLSSLALVFAL 1135
Cdd:TIGR00618 909 ANQSEGRFHGRYADSHVNARKYQGLALLVadaytgSVRPSA-------TLSGGETFLASLSLALAL 967
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
230-537 |
2.62e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 230 KNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSA----VKDVEKKLN 305
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEnsekQRELEEKQN 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 306 KVTKFIEQNKEKFTQLDLEDVQVREkLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEE 385
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 386 KKLKEVMDSLKqetqglqKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASETLKER 465
Cdd:TIGR04523 450 SVKELIIKNLD-------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720405097 466 KAAIKDINTKLPQTQQELKEKEKELQKLTQE--EINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKS 537
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-534 |
7.83e-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: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 311 IEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRnnslekerekeekklke 390
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 391 vMDSLKQETQGLQKEKEIQEKELMGFNKSV--NEARSKMEV---AQSELDIYlsRHNTAVSQLSKAKEALITA-SETLKE 464
Cdd:COG4942 85 -LAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALllsPEDFLDAV--RRLQYLKYLAPARREQAEElRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 465 RKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQE 534
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
786-1065 |
8.55e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 786 LLEENVSVFKKEYDAVAEKAGKVEAEIKRLhNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKA 865
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQA-REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 866 QDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLK 945
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 946 LEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYK 1025
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720405097 1026 KKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMA 1065
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
767-1064 |
1.41e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 767 IKELEaNVLTTAPDrkQQKLLEENVSVFKKEYDavaEKAGKVEAEikrlhNTIIDINNRKLKAQQNKLDTINKQLDECAS 846
Cdd:TIGR00606 697 ISDLQ-SKLRLAPD--KLKSTESELKKKEKRRD---EMLGLAPGR-----QSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 847 AITKAQVAIKTADRNLKKAQDSVC------RTEKEIKDTEKEINDLKTELKNIE---------DKAEEVINNTKTAETSL 911
Cdd:TIGR00606 766 DIEEQETLLGTIMPEEESAKVCLTdvtimeRFQMELKDVERKIAQQAAKLQGSDldrtvqqvnQEKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 912 PEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEEL 991
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 992 EAIKNPESITNEIALLEAQcrEMKPNLGAIAEYKK---------KEDLYLQRVAELDKITSERDNFRQayedlRKQRLNE 1062
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVN--DIKEKVKNIHGYMKdienkiqdgKDDYLKQKETELNTVNAQLEECEK-----HQEKINE 998
|
..
gi 1720405097 1063 FM 1064
Cdd:TIGR00606 999 DM 1000
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
826-1066 |
1.42e-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: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 826 KLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEvinntk 905
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 906 tAETSLPEIQKEHRNLLQELKVIQENEHA---LQKDALSIKLKLEQIDGHISEHNskikywQKEISKIKlhpvednpvet 982
Cdd:COG4942 95 -LRAELEAQKEELAELLRALYRLGRQPPLallLSPEDFLDAVRRLQYLKYLAPAR------REQAEELR----------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 983 vavLSQEELEAIKnpESITNEIALLEAQCREMKpnlgaiAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRK--QRL 1060
Cdd:COG4942 157 ---ADLAELAALR--AELEAERAELEALLAELE------EERAALEALKAERQKLLARLEKELAELAAELAELQQeaEEL 225
|
....*.
gi 1720405097 1061 NEFMAG 1066
Cdd:COG4942 226 EALIAR 231
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1119-1195 |
1.93e-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: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1119 LSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTK---NAQFIIISLRNNMFEISDRLIGIYK 1195
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKkqpGRQFIFITPQDISGLASSDDVKVFR 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
702-948 |
2.29e-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: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 702 EEVNKMESQLERHSKQAM---QIQEQKVQHEEAVVKLRHSERdMRNTLEKFAAsiqglseqeeylcvqikELEANVLtta 778
Cdd:COG4913 235 DDLERAHEALEDAREQIEllePIRELAERYAAARERLAELEY-LRAALRLWFA-----------------QRRLELL--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 779 pdRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTA 858
Cdd:COG4913 294 --EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 859 DRnlkkaqdSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETslpEIQKEHRNLLQELKVIQENEHALQKD 938
Cdd:COG4913 372 GL-------PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRKSNIPAR 441
|
250
....*....|
gi 1720405097 939 ALSIKLKLEQ 948
Cdd:COG4913 442 LLALRDALAE 451
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
832-1026 |
3.19e-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: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 832 NKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNtktaetsl 911
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 912 peiqKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKlhpvednpvetvavlsqEEL 991
Cdd:COG1579 89 ----KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK-----------------AEL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720405097 992 EAIKnpESITNEIALLEAQCREMKPNLGA--IAEYKK 1026
Cdd:COG1579 148 DEEL--AELEAELEELEAEREELAAKIPPelLALYER 182
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
743-1061 |
3.21e-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: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 743 RNTLEKFAA--SIQGLSEQEEYLCVQIKE-LEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTI 819
Cdd:pfam12128 305 ELNGELSAAdaAVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 820 IDINNRKL----KAQQNKLDTINKQLDECASA------------------ITKAQVAIKTADRNLKKAQDSVCRTEKEIK 877
Cdd:pfam12128 385 KEQNNRDIagikDKLAKIREARDRQLAVAEDDlqaleselreqleagkleFNEEEYRLKSRLGELKLRLNQATATPELLL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 878 DTE---KEINDLKTEL----KNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQID 950
Cdd:pfam12128 465 QLEnfdERIERAREEQeaanAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEA 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 951 GHISEHNSKIkywqkeISKIKLHPVEDNPVETVAVLSQE--------ELEAIKNPESITNEIAlLEAQCREMKPNLGAIA 1022
Cdd:pfam12128 545 PDWEQSIGKV------ISPELLHRTDLDPEVWDGSVGGElnlygvklDLKRIDVPEWAASEEE-LRERLDKAEEALQSAR 617
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720405097 1023 EYKKKEDLYL-QRVAELDKITSERDNFRQAYE--DLRKQRLN 1061
Cdd:pfam12128 618 EKQAAAEEQLvQANGELEKASREETFARTALKnaRLDLRRLF 659
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
12-98 |
3.27e-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: 47.69 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 12 ITHIVNQNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRaqkiRSKKLSVL-IHNSDEHKDIqSCTVEV 90
Cdd:COG3593 3 LEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPS----SSRKFDEEdFYLGDDPDLP-EIEIEL 75
|
....*...
gi 1720405097 91 HFQKIIDK 98
Cdd:COG3593 76 TFGSLLSR 83
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
264-523 |
3.27e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 264 EITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHatsKAKKLE 343
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ---KGDEVK 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 344 KQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKlkevMDSLKQETQGLQKEKEIQEKELMGFNKSVNEA 423
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN----IEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 424 RSKMEVAQSELDIYLSRHNTAVSQ--------LSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQ 495
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDkkiseeklLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE 721
|
250 260
....*....|....*....|....*...
gi 1720405097 496 EEINLKSLVHDLFQKVEEAKSSLAMNRS 523
Cdd:pfam05483 722 ERDSELGLYKNKEQEQSSAKAALEIELS 749
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
753-1201 |
6.89e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 753 IQGLSEQEEYLCVQIKELEANVLttapdrKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINnRKLKAQQN 832
Cdd:PHA02562 183 IQTLDMKIDHIQQQIKTYNKNIE------EQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLV-MDIEDPSA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 833 KLDTINkqldecaSAITKAQVAIKTADRNLKKAQD-SVCRTEKE-IKDTEKEINDLKTELKNIEDKAEEVinntktaets 910
Cdd:PHA02562 256 ALNKLN-------TAAAKIKSKIEQFQKVIKMYEKgGVCPTCTQqISEGPDRITKIKDKLKELQHSLEKL---------- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 911 lpeiqKEHRnllQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDnpvetvavlsqee 990
Cdd:PHA02562 319 -----DTAI---DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN------------- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 991 leaiknpesiTNEIALLEAQCREMKPNLGAIaeykKKEDLYLQRVAELDKITSERDNFRQAYEDLRKQRLNEFMagfyvi 1070
Cdd:PHA02562 378 ----------AEELAKLQDELDKIVKTKSEL----VKEKYHRGIVTDLLKDSGIKASIIKKYIPYFNKQINHYL------ 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1071 tnKLKENYQMLTLggDAElelvdsldpFSEGImfsvrppKKSWKKIF---NLSGGEKTLSSLALVFA------LHHYKPT 1141
Cdd:PHA02562 438 --QIMEADYNFTL--DEE---------FNETI-------KSRGREDFsyaSFSQGEKARIDLALLFTwrdvasKVSGVDT 497
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720405097 1142 PLYFMDEI-DAALDFKNVSIVaFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTK 1201
Cdd:PHA02562 498 NLLILDEVfDGALDAEGTKAL-LSILDSLKDTNVFVISHKDHDPQKFDRHLKMEKVGRFSV 557
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
781-1057 |
7.88e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 781 RKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTI--IDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTA 858
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIneISSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 859 DRNLKKAQDSVCRTEKEIKDTEKEINDLKT---ELKNIEDKAEEVInntktaetslpEIQKEHRNLLQELKVIQENEHAL 935
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEkvkELKELKEKAEEYI-----------KLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 936 QKDALSIKLKLEQidghISEHNSKIKYWQKEISKIklhpvednpvetvavlsQEELEAIKNPESITNEIALLEAQCREMK 1015
Cdd:PRK03918 320 EEEINGIEERIKE----LEEKEERLEELKKKLKEL-----------------EKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720405097 1016 PNLG------AIAEYKKKEDLYLQRVAELDKITSERDNFRQAYEDLRK 1057
Cdd:PRK03918 379 KRLTgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
800-1047 |
1.20e-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: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 800 AVAEKAGKVEAEIKRLhntiidinNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDT 879
Cdd:COG4942 17 AQADAAAEAEAELEQL--------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 880 EKEINDLKTELKNIEDKAEEVINNT-KTAETSLPEI---QKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISE 955
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALyRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 956 HNSKIKYWQKEISKIKlhpvednpvETVAVLSQEELEAIKNPESITNEIALLEAQcremkpnlgaIAEYKKKEDLYLQRV 1035
Cdd:COG4942 169 LEAERAELEALLAELE---------EERAALEALKAERQKLLARLEKELAELAAE----------LAELQQEAEELEALI 229
|
250
....*....|..
gi 1720405097 1036 AELDKITSERDN 1047
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
18-505 |
1.30e-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: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 18 QNFKSYAGEKVL--GPFHKRFsCIIGPNGSGKSNVIDSMLF-VFGyraqKIRSKKLSVLIHNSDEHKDIQSCTVEVHFQk 94
Cdd:TIGR00618 9 KNFGSYKGTHTIdfTALGPIF-LICGKTGAGKTTLLDAITYaLYG----KLPRRSEVIRSLNSLYAAPSEAAFAELEFS- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 95 iidKEGDDYEVLPNsnfYVSRTAYRDSTSVYHI-------------SGKKKTFKDVGNLLRshgidLDHNRF----LILQ 157
Cdd:TIGR00618 83 ---LGTKIYRVHRT---LRCTRSHRKTEQPEQLyleqkkgrgrilaAKKSETEEVIHDLLK-----LDYKTFtrvvLLPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 158 GEVEQIAMMKPKGQTEHDEGMLEY-------LEDIIGCGRLNEPIKVLCRRVEIL----NEHRGEKLNRVKMVEKEKDAL 226
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLdqytqlaLMEFAKKKSLHGKAELLTLRSQLLtlctPCMPDTYHERKQVLEKELKHL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 227 E---GEKNIAIEFLTLENEMFKKKNHIcQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKnsAVKDVEKK 303
Cdd:TIGR00618 232 RealQQTQQSHAYLTQKREAQEEQLKK-QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK--AVTQIEQQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 304 LNKVTKFIEQNKEKFTQLdLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREK 383
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKL-LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 384 EEKKLKEvMDSLKQETQGLQKEKEIQEKELMGFN--KSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKE-ALITASE 460
Cdd:TIGR00618 388 KTTLTQK-LQSLCKELDILQREQATIDTRTSAFRdlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQ 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1720405097 461 TLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINL-KSLVH 505
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLcGSCIH 512
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
766-911 |
1.33e-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: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 766 QIKELEaNVLTTAPDRKQQklLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQnKLDTI--NKQLDE 843
Cdd:COG1579 18 ELDRLE-HRLKELPAELAE--LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVrnNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720405097 844 CASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSL 911
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
766-961 |
1.46e-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: 46.00 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 766 QIKELEANVlttapdrkqQKLLEENvsvFKKEYDAVAEKAGKVEaeiKRLHNTIIDINNRKLKAQQNKLDTINKQLDECA 845
Cdd:pfam06160 212 QLEELKEGY---------REMEEEG---YALEHLNVDKEIQQLE---EQLEENLALLENLELDEAEEALEEIEERIDQLY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 846 SAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEI-----------------NDLKTELKNIEDKAEEVINNTKTAE 908
Cdd:pfam06160 277 DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELervqqsytlnenelervRGLEKQLEELEKRYDEIVERLEEKE 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 909 TSLPEIQKEHRNLLQELKVIQENE-------HALQKDALSIKLKLEQIDGHISEHNSKIK 961
Cdd:pfam06160 357 VAYSELQEELEEILEQLEEIEEEQeefkeslQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
810-1062 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 810 AEIKRLHNTIIDI---NNRKLKAQQNK--LDTINKQLDECASAITKAQVAIktadRNLKKAQDSVcrtekeikDTEKEIN 884
Cdd:COG3206 148 ELAAAVANALAEAyleQNLELRREEARkaLEFLEEQLPELRKELEEAEAAL----EEFRQKNGLV--------DLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 885 DLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEH--ALQKDALSIKLKLEQIDGHISEHNSKIKY 962
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 963 WQKEISKIKlhpvednpvetvAVLSQEELEAIknpESITNEIALLEAQCREMKpnlGAIAEYKKKEDLYLQRVAELDKIT 1042
Cdd:COG3206 296 LRAQIAALR------------AQLQQEAQRIL---ASLEAELEALQAREASLQ---AQLAQLEARLAELPELEAELRRLE 357
|
250 260
....*....|....*....|
gi 1720405097 1043 SERDNFRQAYEDLRkQRLNE 1062
Cdd:COG3206 358 REVEVARELYESLL-QRLEE 376
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
754-936 |
2.21e-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: 45.51 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 754 QGLSEQEEYLCVQIKEL---EANVLTTAPDRKQQKLLEENVSVfKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKL-KA 829
Cdd:pfam07111 59 QALSQQAELISRQLQELrrlEEEVRLLRETSLQQKMRLEAQAM-ELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLeEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 830 QQNKLDTI----NKQLDECASAITKAQVAIKTADRNLKKAQDSV----CRTEKEIKDTEKEINDLKTELKNIEDKAEEVI 901
Cdd:pfam07111 138 SQRELEEIqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLetkrAGEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720405097 902 NNTKT-----AETSLPEIQK-----EHRNLLQELKVIQENEHALQ 936
Cdd:pfam07111 218 TLVESlrkyvGEQVPPEVHSqtwelERQELLDTMQHLQEDRADLQ 262
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
701-1090 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 701 VEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSE-RDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVlttAP 779
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSElTEARTERDQFSQESGNLDDQLQKLLADLHKREKEL---SL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 780 DRKQQKLLEE-------NVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKqldecASAITkAQ 852
Cdd:pfam15921 396 EKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEK-----VSSLT-AQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 853 vaIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEdKAEEVINNTKTAETSLPEIQKEHrnlLQELKVIQENE 932
Cdd:pfam15921 470 --LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE-RAIEATNAEITKLRSRVDLKLQE---LQHLKNEGDHL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 933 HALQKDALSIKLKLEQIDGHISEHNSKIKYWQK------------EISKIKLHP-VEDNPVE--TVAVLSQEELEAIKNP 997
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamQVEKAQLEKeINDRRLElqEFKILKDKKDAKIREL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 998 ESITNEIALLEAQ-CREMKPNLGAIAEYKKKEDlylQRVAELDKITSERDNFRQAYEDLRKQRLNEfMAGFYVITNKLKe 1076
Cdd:pfam15921 624 EARVSDLELEKVKlVNAGSERLRAVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRNFRNK-SEEMETTTNKLK- 698
|
410
....*....|....
gi 1720405097 1077 nyqMLTLGGDAELE 1090
Cdd:pfam15921 699 ---MQLKSAQSELE 709
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
151-536 |
2.56e-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: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 151 NRFLILQGEVEQIAMMKPKGQT---------EHDEGMLEYLEDIIGCGRlNEPIKVLCRRVEILnehRGEKLNRVKMVEK 221
Cdd:TIGR00606 444 LKKEILEKKQEELKFVIKELQQlegssdrilELDQELRKAERELSKAEK-NSLTETLKKEVKSL---QNEKADLDRKLRK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 222 EKDALEgEKNIAIEFLTlENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVE 301
Cdd:TIGR00606 520 LDQEME-QLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLN 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 302 KKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHAT------SKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNN 375
Cdd:TIGR00606 598 KELASLEQNKNHINNELESKEEQLSSYEDKLFDVCgsqdeeSDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 376 S---LEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELDIY----------LSRHN 442
Cdd:TIGR00606 678 SccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKekeipelrnkLQKVN 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 443 TAV----SQLSKAKEALITASETLKERKAAIKDInTKLPQTQQELKEKEKELQKLTQE--EINLKSLVHDLFQKVEEAKS 516
Cdd:TIGR00606 758 RDIqrlkNDIEEQETLLGTIMPEEESAKVCLTDV-TIMERFQMELKDVERKIAQQAAKlqGSDLDRTVQQVNQEKQEKQH 836
|
410 420
....*....|....*....|
gi 1720405097 517 SLAMNRSRGKVLDAIIQEKK 536
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQ 856
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-971 |
2.98e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 711 LERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQglseqEEYLCVQIKELEanvlttapdRKQQKLLEEN 790
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELE---------EKLKKYNLEE 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 791 VSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDIN--NRKLKAQQNKLDTINKQLDECASAITKAQV-AIKTADRNLKKAQD 867
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEP 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 868 ------SVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQK-----EHRNlLQELKVIQENEHAlq 936
Cdd:PRK03918 600 fyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEE-LREEYLELSRELA-- 676
|
250 260 270
....*....|....*....|....*....|....*
gi 1720405097 937 kdalSIKLKLEQIDGHISEHNSKIKYWQKEISKIK 971
Cdd:PRK03918 677 ----GLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
12-53 |
3.48e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 44.38 E-value: 3.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1720405097 12 ITHIVNQNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDS 53
Cdd:COG1195 2 LKRLSLTNFRNYESLEL--EFSPGINVLVGPNGQGKTNLLEA 41
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
190-991 |
3.78e-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: 45.04 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 190 RLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEgEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAeITTQK 269
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQ-EHIRARDSLIQSLATRLELDGFERGPFSERQIKNF-HTLVI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 270 EKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLekqLQKD 349
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI---LELD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 350 KEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDslkQETQGLQKEKEIQEKELMgfnksvnEARSKMEV 429
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD---QEMEQLNHHTTTRTQMEM-------LTKDKMDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 430 AQSELDIYLSRHNTAVSQL------SKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSL 503
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 504 VHD-------------LFQKVEEAKSSLAMNRSRGKVLDAIIQE---KKSGRIPgiygrlgdLGAIDEKYDIAISSCCHA 567
Cdd:TIGR00606 628 LFDvcgsqdeesdlerLKEEIEKSSKQRAMLAGATAVYSQFITQltdENQSCCP--------VCQRVFQTEAELQEFISD 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 568 LDYIVVDSIDTAQECVNFLKKHNIGIATFIGLDKMTVWAKKMSKIQTPENTPRL----FDLVKVKNEEIRQAFYFALRDT 643
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqkvnRDIQRLKNDIEEQETLLGTIMP 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 644 LVANNLDQATRVAYQRDRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVIDEisVEEVNKMESQLERHSKqAMQIQE 723
Cdd:TIGR00606 780 EEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEK--QHELDTVVSKIELNRK-LIQDQQ 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 724 QKVQHEEAVVKLRHSERdmrNTLEKFAASIQGLSEQEEYLCVQIKEL---------EANVLTTAPDRKQQKLLE------ 788
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEK---LQIGTNLQRRQQFEEQLVELSTEVQSLireikdakeQDSPLETFLEKDQQEKEElisske 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 789 ENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNL--KKAQ 866
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtQKIQ 1013
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 867 DSVCRTEKEIKDTEKEINDLKTELKNiedkaeeviNNTKTAETSLPEIQKEHRNLLQELKVIQENEhalqkdalsiklkl 946
Cdd:TIGR00606 1014 ERWLQDNLTLRKRENELKEVEEELKQ---------HLKEMGQMQVLQMKQEHQKLEENIDLIKRNH-------------- 1070
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1720405097 947 EQIDGHISEHNSKIKYWQKEISKIKLHPVEDNPVETVAVLSQEEL 991
Cdd:TIGR00606 1071 VLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTEL 1115
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
815-1032 |
3.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 815 LHNTIIDINNRKLKAQQNKLDTINKQLDE-CASAITKAQVAIKTAD---RNLKKAQDSVCRTEKEIKDTEKEINDLKTEL 890
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 891 KNIED--KAEEVINNTKTAETSLPEIQKEHRNLLQELKVIQENEHalqkdalsiklKLEQIDGHISEHNSKIKYWQKEIS 968
Cdd:COG4717 119 EKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEE-----------ELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720405097 969 KIKLHPVEDNpVETVAVLSQEELEAIKNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYL 1032
Cdd:COG4717 188 LATEEELQDL-AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
32-166 |
4.29e-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: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 32 FHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQK--IRSKKLSVLIH----NSDEHKdiqsctvevHFQKIIDKEGDDYEV 105
Cdd:cd03241 19 FEEGLTVLTGETGAGKSILLDALSLLLGGRASAdlIRSGAEKAVVEgvfdISDEEE---------AKALLLELGIEDDDD 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720405097 106 LpnsnfYVSRTAYRDSTSVYHISGK---KKTFKDVGNLL------RSHGIDLDHNRFL-ILQGEVEQIAMM 166
Cdd:cd03241 90 L-----IIRREISRKGRSRYFINGQsvtLKLLRELGSLLvdihgqHDHQNLLNPERQLdLLDGGLDDVEFL 155
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
608-1002 |
4.35e-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: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 608 KMSKIQTPENTPRLFDLVKVK-NEEIRQAFYFALRDTLVANN----LDQATRV--AYQRDRRWRVVTLQGQIIEQSGTMS 680
Cdd:NF012221 1438 RVSELDTYTNTSLYQDLSNLTaGEVIALSFDFARRAGLSTNNgievLWNGEVVfaSSGDASAWQQKTLKLTAKAGSNRLE 1517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 681 GGGSKVMRGrMGSSVIDEISVEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASiqglseqe 760
Cdd:NF012221 1518 FKGTGHNDG-LGYILDNVVATSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGS-------- 1588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 761 eylcvQiKELEANvlttapdrkQQKLLEENVSVfkkEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNK------- 833
Cdd:NF012221 1589 -----Q-SQLEST---------DQNALETNGQA---QRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGdqwrnpf 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 834 ----LDTINKQLDECASAITKAQVAIKTA-DRNLKKAQDSVC-------RTEKEIKDTEKEINDLKTELKNIEDKAEEVI 901
Cdd:NF012221 1651 agglLDRVQEQLDDAKKISGKQLADAKQRhVDNQQKVKDAVAkseagvaQGEQNQANAEQDIDDAKADAEKRKDDALAKQ 1730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 902 NNTKTAET-SLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIK---YWQKEISKIKLHPVED 977
Cdd:NF012221 1731 NEAQQAESdANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNRQGAAGSGLSgkaYSVEGVAEPGSHINPD 1810
|
410 420
....*....|....*....|....*....
gi 1720405097 978 NPVET----VAVLSQEELEAIKNPESITN 1002
Cdd:NF012221 1811 SPAAAdgrfSEGLTEQEQEALEGATNAVN 1839
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
280-533 |
5.46e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 280 TEKSNVL----SNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVqvrEKLKHATSKAKKLEKQLQKDKEKVEE 355
Cdd:PRK01156 464 EEKSNHIinhyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEI---NKSINEYNKIESARADLEDIKIKINE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 356 LKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETqgLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD 435
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIET--NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 436 IYLSRHNTAVSQLSKAK---EALITASETL--------------KERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEI 498
Cdd:PRK01156 619 KSIREIENEANNLNNKYneiQENKILIEKLrgkidnykkqiaeiDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698
|
250 260 270
....*....|....*....|....*....|....*
gi 1720405097 499 NLKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQ 533
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
698-1056 |
5.93e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 698 EISVEEVNKMESQLERHSKQAMQIQEQkvqhEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTT 777
Cdd:PRK02224 230 EQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 778 APDRK----QQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQqNKLDTINKQLDECASAITKAQV 853
Cdd:PRK02224 306 DADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR-EEAAELESELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 854 AIKTadrnlkkaqdsvcrTEKEIKDTEKEINDLKTELKNIEDKAEEVINN-------TKTAETSLPEIQK---EHRNLLQ 923
Cdd:PRK02224 385 EIEE--------------LEEEIEELRERFGDAPVDLGNAEDFLEELREErdelrerEAELEATLRTARErveEAEALLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 924 ELKV------IQENEHA------------LQKDALSIKLKLEQIDGHIsEHNSKIKYWQKEISKIKlhpvedNPVETVav 985
Cdd:PRK02224 451 AGKCpecgqpVEGSPHVetieedrerveeLEAELEDLEEEVEEVEERL-ERAEDLVEAEDRIERLE------ERREDL-- 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720405097 986 lsqEELEAIKnpESITNEIALLEAQCREMKPNLGAIAEYKKKE--------DLYLQRVAELDKITSERDNFRQAYEDLR 1056
Cdd:PRK02224 522 ---EELIAER--RETIEEKRERAEELRERAAELEAEAEEKREAaaeaeeeaEEAREEVAELNSKLAELKERIESLERIR 595
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
218-505 |
6.04e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.18 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 218 MVEKEKDALEGEKNIAIEFLTLENEMFKKKNHIcqyyiydLQNRIAEITTQKEKIHEDTKEIteksnvlsnEMKAKNSAV 297
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLGENAESSKRLNEN-------ANNLIKQFENTKEKIAEYTKSI---------DIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 298 KDVEKKLNKVTKFIEQNKEKFTQLDledvQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSL 377
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETETGIQ----NLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 378 EKEREKEEKKLKEVMDSLKQetqgLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD-----IYLSRHNTAVSQLSKAK 452
Cdd:COG5185 391 ESLDEIPQNQRGYAQEILAT----LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNeliseLNKVMREADEESQSRLE 466
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1720405097 453 EALITASETLKERKAAIKDINTKLPQTQQELKEK-EKELQKLTQEEINLKSLVH 505
Cdd:COG5185 467 EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATlEKLRAKLERQLEGVRSKLD 520
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
11-57 |
7.32e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.11 E-value: 7.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720405097 11 MITHIVNQNFKSYAGEKVL-----GPFHKRFSCIIGPNGSGKSNVIDSMLFV 57
Cdd:COG1106 1 MLISFSIENFRSFKDELTLsmvasGLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
709-951 |
8.43e-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: 43.58 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 709 SQLERHSKQamQIQEQKVQHEEAVVKLRHSERDMRNTLEK---FAASIQGLSEQEEylcvqikELEANVLTTAPDRKQQK 785
Cdd:pfam05557 12 SQLQNEKKQ--MELEHKRARIELEKKASALKRQLDRESDRnqeLQKRIRLLEKREA-------EAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 786 LLEENVSVFKKEYDAVAEKAGKVEAEIK---RLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKtadrNL 862
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKnelSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ----NL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 863 KKAQDSVCRTEKEIKDTEKEI---NDLKTELKNIEDKAEevinntktaetSLPEIQKEHRNLLQE---LKVIQENEHALQ 936
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELEFEIqsqEQDSEIVKNSKSELA-----------RIPELEKELERLREHnkhLNENIENKLLLK 227
|
250
....*....|....*
gi 1720405097 937 KDALSIKLKLEQIDG 951
Cdd:pfam05557 228 EEVEDLKRKLEREEK 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
257-496 |
9.25e-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: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 257 DLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEkftqldledvqvreklkhat 336
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 337 sKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEiqekelmgf 416
Cdd:COG4942 91 -EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 417 nkSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKealitasetlKERKAAIKDINTKLPQTQQELKEKEKELQKLTQE 496
Cdd:COG4942 161 --ELAALRAELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
709-917 |
1.00e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 709 SQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVLTTapdRKQQKLLE 788
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 789 ENVSVFKKEYD---AVAEKAGKVEAEIKRLHNTIIDINNRKL-------KAQQNKLDTINKQLDECASAITKAQVAIKTA 858
Cdd:COG4942 97 AELEAQKEELAellRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720405097 859 DRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKE 917
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
818-892 |
1.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720405097 818 TIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKN 892
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
334-519 |
1.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 334 HATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRnnslekerekeekklkevMDSLKQETQGLQKEKEIQEKEL 413
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE------------------YNELQAELEALQAEIDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 414 MGFNKSVNEARSKME----------VAQSELDIYLSRHN--------TAVSQLSKAKEALI----TASETLKERKAAIKD 471
Cdd:COG3883 75 AEAEAEIEERREELGeraralyrsgGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLeelkADKAELEAKKAELEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720405097 472 INTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVEEAKSSLA 519
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
693-1044 |
1.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 693 SSVIDEISvEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKfaasIQGLSEQEEYLCVQIKELEA 772
Cdd:PRK03918 206 LREINEIS-SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK----IRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 773 NVL---TTAPDRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINN--RKLKAQQNKLDTINKQLDECASA 847
Cdd:PRK03918 281 KVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 848 IT---------------KAQVAIKTADRnLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLP 912
Cdd:PRK03918 361 HElyeeakakkeelerlKKRLTGLTPEK-LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 913 ----EIQKEHR------------NLLQELKVIQENEHALQKDALSIKLKLEQIDGHISEHN--SKIKYWQKEISKIKLHP 974
Cdd:PRK03918 440 vcgrELTEEHRkelleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEE 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 975 VEDNpvetvavlsQEELEAIKnpesitNEIALLEAQCREMKPNLGAIAEYKKKEDLYLQRVAELDKITSE 1044
Cdd:PRK03918 520 LEKK---------AEEYEKLK------EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
696-1059 |
1.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 696 IDEISVEEVNKMESQLerhsKQAMQIQEQKVQHEEAVVKLRHSERDMRNTLEKFAASIQGLSEQEEYLCVQIKELEANVL 775
Cdd:COG4717 65 KPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 776 TTAPDRKQQKLLEEnvsvfKKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAI 855
Cdd:COG4717 141 LAELPERLEELEER-----LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 856 KTADRNLKKAQDSVCRTEKE--IKDTEKEINDLKTEL-------------KNIEDKAEEVIN-------------NTKTA 907
Cdd:COG4717 216 EEAQEELEELEEELEQLENEleAAALEERLKEARLLLliaaallallglgGSLLSLILTIAGvlflvlgllallfLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 908 ETSLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQID-----GHISEHNSKIKYWQKEISKIKLHPVED---NP 979
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllellDRIEELQELLREAEELEEELQLEELEQeiaAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 980 VETVAVLSQEELEAI----KNPESITNEIALLEAQCREMKPNLGAIAEYKKKEDLYlqrvAELDKITSERDNFRQAYEDL 1055
Cdd:COG4717 376 LAEAGVEDEEELRAAleqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELE----EELEELEEELEELEEELEEL 451
|
....
gi 1720405097 1056 RKQR 1059
Cdd:COG4717 452 REEL 455
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
709-1052 |
2.05e-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: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 709 SQLERHSKQAMQIQEQKVQHEEAVVKLRHSERD---------MRNTLEKFAASIQGLSEQEEYLCVQIKELeANVLTTAP 779
Cdd:pfam05667 207 SLLERNAAELAAAQEWEEEWNSQGLASRLTPEEyrkrkrtklLKRIAEQLRSAALAGTEATSGASRSAQDL-AELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 780 DRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIkrLHNTIIDINNRKLKaQQNKLDTINKQLDECASAITKAqvaiktad 859
Cdd:pfam05667 286 GSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSS--PPTKVETEEELQQQ-REEELEELQEQLEDLESSIQEL-------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 860 rnlkkaqdsvcrtekeikdtEKEINDLKTELKNIEDKAEEvinnTKTAETSLPEIQKEHRNLLQELKVIQENEHALQKDA 939
Cdd:pfam05667 355 --------------------EKEIKKLESSIKQVEEELEE----LKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALV 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 940 LSIKLKLEQIDGHISEHNSKIkywqkeISKIKLHPVEdnpvetvavLSQEELEAiknpESITNEIALLEAQCREMkpnlg 1019
Cdd:pfam05667 411 DASAQRLVELAGQWEKHRVPL------IEEYRALKEA---------KSNKEDES----QRKLEEIKELREKIKEV----- 466
|
330 340 350
....*....|....*....|....*....|...
gi 1720405097 1020 aIAEYKKKEDLYLQRVAELDKITseRDNFRQAY 1052
Cdd:pfam05667 467 -AEEAKQKEELYKQLVAEYERLP--KDVSRSAY 496
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
18-186 |
2.11e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.56 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 18 QNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNS--DEHKDIQSCTVEVHFQKI 95
Cdd:pfam13476 4 ENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDirIGLEGKGKAYVEITFENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 96 IDKEGDDYEVLPNSNFYVSRTAYRDSTSVYHISGKKKTFKDvgnllrSHGIDLDHNRFLILQGEvEQIAMMKPKGQTEHD 175
Cdd:pfam13476 82 DGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISE------LLKSDKIILPLLVFLGQ-EREEEFERKEKKERL 154
|
170
....*....|.
gi 1720405097 176 EGMLEYLEDII 186
Cdd:pfam13476 155 EELEKALEEKE 165
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
747-1201 |
2.27e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 747 EKFAASIQGLSEQEEYLCVQIKELEANVLTTAPDRKQQKLLEENVSVFK-KEYDAVAEKAGKVEAEIKRLHNTIIDINNR 825
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELKDK 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 826 KLKAQQnkldtinkqLDECASAITKAQVAIKTADRNLKKAQdsvcRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTK 905
Cdd:PRK01156 545 HDKYEE---------IKNRYKSLKLEDLDSKRTSWLNALAV----ISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFP 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 906 TAET----SLPEIQKEHRNLLQELKVIQENehalqkdalsiKLKLEQIDGhisehnsKIKYWQKEISKIKlhPVEDNPVE 981
Cdd:PRK01156 612 DDKSyidkSIREIENEANNLNNKYNEIQEN-----------KILIEKLRG-------KIDNYKKQIAEID--SIIPDLKE 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 982 TVAVLSQeeleaiknpesITNEIALLEAQCREMKPNLgaiAEYKKKEDLYLQRVAELDKITSERD-------NFRQAYED 1054
Cdd:PRK01156 672 ITSRIND-----------IEDNLKKSRKALDDAKANR---ARLESTIEILRTRINELSDRINDINetlesmkKIKKAIGD 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 1055 LRKQRLNEFMAGFYVITNKLKENYqMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSW-KKIFNLSGGEKTLSSLALVF 1133
Cdd:PRK01156 738 LKRLREAFDKSGVPAMIRKSASQA-MTSLTRKYLFEFNLDFDDIDVDQDFNITVSRGGMvEGIDSLSGGEKTAVAFALRV 816
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720405097 1134 ALHHY--KPTPLYFMDEIDAALDFKNVS----IVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNSTK 1201
Cdd:PRK01156 817 AVAQFlnNDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSK 890
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
12-94 |
2.54e-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: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 12 ITHIVNQNFKSYagEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQkiRSKKLSVLIHNSDEHkdiqsCTVEVH 91
Cdd:TIGR00611 3 LSRLELTDFRNY--DAVDLELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSH--RTSRDKPLIRFGAEA-----FVIEGR 73
|
...
gi 1720405097 92 FQK 94
Cdd:TIGR00611 74 VSK 76
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
795-948 |
2.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 795 KKEYDAVAEKAGKVEAEIKRLHNTIIDINNRKLKAQQnKLDTINKQLDECASAITKAQVAIKTADRNLKKA--------- 865
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 866 --------------QDSVCRTE-------------KEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEH 918
Cdd:COG3883 101 svsyldvllgsesfSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190
....*....|....*....|....*....|
gi 1720405097 919 RNLLQELKViQENEHALQKDALSIKLKLEQ 948
Cdd:COG3883 181 EALLAQLSA-EEAAAEAQLAELEAELAAAE 209
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
242-496 |
2.85e-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: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 242 EMFKKKNHICQYYIYDLQNRIAEIT------TQKEKIHEDT----KEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFI 311
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEINDKEKQVSllliqiTEKENKMKDLtfllEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 312 EQNKEKFTQldleDVQVREKLKHATSKAKKLEKQLQKDKE-KVEELKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKE 390
Cdd:pfam05483 299 EDIKMSLQR----SMSTQKALEEDLQIATKTICQLTEEKEaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 391 VMDSLKQETQGLQKE-KEIQEKELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAKEALITAseTLKERKAAI 469
Cdd:pfam05483 375 NEDQLKIITMELQKKsSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIF--LLQAREKEI 452
|
250 260
....*....|....*....|....*..
gi 1720405097 470 KDINTKLPQTQQELKEKEKELQKLTQE 496
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
200-489 |
3.72e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.57 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 200 RRVEILNEHRGEKLNRVKMVEKEKDAL--EGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITtqKEKIHEDTK 277
Cdd:PTZ00108 1032 KKKDLVKELKKLGYVRFKDIIKKKSEKitAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLT--KEKVEKLNA 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 278 EITEKSNVLSnemKAKNSAVKDVEKK-LNKVTKFIEQNKEKftqlDLEDVQVREKLKHATS-KAKKLEKQLQKDKEKVEE 355
Cdd:PTZ00108 1110 ELEKKEKELE---KLKNTTPKDMWLEdLDKFEEALEEQEEV----EEKEIAKEQRLKSKTKgKASKLRKPKLKKKEKKKK 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 356 LKSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGFNKSVNEARSKMEVAQSELD 435
Cdd:PTZ00108 1183 KSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSS 1262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720405097 436 IYLSRHN---TAVSQLSKAKEALITASETLKERK-------AAIKDINTKLPQTQQELKEKEKE 489
Cdd:PTZ00108 1263 DDLSKEGkpkNAPKRVSAVQYSPPPPSKRPDGESnggskpsSPTKKKVKKRLEGSLAALKKKKK 1326
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
12-56 |
3.73e-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: 3.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1720405097 12 ITHIVNQNFKSYAGEKVlgPFHKRFSCIIGPNGSGKSNVIDSMLF 56
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
172-540 |
3.79e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 172 TEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKL-NRVKMVEKEKDALEGEKNIAIEFLTLENEMFKKKnhi 250
Cdd:COG5022 806 LGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLiQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAER--- 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 251 cqyYIYDLQNRIAEITTQKEKIHEDTKEITEKSNVLSNEMkaknsaVKDVEKKLNKVTKfIEQNKEKftqLDLEDVQVRE 330
Cdd:COG5022 883 ---QLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDL------IENLEFKTELIAR-LKKLLNN---IDLEEGPSIE 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 331 klKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSlekerekeekklkevMDSLKQETQGLQKEKEIQE 410
Cdd:COG5022 950 --YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSE---------------LKNFKKELAELSKQYGALQ 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 411 KELmgfnKSVNEARSKMEVAQSELDIYLSRHnTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEK-E 489
Cdd:COG5022 1013 EST----KQLKELPVEVAELQSASKIISSES-TELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQlE 1087
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1720405097 490 LQKLTQEEINLKSLvhdLFQKVEEAKSS--LAMNRSRGKVLDAIIQEKKSGRI 540
Cdd:COG5022 1088 STENLLKTINVKDL---EVTNRNLVKPAnvLQFIVAQMIKLNLLQEISKFLSQ 1137
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
803-971 |
4.13e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 803 EKAGKVEAEIKRLHNTIIDINNRKLKAQQNKLDTINKQLDECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKE 882
Cdd:TIGR04523 60 DKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 883 INDLKTELKNIEDKAEEVINNTKtaetslpEIQKEHRNLLQELKVIQENEHALQKDALSIK---LKLEQIDGHISEHNSK 959
Cdd:TIGR04523 140 IDKFLTEIKKKEKELEKLNNKYN-------DLKKQKEELENELNLLEKEKLNIQKNIDKIKnklLKLELLLSNLKKKIQK 212
|
170
....*....|..
gi 1720405097 960 IKYWQKEISKIK 971
Cdd:TIGR04523 213 NKSLESQISELK 224
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
36-136 |
4.15e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 36 FSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSK-KLSVLIHNSDEHKDIQSCTVEVHFQKIIDKEGDDyEVLPNSNFYVS 114
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTdERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLED-GVRYRYGLDLE 79
|
90 100
....*....|....*....|..
gi 1720405097 115 RTAYRDSTSVYHISGKKKTFKD 136
Cdd:pfam13304 80 REDVEEKLSSKPTLLEKRLLLR 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
833-1067 |
4.43e-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: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 833 KLDTINKQLDECASAITKAQVAIktadrnlkkaqdsvcrteKEIKDTEKEINDLKTELKNIEDKAEEVInNTKTAETSLP 912
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERL------------------EALEAELDALQERREALQRLAEYSWDEI-DVASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 913 EIQKEHRNLLQ---ELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEI--SKIKLHPVEDNPVETVAVLS 987
Cdd:COG4913 672 ELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdeLQDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 988 QEELEAIKNP-------ESITNEIALLEAQCREMKPNL-GAIAEYKKKEDLYLQRV-----------AELDKITSER-DN 1047
Cdd:COG4913 752 EERFAAALGDaverelrENLEERIDALRARLNRAEEELeRAMRAFNREWPAETADLdadleslpeylALLDRLEEDGlPE 831
|
250 260
....*....|....*....|
gi 1720405097 1048 FRQAYEDLRKQRLNEFMAGF 1067
Cdd:COG4913 832 YEERFKELLNENSIEFVADL 851
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
11-82 |
4.59e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 4.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720405097 11 MITHIVNQNFKSYAGEKVLGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKD 82
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGD 73
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
311-490 |
4.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 311 IEQNKEKFTQLDLEDVQVREKL-----KHATSK-AKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRnnslekereke 384
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVeeveeRLERAEdLVEAEDRIERLEERREDLEELIAERRETIEEKRER----------- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 385 ekklkevMDSLKQETQGLQKEKEIQEK---ELMGFNKSVNEARSKMEVAQSELDIYLSRHNTAVSQLSKAkEALITASET 461
Cdd:PRK02224 539 -------AEELRERAAELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAI-ADAEDEIER 610
|
170 180
....*....|....*....|....*....
gi 1720405097 462 LKERKAAIKDINTKLPQTQQELKEKEKEL 490
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKREL 639
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
766-899 |
5.11e-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: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 766 QIKELEANVLTTAPDRKQQKLLEENVSVFKKEYDAVAE------KAGKVEAEIKRLHNTIidinnRKLKAQQNKLDTINK 839
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAEL-----ERLDASSDDLAALEE 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 840 QLDEcasaitkAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEE 899
Cdd:COG4913 693 QLEE-------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
622-978 |
5.34e-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: 40.86 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 622 FDLVKVKNEEIRQAFYFALR-DTLVANNLDQAtrvaYQR---DRRWRVVTLQGQIIEQSGTMSGGGSKVMRGRMGSSVID 697
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKeDHEKIQHLEEE----YKKeinDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 698 EISVEEVNKMESQLERHSKQAMQIQEQKVQHEEAVVKLRHSERDMR-------NTLEKFAASIQGLSEQEEYLCVQIKEL 770
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEF 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 771 EANVLTTAPD-RKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINN-RKLKAQQNKLDTINKQLDECASAI 848
Cdd:pfam05483 355 EATTCSLEELlRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElKKILAEDEKLLDEKKQFEKIAEEL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 849 TKAQVAI----KTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQE 924
Cdd:pfam05483 435 KGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLE 514
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 925 LKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEIS------KIKLHPVEDN 978
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevKCKLDKSEEN 574
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
201-516 |
5.62e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 201 RVE-ILNEHRGEKlnrVKMVEKEKDALEGEKNIAIEfLTLENEMFKKKNHICQYYIYDLQNRIAEITTQ---KEKIHEDT 276
Cdd:pfam15921 268 RIEqLISEHEVEI---TGLTEKASSARSQANSIQSQ-LEIIQEQARNQNSMYMRQLSDLESTVSQLRSElreAKRMYEDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 277 KEITEKSNVLSNemkaknsavkdvekklnkvTKFIEQNKEKfTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEL 356
Cdd:pfam15921 344 IEELEKQLVLAN-------------------SELTEARTER-DQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 357 KSVPAKSKTVIN----ETTTRNnslekereKEEKKLKEVMDSLKQETQGlqkEKEIQEKELMGFNKSvnearskmevaqs 432
Cdd:pfam15921 404 WDRDTGNSITIDhlrrELDDRN--------MEVQRLEALLKAMKSECQG---QMERQMAAIQGKNES------------- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 433 eldiyLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEINLKSLVHDLFQKVE 512
Cdd:pfam15921 460 -----LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
....
gi 1720405097 513 EAKS 516
Cdd:pfam15921 535 HLKN 538
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
261-520 |
5.67e-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: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 261 RIAEITTQKEKIHEDTKEITEKSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLE-DVQVREkLKHAtska 339
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRvDLKLQE-LQHL---- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 340 KKLEKQLQKDKEKVEELKSVPAKSKTVINetttrnnslekEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKElmgfnks 419
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIE-----------ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE------- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 420 VNEAR---SKMEVAQSELDIYLSRHNTAVSQLSKAKEALITASEtlkERKAAIKDINTKLPQTQQELKEKEKELQKLTQE 496
Cdd:pfam15921 599 INDRRlelQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS---ERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
250 260
....*....|....*....|....
gi 1720405097 497 EINLKSLVHDLFQKVEEAKSSLAM 520
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKM 699
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
198-536 |
5.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 198 LCRRvEILNEHRGEKLNR----VKMVEKE-KDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYD----LQNRIAEITTQ 268
Cdd:PRK03918 440 VCGR-ELTEEHRKELLEEytaeLKRIEKElKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeLEEKLKKYNLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 269 K-EKIHEDTKEITEKSNVLSNEMKAKNSAVK---DVEKKLNKVTKFIEQNKEKFTQL----------DLEDVQVREK--- 331
Cdd:PRK03918 519 ElEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEELAELlkeleelgfeSVEELEERLKele 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 332 --------LKHATSKAKKLEKQLQKDKEKVEELKSVPAKSKTVINETTTRNNSLEKEREkeekklkevmdslKQETQGLQ 403
Cdd:PRK03918 599 pfyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS-------------EEEYEELR 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 404 KEKEIQEKELMGFNKSVNEARSKMEVAQSELDiylsrhntavsqlsKAKEALitasETLKERKAAIKDINTKLPQTqQEL 483
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLE--------------KLKEEL----EEREKAKKELEKLEKALERV-EEL 726
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1720405097 484 KEKEKELQKLTQEEInlkslvhdlFQKVEEAKSSLAMNRSRGKVLDAIIQEKK 536
Cdd:PRK03918 727 REKVKKYKALLKERA---------LSKVGEIASEIFEELTEGKYSGVRVKAEE 770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
200-517 |
5.94e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 200 RRVEilNEHRGEKLNRVKMVEK-EKDALEGEKNIAIEFLTLENEMFKKKNHICQYYIYDLQNRIAEITTQKEKIH--EDT 276
Cdd:PTZ00121 1218 RKAE--DAKKAEAVKKAEEAKKdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 277 KEITEKSNVLSNEMKAKNS--------AVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQK 348
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAkkadeakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 349 DKEKVEEL-KSVPAKSKTVINETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELMGfnKSVNEARSKM 427
Cdd:PTZ00121 1376 AKKKADAAkKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKA 1453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 428 EVAQSELDIylsrhNTAVSQLSKAKEALITASETLKERKAAIKDINTKlpQTQQELKEKEKELQKLTQEEINLKSLVHDL 507
Cdd:PTZ00121 1454 EEAKKAEEA-----KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
330
....*....|
gi 1720405097 508 FQKVEEAKSS 517
Cdd:PTZ00121 1527 AKKAEEAKKA 1536
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
282-499 |
6.92e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 282 KSNVLSNEMKAKNSAVKDVEKKLNKVTKFIEQNKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEELKSVPA 361
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 362 KSKTVIN--------ETTTRNNSLEKEREKEEKKLKEVMDSLKQETQGLQKEKEIQEKELmgfnKSVNEARSKMEVAQSE 433
Cdd:COG3883 97 RSGGSVSyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL----AELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720405097 434 LDIYLSRHNTAVSQLSKAKEALITASETLKERKAAIKDINTKLPQTQQELKEKEKELQKLTQEEIN 499
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
780-971 |
7.30e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 780 DRKQQKLLEENVSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINN--RKLKAQ------------------QNKLDTINK 839
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNkyNDLKKQkeelenelnllekeklniQKNIDKIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 840 QL-----------------DECASAITKAQVAIKTADRNLKKAQDSVCRTEKEIKDTEKEINDLKTELKNIEDKAEEVIN 902
Cdd:TIGR04523 195 KLlklelllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720405097 903 NTKTAETSLPEIQKEHRNLLQELKVI-----QENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIK 971
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
701-996 |
7.82e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 701 VEEVNKMESQLERHSKQ-AMQIQEQKVQHEEAVVKLRHSE--------RDMRNTLEKFAASIQGLSEQEEYLCVQIKELE 771
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQlKSEISDLNNQKEQDWNKELKSElknqekklEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 772 ANVLTtapdrKQQKLLEEN--VSVFKKEYDAVAEKAGKVEAEIKRLHNTIIDINN------RKLKAQQNKLDTINKQLDE 843
Cdd:TIGR04523 356 SENSE-----KQRELEEKQneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlnqqkdEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 844 CASAITKAQVAIKtadrNLKKaQDSVcrTEKEIKDTEKEINDLKTELKNIEDKAEEVINNTKTAETSLPEIQKEHRNLLQ 923
Cdd:TIGR04523 431 LKETIIKNNSEIK----DLTN-QDSV--KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720405097 924 ELKVIQENEHALQKDALSIKLKLEQIDGHISEHNSKIKYWQKEISKIKLHPVEDNpVETVAVLSQEELEAIKN 996
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN-LEKEIDEKNKEIEELKQ 575
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
18-111 |
8.04e-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: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720405097 18 QNFKSYAGEKVLG--PFHKR-FSCIIGPNGSGKSNVIDSMLF-VFGYRAQKIRSKKLSVLIHNSDehkdiqsCTVEVHFQ 93
Cdd:cd03279 9 KNFGPFREEQVIDftGLDNNgLFLICGPTGAGKSTILDAITYaLYGKTPRYGRQENLRSVFAPGE-------DTAEVSFT 81
|
90 100 110
....*....|....*....|....*....|..
gi 1720405097 94 --------KIIDKEGDDYE------VLPNSNF 111
Cdd:cd03279 82 fqlggkkyRVERSRGLDYDqftrivLLPQGEF 113
|
|
| |
