|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1162 |
0e+00 |
|
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: 1152.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 2 RLTEIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESLQDVIFNGSATRKPIGRASVE 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 82 LVFDNSSGKAAGqwKSYSEIAIRRVIQRDGESSYYINNIHVRRRDITDMFLGTGVSGRGYAIIEQGMISRIIEARPQELR 161
Cdd:TIGR02168 81 LVFDNSDGLLPG--ADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 162 TFLEEAAGITRYHEKRHETGLRLADARGNLQRVDDILEELDKQQQHLEAQAECAVRYQDLHRQLTAAQHTLWTLHKQQAA 241
Cdd:TIGR02168 159 AIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 242 ESRHQAQVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQGALYAANGEIARIEQNIRHIRANREQLDRQL 321
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 322 AEAELQLQNHEQQLNEVNENLTSWQDKLEQAKNCHLSCKEEHIVEAGKLPQMESAAQADQVRLIGLREKLALARQNEKLL 401
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 402 QNQQAYAEKTLHQLVVRRERLLEEQSSQ-PEIDPVQLDELQMESAELAAMLEQKQHSLSTLETQAYTVQQERDAILQIIQ 480
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELlKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 481 SLERDMARANARCDVLQRLQDQIEDNQE--LNAWMARLQLN-LLPRLWQQISIESGWETALEAVLRERIQAVTVDRLEQ- 556
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEgvKALLKNQSGLSgILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAa 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 557 MLEWEAQRPSA--KWAVCELV---PDRPVSNDTDQRTWKP--LSTLLSCRS--PAVQAVLGNWLYGVFVTDSLTAALADR 627
Cdd:TIGR02168 559 KKAIAFLKQNElgRVTFLPLDsikGTEIQGNDREILKNIEgfLGVAKDLVKfdPKLRKALSYLLGGVLVVDDLDNALELA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 628 SLLTSGEMLVTAEGHSITSCGVSYFAPDSAVHGILQRQREIAQIREECEQIGQSVLSQQQTLAAVEQDDQQIAADIVQLR 707
Cdd:TIGR02168 639 KKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 708 KVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESAC 787
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 788 QSSGRALASQRSRVQRLSDRLHETAFGEQDCQNRVIDCERRIGMITRNSVILTENMQRLQHARADLDES--TLTADTVHW 865
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieELESELEAL 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 866 QIQRDQHEQALMAVRHELENMDDTLREMEQARMYAEQRLQECGEAVGQARLREQEAEMTEARFADKLAESGETMLEMVPQ 945
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 946 FVNE---SPAKLQTRINRLTGEVTALGPVNLAALQELEALKSRRIHLEEQSHDLREAITTLEQAIRQIDRETRERLQETF 1022
Cdd:TIGR02168 959 LENKiedDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTF 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1023 DQVNQNLAGLFASIFGGGVAELVL-SGEDILDAGVQLNAHPPGKRNSSIHLLSGGEKALTALALVFSLFRLNPAPFCLLD 1101
Cdd:TIGR02168 1039 DQVNENFQRVFPKLFGGGEAELRLtDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILD 1118
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42627761 1102 EVDAPLDDSNSVRFCELVKRMSGETQFLFISHNKITMQMAQQLIGVTMREQGVSRVVTVDI 1162
Cdd:TIGR02168 1119 EVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1170 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 722.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESLQDVIFNGSATRKPIGRASV 80
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 81 ELVFDNSSGKAAGQwksYSEIAIRRVIQRDGESSYYINNIHVRRRDITDMFLGTGVSGRGYAIIEQGMISRIIEARPQEL 160
Cdd:COG1196 81 SLTFDNSDGTLPID---YDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 161 RTFLEEAAGITRYHEKRHETGLRLADARGNLQRVDDILEELDKQQQHLEAQAECAVRYQDLHRQLTAAQHTLWTLHKQQA 240
Cdd:COG1196 158 RAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLREL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 241 AESRHQAQVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQGALYAANGEIARIEQNIRHIRANREQLDRQ 320
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 321 LAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKNCHLSCKEEHIVEAGKLPQMESAAQADQVRLIGLREKLALARQNEKL 400
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 401 LQNQQAYAEKTLHQLVVRRERLLEEQSS---QPEIDPVQLDELQMESAELAAMLEQKQHSLSTLETQAYTVQQERDAILQ 477
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEEleeALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 478 IIQSLERDMARANARCDVLQRLQDQieDNQELNAWMARLQLNLLPRLWQQISIESGWETALEAVLRERIQAVTVDRLeqm 557
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEAD--YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV--- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 558 leweaqrpsakwavcelvpdrpvsndtdqrtwkplstllscrspavqavlgnwlygvfVTDSLTAALADRSLLTSGEMLV 637
Cdd:COG1196 553 ----------------------------------------------------------VEDDEVAAAAIEYLKAAKAGRA 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 638 TaeghsitscgvsyFAPDSAVHgilqrqreiaqireeceqiGQSVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQQ 717
Cdd:COG1196 575 T-------------FLPLDKIR-------------------ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 718 HDRQIQIVRLTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVELEaqvnqaesacqssgralasq 797
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE-------------------- 682
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 798 rsrvqrlsdrlhetafgeqdcqnrvidcerrigmitrnsviltenmqrlqharadldestltadtvhwqiqrdqhEQALM 877
Cdd:COG1196 683 ---------------------------------------------------------------------------ELAER 687
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 878 AVRHELENMDDTLREMEQARMYAEQRLQECGEAVGQARLREQEAEMTEARFADKLAESGETMLEMVPQF-VNESPAKLQT 956
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELpEPPDLEELER 767
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 957 RINRLTGEVTALGPVNLAALQELEALKSRRIHLEEQSHDLREAITTLEQAIRQIDRETRERLQETFDQVNQNLAGLFASI 1036
Cdd:COG1196 768 ELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRL 847
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1037 FGGGVAELVLS-GEDILDAGVQLNAHPPGKRNSSIHLLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRF 1115
Cdd:COG1196 848 FGGGEAELLLTdPDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERF 927
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*
gi 42627761 1116 CELVKRMSGETQFLFISHNKITMQMAQQLIGVTMREQGVSRVVTVDIGKIMAAGD 1170
Cdd:COG1196 928 AELLKEMSEDTQFIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEELAE 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
5-1161 |
3.08e-113 |
|
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: 380.95 E-value: 3.08e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 5 EIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESLQDVIFNGSATRKPIgRASVELVF 84
Cdd:TIGR02169 4 RIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQSGN-EAYVTVTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 85 DNSSGKAAGQWksysEIAIRRVIQRDG-ESSYYINNIHVRRRDITDMFLGTGVSGRGYAIIEQGMISRIIEARPQELRTF 163
Cdd:TIGR02169 83 KNDDGKFPDEL----EVVRRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 164 LEEAAGITRYHEKRHETGLRLADARGNLQRVDDILEELDKQQQHLEAQAECAVRYQDLHRQLTAAQHTLWTLHKQQAAES 243
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 244 RHQAQVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVN--------DRQHQIQGALYAANGEIARIEQNIRHIRANRE 315
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 316 QLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKNCHLSCKEEHIVEAGKLPQMESAAQADQVRLIGLREKL-ALA 394
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLeKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 395 RQNEKLLQNQQAYAEkTLHQLVVRRERLLEE----QSSQPEIDPVqLDELQMESAELAAMLEQKQHSLSTLETQAYTVQQ 470
Cdd:TIGR02169 399 REINELKRELDRLQE-ELQRLSEELADLNAAiagiEAKINELEEE-KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 471 ERDAILQIIQSLERDMARANARCDVLQRLQDQIEDNQELNAwmARLQlNLLPRLWQQISIESGWETALEAVLRERIQAVT 550
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK--ASIQ-GVHGTVAQLGSVGERYATAIEVAAGNRLNNVV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 551 VDR---LEQMLEWEAQR--------PSAKWAVCELVPDRPVSN----------DTDQRTwkplstllscrSPAVQAVLGN 609
Cdd:TIGR02169 554 VEDdavAKEAIELLKRRkagratflPLNKMRDERRDLSILSEDgvigfavdlvEFDPKY-----------EPAFKYVFGD 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 610 WLygvfVTDSLTAAladRSLLTSGEMlVTAEGHSITSCGVSYFAPDSAVHGILQRQREIAQIREECEQIGqsvlsqqqtl 689
Cdd:TIGR02169 623 TL----VVEDIEAA---RRLMGKYRM-VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLE---------- 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 690 aAVEQDDQQIAADIVQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVC 769
Cdd:TIGR02169 685 -GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 770 EAERVELEAQVNQAESACQSSGRALAsqRSRVQRLSDRLHETAFGEQDCQNRVIDCERRIGMITRNSVILTENMQRLQHA 849
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 850 RADLDE---------STLTADTVHWQIQRDQHEQALMAVRHELENMDDTLREMEQARMYAEQRLQECGEAVGQARLREQE 920
Cdd:TIGR02169 842 RIDLKEqiksiekeiENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 921 AEMTEARFADKLAESGETMLEMVPQFVNESPA-KLQTRINRLTGEVTALGPVNLAALQELEALKSRRIHLEEQSHDLREA 999
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEELSLeDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1000 ITTLEQAIRQIDRETRERLQETFDQVNQNLAGLFASIfGGGVAELVLSG-EDILDAGVQLNAHPPGKRNSSIHLLSGGEK 1078
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENpDDPFAGGLELSAKPKGKPVQRLEAMSGGEK 1080
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1079 ALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMSGETQFLFISHNKITMQMAQQLIGVTMREQGVSRVV 1158
Cdd:TIGR02169 1081 SLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQVF 1160
|
...
gi 42627761 1159 TVD 1161
Cdd:TIGR02169 1161 GLK 1163
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1155 |
4.32e-100 |
|
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: 344.26 E-value: 4.32e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 3 LTEIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESLQDVIFngSATRKPIGRASVEL 82
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 83 VFDNSSGKAAgqwKSYSEIAIRRVIQRDGESSYYINNIHVRRRDITDMFLGTGVSGRGYAIIEQGMISRIIEARPQELRT 162
Cdd:pfam02463 80 TFDNEDHELP---IDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 163 FLEEAAGITRYHEKRHETGLRLADARGNLQRVDDILEELDKQQQHLEAQAECAVRYQDLHRQLTAAQHTLWTLHKQQAAE 242
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 243 SRHQAQVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQGALYAANGEIARIEQNIR-HIRANREQLDRQL 321
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELlKLERRKVDDEEKL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 322 AEAELQLQNHEQQLNEVNEN-------LTSWQ----------DKLEQAKNCHLSCKEEHIVEAGKLPQMESAAQADQVRL 384
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEieelekeLKELEikreaeeeeeEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 385 IGLREKLALARQNEKLLQNQQAYAEKTLHQlvVRRERLLEEQSSQpEIDPVQLDELQMESAELAAMLEQKQHSLSTLETQ 464
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKK--EELEILEEEEESI-ELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 465 AYTVQQERDAILQIIQSLERDMARANArcdvlqrlqdQIEDNQELNAWMARLQLNLLPRLWQQISI---ESGWETALEAV 541
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQ----------KESKARSGLKVLLALIKDGVGGRIISAHGrlgDLGVAVENYKV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 542 LRERIQAVTVDRLEQMLEWEAQRPSAKWAVCELVPDRPVSNDTDQRTWKPLSTLLSCRSPAVQAVLGNWLYGVFVTDSLT 621
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 622 AALADRSLLTSGEMLVTAEGHSITSCGVSYFAPDSAVHGILQRQREIAQIREECEQIGQSVLSQQQTLAAVEQDDQQIAA 701
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 702 DI-----VQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVEL 776
Cdd:pfam02463 704 KEqrekeELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 777 EAQVNQAESacqsSGRALASQRSRVQRLSDRLHETAFGEQDCQNRVIDCERRIGMITRNSVILTENMQRLQHArADLDES 856
Cdd:pfam02463 784 EKLKVEEEK----EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLA-EEELER 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 857 TLTADTVHWQIQR---DQHEQALMAVRHELENMDDTLREMEQARMYAEQRLQECGEAVGQARLREQEAEMTEARFADKLA 933
Cdd:pfam02463 859 LEEEITKEELLQElllKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 934 ESgETMLEMVPQFVNESPAKLQTRINRLTGEVTALGPVNLAALQELEALKSRRIHLEEQSHDLREAITTLEQAIRQIDRE 1013
Cdd:pfam02463 939 EL-LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1014 TRERLQETFDQVNQNLAGLFASIFGGGVAEL-VLSGEDILDAGVQLNAHPPGKRNSSIHLLSGGEKALTALALVFSLFRL 1092
Cdd:pfam02463 1018 RLKEFLELFVSINKGWNKVFFYLELGGSAELrLEDPDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKY 1097
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42627761 1093 NPAPFCLLDEVDAPLDDSNSVRFCELVKRMSGETQFLFISHNKITMQMAQQLIGVTMREQGVS 1155
Cdd:pfam02463 1098 KPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVS 1160
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1021-1156 |
5.26e-57 |
|
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: 195.38 E-value: 5.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1021 TFDqvnqNLAGLFASIFGGGVaelvlsgEDILDAgvqlnahpPGKRNSSIHLLSGGEKALTALALVFSLFRLNPAPFCLL 1100
Cdd:cd03278 81 TFD----NSDGRYSIISQGDV-------SEIIEA--------PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVL 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 42627761 1101 DEVDAPLDDSNSVRFCELVKRMSGETQFLFISHNKITMQMAQQLIGVTMREQGVSR 1156
Cdd:cd03278 142 DEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLYGVTMQESGVSK 197
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-156 |
5.80e-49 |
|
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: 172.65 E-value: 5.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 3 LTEIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESLQDVIFNGSATRKPIGRASVEL 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42627761 83 VFDNSSGKaagqwksyseiairrviqrdgessyyinnihvrrrditdmflgtgvsgrgYAIIEQGMISRIIEAR 156
Cdd:cd03278 81 TFDNSDGR--------------------------------------------------YSIISQGDVSEIIEAP 104
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1072-1156 |
3.48e-23 |
|
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: 97.76 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1072 LLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMS-GETQFLFISHNKITMQMAQQLIGVTmR 1150
Cdd:cd03239 94 ILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAkHTSQFIVITLKKEMFENADKLIGVL-F 172
|
....*.
gi 42627761 1151 EQGVSR 1156
Cdd:cd03239 173 VHGVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1062-1161 |
6.83e-21 |
|
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: 93.41 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1062 PPGKRNSSIHLLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMSGET-QFLFISHNKITMQM 1140
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNfQFIVISLKEEFFSK 224
|
90 100
....*....|....*....|...
gi 42627761 1141 AQQLIGVTmREQG--VSRVVTVD 1161
Cdd:cd03275 225 ADALVGVY-RDQEcnSSKVLTLD 246
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-153 |
8.61e-19 |
|
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: 87.35 E-value: 8.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDPAVV-PVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESLQDVIF-NGSATrkpIGRA 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYkRGQAG---ITKA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42627761 79 SVELVFDNSSGKAAGQ-WKSYSEIAIRRVIQRDGESSYYINNIHVRRRDITDMFLGTGVS-GRGYAIIEQGMISRII 153
Cdd:cd03273 78 SVTIVFDNSDKSQSPIgFENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNvNNPHFLIMQGRITKVL 154
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-144 |
3.65e-18 |
|
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: 83.51 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 3 LTEIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESLQDvifNGSATRKPIGRASVEL 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFL---AGGGVKAGINSASVEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 83 VFDNS-------------SGkaaGQwKSYSEIAIRRVIQRDGESSYYI--------NNIHVRRrdITDMFLGTGVSGRGY 141
Cdd:cd03239 78 TFDKSyflvlqgkveqilSG---GE-KSLSALALIFALQEIKPSPFYVldeidaalDPTNRRR--VSDMIKEMAKHTSQF 151
|
...
gi 42627761 142 AII 144
Cdd:cd03239 152 IVI 154
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1066-1155 |
9.59e-18 |
|
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: 81.64 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1066 RNSSIHLLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMSGET-QFLFISHNKITMQMAQQL 1144
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKL 150
|
90
....*....|.
gi 42627761 1145 IGVTMREQGVS 1155
Cdd:cd03227 151 IHIKKVITGVY 161
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-119 |
1.17e-15 |
|
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: 78.00 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 3 LTEIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGEsRASALRGESLQDVIFNGSATRKPIGRASVEL 82
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGE-KSSHLRSKNLKDLIYRARVGKPDSNSAYVTA 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 42627761 83 VFDNSSGKaagqwksysEIAIRRVIqRDGESSYYINN 119
Cdd:cd03275 80 VYEDDDGE---------EKTFRRII-TGGSSSYRING 106
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
5-150 |
1.17e-14 |
|
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: 74.99 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 5 EIKLAGFKTFVDPAVV-PVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRaSALRGESLQDVIFNGSATRkpIGRASVELV 83
Cdd:cd03272 3 QVIIQGFKSYKDQTVIePFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEY-THLREEQRQALLHEGSGPS--VMSAYVEII 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42627761 84 FDNSSGK-AAGQwksySEIAIRRVI--QRDgesSYYINNIHVRRRDITDMFLGTGVS-GRGYAIIEQGMIS 150
Cdd:cd03272 80 FDNSDNRfPIDK----EEVRLRRTIglKKD---EYFLDKKNVTKNDVMNLLESAGFSrSNPYYIVPQGKIN 143
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1044-1147 |
1.32e-14 |
|
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: 73.87 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1044 LVLSGEdildagVQLNAHPPGKRNSSIHLLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMS 1123
Cdd:cd03274 105 LILQGE------VEQIAQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERT 178
|
90 100
....*....|....*....|....
gi 42627761 1124 GETQFLFISHNKITMQMAQQLIGV 1147
Cdd:cd03274 179 KNAQFIVISLRNNMFELADRLVGI 202
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1069-1161 |
3.44e-13 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 70.75 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1069 SIHLLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMSGETQFLFISHNKITMQMAQQLIGVT 1148
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
90
....*....|...
gi 42627761 1149 MReqgvSRVVTVD 1161
Cdd:cd03272 235 FR----NKVSTID 243
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
518-625 |
1.51e-12 |
|
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: 65.33 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 518 LNLLPRLWQQISIESGWETALEAVLRERIQAVTVDR-------LEQMLEWEAQRpsAKWAVCELVPDRPVSNDTDQRT-- 588
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTeetakkaIEFLKKNRLGR--ATFLPLDKIKPRSPAGSKLREAll 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 42627761 589 -----WKPLSTLLSCrSPAVQAVLGNWLYGVFVTDSLTAALA 625
Cdd:smart00968 79 pepgfVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARR 119
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-208 |
5.27e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 66.19 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 2 RLTEIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESlqDVIFNGSAtrkpigRASVE 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRS--DLINVGSE------EASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 82 LVFDNssgkaagqwksyseiairrviqrdGESSYyinniHVRRRditdmflgtgvsgrgyaiieQGMISRIIEARPQELR 161
Cdd:COG0419 73 LEFEH------------------------GGKRY-----RIERR--------------------QGEFAEFLEAKPSERK 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 42627761 162 TFLEEAAGITRYHEKRHetglRLADARGNLQRVDDILEELDKQQQHL 208
Cdd:COG0419 104 EALKRLLGLEIYEELKE----RLKELEEALESALEELAELQKLKQEI 146
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1069-1133 |
1.54e-11 |
|
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: 65.78 E-value: 1.54e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42627761 1069 SIHLLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMSGETQFLFISH 1133
Cdd:cd03273 163 SLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSL 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
299-1027 |
5.05e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 299 EIARIEQNIRHIRANREQLD--RQLAEAELQLQNHEQQLNEVNENLTSWQD--KLEQAKNCHLSCKEEHIVEAGKLPQME 374
Cdd:COG4913 236 DLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAqrRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 375 SAAQADQVRLIGLREKLA-LARQNEKLLQNQQAYAEKTLHQLVVRRERL---LEEQSSQPEIDPVQLDELQMESAELAAM 450
Cdd:COG4913 316 ARLDALREELDELEAQIRgNGGDRLEQLEREIERLERELEERERRRARLealLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 451 LEQKQHSLST----LETQAYTVQQERDAILQIIQSLERdmaRANARCDVLQRLQDQIEdnQELNAWMARLQ-----LNLL 521
Cdd:COG4913 396 LEEELEALEEalaeAEAALRDLRRELRELEAEIASLER---RKSNIPARLLALRDALA--EALGLDEAELPfvgelIEVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 522 PRlwqqisiESGWETALEAVLREriQA----VTVDRLEQMLEWEAQRPSAKWAVCELVPDRPVSNDTDQRTWKPLSTLLS 597
Cdd:COG4913 471 PE-------EERWRGAIERVLGG--FAltllVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 598 CR-SPAvqavlGNWLygvfvtDSLTAALADRSLLTSGEMLvTAEGHSITSCGVSYfapDSAVHGILQRQREIAQIReece 676
Cdd:COG4913 542 FKpHPF-----RAWL------EAELGRRFDYVCVDSPEEL-RRHPRAITRAGQVK---GNGTRHEKDDRRRIRSRY---- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 677 QIGQSVLSQqqtLAAVEQDDQQIAADIVQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQ--AQLEIELADLAVQIEE 754
Cdd:COG4913 603 VLGFDNRAK---LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 755 ---ESSQKQQAETELVVCEAERVELEAQVNQAESACQSSGRALASQRSRVQRLSDRLHetAFGEQDCQNRVIDCERRIGm 831
Cdd:COG4913 680 ldaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERFA- 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 832 itrnSVILTENMQRLqhaRADLDESTLTADTvhwqiQRDQHEQALMAVRHE--------LENMDDTLREMEQarmYAEQR 903
Cdd:COG4913 757 ----AALGDAVEREL---RENLEERIDALRA-----RLNRAEEELERAMRAfnrewpaeTADLDADLESLPE---YLALL 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 904 lqecgeavgqARLREQEAEMTEARFADKLAESGETMLEMVPQFVNESPAKLQTRINrltgevtalgPVNlAALQELEALK 983
Cdd:COG4913 822 ----------DRLEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERID----------PLN-DSLKRIPFGP 880
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 42627761 984 SRRIHLE---EQSHDLREAITTLEQAIRQIDRETRERLQETFDQVNQ 1027
Cdd:COG4913 881 GRYLRLEarpRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKR 927
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-84 |
7.45e-11 |
|
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: 63.08 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 3 LTEIKLAGFKTFVDPAVV-PVPGNLVGIVGPNGCGKSNVIDAVRWVLGeSRASALRGESLQDVIFNgSATRKPIGRASVE 81
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIgPFHKSFSAIVGPNGSGKSNVIDSMLFVFG-FRASKMRQKKLSDLIHN-SAGHPNLDSCSVE 80
|
...
gi 42627761 82 LVF 84
Cdd:cd03274 81 VHF 83
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
184-920 |
1.01e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 66.51 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 184 LADARGNLQRVDDILEELDKQQQHLEA-----------------QAECAVRYQDLHRQLTAAqhtlwtLHKQQ-----AA 241
Cdd:COG3096 301 LAEEQYRLVEMARELEELSARESDLEQdyqaasdhlnlvqtalrQQEKIERYQEDLEELTER------LEEQEevveeAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 242 ESRHQAQVEVERLVQEMETIRSGMQETGEKLDELRL----YHRVVNdRQHQIQGALYAANGEIARIEQNIRHIRANREQL 317
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTraiqYQQAVQ-ALEKARALCGLPDLTPENAEDYLAAFRAKEQQA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 318 DRQLAEAELQL---QNHEQQLNEVNENLTSWQDKLEQAkNCHLSCKEehIVEAGKlpqmESAAQADqvRLIGLREKLALA 394
Cdd:COG3096 454 TEEVLELEQKLsvaDAARRQFEKAYELVCKIAGEVERS-QAWQTARE--LLRRYR----SQQALAQ--RLQQLRAQLAEL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 395 RQNEkllqNQQAYAEKTLHQLVVRRERLLEEQssqpeidpvqlDELQMESAELAAMLEQKQHSLSTLETQAYTVQQERDA 474
Cdd:COG3096 525 EQRL----RQQQNAERLLEEFCQRIGQQLDAA-----------EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 475 ILQIIQSLERDMARANARCDVLQRLQDQ----IEDNQELNAWMARL--QLNLLPRLWQQISIEsgwETALEAVLRERIQA 548
Cdd:COG3096 590 LRARIKELAARAPAWLAAQDALERLREQsgeaLADSQEVTAAMQQLleREREATVERDELAAR---KQALESQIERLSQP 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 549 VTVD--RLEQMleweAQRPSAKwAVCELVPDRPVSNdtdqrtwKP-LSTLLscrSPAVQAVlgnwlygvfVTDSLTAALA 625
Cdd:COG3096 667 GGAEdpRLLAL----AERLGGV-LLSEIYDDVTLED-------APyFSALY---GPARHAI---------VVPDLSAVKE 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 626 ----------------------DRSLLTSGEM----LVTAEGHSITscgVSYFaPDSAVHGILQRQREIAQIREE----C 675
Cdd:COG3096 723 qlagledcpedlyliegdpdsfDDSVFDAEELedavVVKLSDRQWR---YSRF-PEVPLFGRAAREKRLEELRAErdelA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 676 EQIGQSVLSQQQTLAAVEQDDQQIA------------ADIVQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQL-- 741
Cdd:COG3096 799 EQYAKASFDVQKLQRLHQAFSQFVGghlavafapdpeAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLnk 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 742 ---------EIELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVN------QAESACQSSGRALASQRSRVQRLSD 806
Cdd:COG3096 879 llpqanllaDETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAvlqsdpEQFEQLQADYLQAKEQQRRLKQQIF 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 807 RLHE-----TAFGEQDCQnrvidcerriGMITRNSVILTENMQRLQHARADLDEstltADTVHWQIQrDQHEQALmAVRH 881
Cdd:COG3096 959 ALSEvvqrrPHFSYEDAV----------GLLGENSDLNEKLRARLEQAEEARRE----AREQLRQAQ-AQYSQYN-QVLA 1022
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 42627761 882 ELENMDDTLREMEQArmyAEQRLQECG-----EAVGQARLREQE 920
Cdd:COG3096 1023 SLKSSRDAKQQTLQE---LEQELEELGvqadaEAEERARIRRDE 1063
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
664-1135 |
2.19e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 664 RQREIAQIREE--CEQIGQSVlSQQQTLAAVEQDDQQIAadivQLRKVIEEIRTQQ------HDRQIQIVRLTQQIERVA 735
Cdd:PRK02224 441 RVEEAEALLEAgkCPECGQPV-EGSPHVETIEEDRERVE----ELEAELEDLEEEVeeveerLERAEDLVEAEDRIERLE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 736 QQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESACQSSGRALASQRSRVQRLSDRLHETAFGE 815
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 816 qDCQNRVIDCERRIGmitrnsviltenmqRLQHARADLDEstltadtvhwqiQRDQHEQALMAVRHELENMDDTLREmeq 895
Cdd:PRK02224 596 -TLLAAIADAEDEIE--------------RLREKREALAE------------LNDERRERLAEKRERKRELEAEFDE--- 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 896 armyaeqrlqecgEAVGQARLREQEAEMTEARFADKLAEsgetmlemvpqfVNESPAKLQTRINRLTGEvtalgpvnlaa 975
Cdd:PRK02224 646 -------------ARIEEAREDKERAEEYLEQVEEKLDE------------LREERDDLQAEIGAVENE----------- 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 976 LQELEALKSRRIHLEEQSHDLR---EAITTLEQAIRQIDRETRER--------LQETFDQVNQNLAglFASIFGGGVAEL 1044
Cdd:PRK02224 690 LEELEELRERREALENRVEALEalyDEAEELESMYGDLRAELRQRnvetlermLNETFDLVYQNDA--YSHIELDGEYEL 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1045 VLSGEDildaGVQLNAhppgkrnssiHLLSGGEKALTALALVFSLFRL--------NPAPFCLLDEVDAPLDDSNSVRFC 1116
Cdd:PRK02224 768 TVYQKD----GEPLEP----------EQLSGGERALFNLSLRCAIYRLlaegiegdAPLPPLILDEPTVFLDSGHVSQLV 833
|
490 500
....*....|....*....|.
gi 42627761 1117 ELVKRMS--GETQFLFISHNK 1135
Cdd:PRK02224 834 DLVESMRrlGVEQIVVVSHDD 854
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-214 |
5.37e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 60.20 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 6 IKLAGFKTFvDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLG----ESRASALRGESLQDVIFNGSATRKpigrASVE 81
Cdd:pfam13476 1 LTIENFRSF-RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYgktsRLKRKSGGGFVKGDIRIGLEGKGK----AYVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 82 LVFDNSSGkaagqwKSYSEIAIRRVIQRDGESSYYINNIHVRRRDITDMFlgtgvsgrgyaiieqgmISRIIEARPQELR 161
Cdd:pfam13476 76 ITFENNDG------RYTYAIERSRELSKKKGKTKKKEILEILEIDELQQF-----------------ISELLKSDKIILP 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 42627761 162 TFLEEAAGITRYHEKRHETGlRLADARGNLQRVDDILEELDKQQQHLEAQAEC 214
Cdd:pfam13476 133 LLVFLGQEREEEFERKEKKE-RLEELEKALEEKEDEKKLLEKLLQLKEKKKEL 184
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-174 |
1.01e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 61.87 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 2 RLTEIKLAGFKTFVDpAVVPvPGNLVGIVGPNGCGKSNVIDAVRWvLGE------SRASALRGeSLQDVIFNGSatRKPI 75
Cdd:COG4637 1 MITRIRIKNFKSLRD-LELP-LGPLTVLIGANGSGKSNLLDALRF-LSDaargglQDALARRG-GLEELLWRGP--RTIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 76 GRASVELVFDNSSGKAAGqwksYsEIAIRRVIQRDG----ESSYYINNIHVRRRDITDMFLGTGVSGRGYAII-EQGMIS 150
Cdd:COG4637 75 EPIRLELEFAEEDERDLR----Y-ELELGLPEPGGRpevkEERLWLKRGSGGRPFLDFRPKGRAVGGEPERLDsPESLLS 149
|
170 180
....*....|....*....|....*
gi 42627761 151 RIIE-ARPQELRTFLEEAAGITRYH 174
Cdd:COG4637 150 QLGDpERFPELRALREALRSWRFYD 174
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
205-1023 |
2.87e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.67 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 205 QQHLE-AQAECAVRYQDLHRQLTAAQHtlwtLHKQQAAESRhQAQVEVERLVQEMETIRSGMqetgekLDELRLYHRVVN 283
Cdd:pfam15921 73 KEHIErVLEEYSHQVKDLQRRLNESNE----LHEKQKFYLR-QSVIDLQTKLQEMQMERDAM------ADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 284 DRQHQIQGALYAANGEIARIEQNIRHIRANREQLDRQLAeaelqlqNHEQQLNEVNENLTSWQDKLEQAKNCHLSCKEEH 363
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMML-------SHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 364 IVEAGK-----LPQMESAAQADQVRLIGLREKLALAR---QN--EKLLQNQQAYAEKTLHQLVVRRERLLEEQSS---QP 430
Cdd:pfam15921 215 FRSLGSaiskiLRELDTEISYLKGRIFPVEDQLEALKsesQNkiELLLQQHQDRIEQLISEHEVEITGLTEKASSarsQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 431 EIDPVQLDELQMESAELAAMLEQKqhsLSTLETqayTVQQERDAILQI-------IQSLERDMARANARCDVLQRLQDQI 503
Cdd:pfam15921 295 NSIQSQLEIIQEQARNQNSMYMRQ---LSDLES---TVSQLRSELREAkrmyedkIEELEKQLVLANSELTEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 504 -EDNQELNAWMARLQLNLLPRLwQQISIESGWETALEAvlRERIQAVTVDRLEQMLEweaqrpsakwavcelvpDRpvsN 582
Cdd:pfam15921 369 sQESGNLDDQLQKLLADLHKRE-KELSLEKEQNKRLWD--RDTGNSITIDHLRRELD-----------------DR---N 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 583 DTDQRTWKPLSTLLS-CRSPAVQ--AVLGNWLYGVFVTDSLTAALAD-----RSL---LTSGEMLVTAEGHSITSCGVSY 651
Cdd:pfam15921 426 MEVQRLEALLKAMKSeCQGQMERqmAAIQGKNESLEKVSSLTAQLEStkemlRKVveeLTAKKMTLESSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 652 FAPDSAVHGIlqrQREIAQIREECE---QIGQSVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRtQQHDRQIQIVRLT 728
Cdd:pfam15921 506 QEKERAIEAT---NAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILR-QQIENMTQLVGQH 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 729 QQIERVAQ-QQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESACQSSGRALAS-QRSRVQRLsd 806
Cdd:pfam15921 582 GRTAGAMQvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDiKQERDQLL-- 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 807 rlhetafgeqdcqNRVIDCERRIGMITRNSVILTENMqrlqhaRADLDESTLTADTVHWQIQRDQheqalmavrHELENM 886
Cdd:pfam15921 660 -------------NEVKTSRNELNSLSEDYEVLKRNF------RNKSEEMETTTNKLKMQLKSAQ---------SELEQT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 887 DDTLREMEQARMYAEQrlqecgEAVGQARlreqeaEMTEARFADKLAESGETMLEMVPQFVNESPAKLQTRINRLTGEVT 966
Cdd:pfam15921 712 RNTLKSMEGSDGHAMK------VAMGMQK------QITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42627761 967 ALGPVNLAALQELEALKSrrihleeQSHDLREAITTLEQAI---------------RQIDRETRERLQETFD 1023
Cdd:pfam15921 780 TVATEKNKMAGELEVLRS-------QERRLKEKVANMEVALdkaslqfaecqdiiqRQEQESVRLKLQHTLD 844
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-85 |
3.36e-09 |
|
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: 60.02 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDpAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGEslqDviFNGSATRKPIgRASV 80
Cdd:COG3593 1 MKLEKIKIKNFRSIKD-LSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE---D--FYLGDDPDLP-EIEI 73
|
....*
gi 42627761 81 ELVFD 85
Cdd:COG3593 74 ELTFG 78
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
691-1032 |
4.19e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 691 AVEQDDQQIAADIVQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVCE 770
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 771 AERVELEAQVNQAESACQSSGRALASQRSRVQRLSDRLHETAFGEQDCQNRVIDCERRI--------GMITRNSVI---L 839
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecGQPVEGSPHvetI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 840 TENMQRLQHARADLDESTLTADTVHWQIQRdqhEQALMAVRHELENMDDTLREMEQARMYAEQRLQECGEAVGQARLR-- 917
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLER---AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERaa 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 918 EQEAEMTEAR-FADKLAESGETMLEMVPQFvNESPAKLQTRINRLTGEVTALGPVNlAALQELEALKSRRIHLEEQSHDL 996
Cdd:PRK02224 548 ELEAEAEEKReAAAEAEEEAEEAREEVAEL-NSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREALAELNDER 625
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 42627761 997 REAITTLEQAIRQID-----------RETRERLQETFDQVNQNLAGL 1032
Cdd:PRK02224 626 RERLAEKRERKRELEaefdearieeaREDKERAEEYLEQVEEKLDEL 672
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
519-625 |
4.97e-09 |
|
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: 55.35 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 519 NLLPRLWQQISIESGWETALEAVLRERIQAVTVDRLEQMLEWEAQRPSAKWAVCELVP-----DRPVSNDTDQRTW-KPL 592
Cdd:pfam06470 3 GVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPldrlkPRPRRPGADLKGGaGPL 82
|
90 100 110
....*....|....*....|....*....|...
gi 42627761 593 STLLSCrSPAVQAVLGNWLYGVFVTDSLTAALA 625
Cdd:pfam06470 83 LDLVEY-DDEYRKALRYLLGNTLVVDDLDEALE 114
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-492 |
1.47e-08 |
|
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: 58.24 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 247 AQVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQGALYAANGEIARIEQNIRHIRANREQLDRQLAEAEL 326
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 327 QLQNHEQQLNEVNENL--TSWQDKLEQAKNchlsckEEHIVEAGKLPQ-MESAAQADQVRLIGLREKLALARQNEKLLQN 403
Cdd:COG4942 98 ELEAQKEELAELLRALyrLGRQPPLALLLS------PEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 404 QQAYAEKTLHQLVVRRERLLEEQSSQpeidpvqldelqmesaelAAMLEQKQHSLSTLETQAYTVQQERDAILQIIQSLE 483
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAER------------------QKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*....
gi 42627761 484 RDMARANAR 492
Cdd:COG4942 234 AEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-1030 |
3.09e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.97 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDPAVV--PVPGNLVGIVGPNGCGKSNVIDAVRWVL-GESRASALRGESLQDVifngSATRKPIGR 77
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALyGKLPRRSEVIRSLNSL----YAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 78 ASVELVFDNSSGKA------AGQWKSYSEIAIRRVIQRDGESSyyINNIHVRRR-----DITDMFLGTGVSGrgyAIIEQ 146
Cdd:TIGR00618 77 AELEFSLGTKIYRVhrtlrcTRSHRKTEQPEQLYLEQKKGRGR--ILAAKKSETeevihDLLKLDYKTFTRV---VLLPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 147 GMISRIIEARPQELRTFLEEAAGITRYHEKRHETGLRLADARGNlqrvddiLEELDKQQQHLEAQAECAVryqdlhrqlt 226
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGK-------AELLTLRSQLLTLCTPCMP---------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 227 aaqhtlwtlhkqqaaESRHQAQVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQgalyaangeiarieqn 306
Cdd:TIGR00618 215 ---------------DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLK---------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 307 irhiranreQLDRQLAEAELQLQNHEQQLNEVNenltswqdkleqaknchLSCKEEHIVEAGK-LPQMESAAQADQVRLI 385
Cdd:TIGR00618 264 ---------QLRARIEELRAQEAVLEETQERIN-----------------RARKAAPLAAHIKaVTQIEQQAQRIHTELQ 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 386 GLREKLALARQNEKLLQNQQA------YAEKTLHQLVVRRERLLEEQSSQPEIDPVQLDELQ--MESAELAAMLEQKQHS 457
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSsieeqrRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQS 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 458 LSTLETQAYTVQQERDAILQIIQSLERDMARANARCDVLQRLQDQIEDNQELNAWMARLQLNLLPRLWQQisiesgweta 537
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS---------- 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 538 leavLRERIQAVTvdRLEQMLEWEAQRPSAKWAVCELVPDRPvsndtdqrtwKPLSTllSCRSPAVQAVLgnwlygvfvt 617
Cdd:TIGR00618 468 ----LKEREQQLQ--TKEQIHLQETRKKAVVLARLLELQEEP----------CPLCG--SCIHPNPARQD---------- 519
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 618 dsLTAALADRSLLTSGEMLVTAEGHSITScgvsyfapdsaVHGILQRQREIAQIREECEQigqsvlSQQQTLAAVEQDDQ 697
Cdd:TIGR00618 520 --IDNPGPLTRRMQRGEQTYAQLETSEED-----------VYHQLTSERKQRASLKEQMQ------EIQQSFSILTQCDN 580
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 698 QIAADIVQLRKVIEEIR--TQQHDRQIQIVRLTQQIERVaqqqaQLEIELADLAVQIEEESSQKQQAetelvvceaerve 775
Cdd:TIGR00618 581 RSKEDIPNLQNITVRLQdlTEKLSEAEDMLACEQHALLR-----KLQPEQDLQDVRLHLQQCSQELA------------- 642
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 776 leaqvnQAESACQSSGRALASQRSRVQRLSDRLHETAFGEQDcQNRVIDCERRIGMITRnsviLTENMQRLQHARADLDE 855
Cdd:TIGR00618 643 ------LKLTALHALQLTLTQERVREHALSIRVLPKELLASR-QLALQKMQSEKEQLTY----WKEMLAQCQTLLRELET 711
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 856 STLTADTvhwqiQRDQHEQALMAVRHELENMDDTLREMEQ-ARMYAEQRLQECGEAVGQARLREQEAEMTEARFADklae 934
Cdd:TIGR00618 712 HIEEYDR-----EFNEIENASSSLGSDLAAREDALNQSLKeLMHQARTVLKARTEAHFNNNEEVTAALQTGAELSH---- 782
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 935 sgetmLEMVPQFVNESPAKLQTRINRLTGEVTALGPvnlAALQELEALKSRRIHLEEQSHDLREAITTLEQAIRQIDRET 1014
Cdd:TIGR00618 783 -----LAAEIQFFNRLREEDTHLLKTLEAEIGQEIP---SDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKY 854
|
1050
....*....|....*.
gi 42627761 1015 RERLQEtFDQVNQNLA 1030
Cdd:TIGR00618 855 EECSKQ-LAQLTQEQA 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-475 |
4.19e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDPAVVPVPGNLVgIVGPNGCGKSNVIDAVRWVLGESRASAlrgESLQDVIFNGSATrkpigrASV 80
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRLEDGVTV-IHGVNGSGKSSLLEACFFALYGSKALD---DTLDDVITIGAEE------AEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 81 ELVFDNSSGkaagqwksysEIAIRRVIQRDGESSY-----------YINNIHVRRRDITDMFLGTGVSGRGYAIIEQGMI 149
Cdd:PRK02224 71 ELWFEHAGG----------EYHIERRVRLSGDRATtakcvletpegTIDGARDVREEVTELLRMDAEAFVNCAYVRQGEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 150 SRIIEARPQELRTFLEEAAGITRYHEKRHetglRLADARGNlqrVDDILEELDKQQQHLEAQAEcAVRYQDLHRQLTAAQ 229
Cdd:PRK02224 141 NKLINATPSDRQDMIDDLLQLGKLEEYRE----RASDARLG---VERVLSDQRGSLDQLKAQIE-EKEEKDLHERLNGLE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 230 HTLWTL---------HKQQAAESRHQAQV----------EVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQ 290
Cdd:PRK02224 213 SELAELdeeieryeeQREQARETRDEADEvleeheerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 291 GALYAANGEIARIEQNIRHIRANREQLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEqaknchlsckeehiveagkl 370
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD-------------------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 371 pQMESAAQadqvrliGLREKlalARQNEKLLQNQQAYAEKTLHQLVVRRERlLEEQSSQPEIDPVQLDELQMESAELAAM 450
Cdd:PRK02224 353 -DLEERAE-------ELREE---AAELESELEEAREAVEDRREEIEELEEE-IEELRERFGDAPVDLGNAEDFLEELREE 420
|
490 500
....*....|....*....|....*
gi 42627761 451 LEQKQHSLSTLETqayTVQQERDAI 475
Cdd:PRK02224 421 RDELREREAELEA---TLRTARERV 442
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-510 |
5.05e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 156 RPQELRTFLEEAAgiTRYHEKRHETGLRLADARGNLQRVDDILEELDKQQQHLEaqaECAVRYQDLHRQLTAAQHTLWTL 235
Cdd:PRK02224 280 EVRDLRERLEELE--EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE---ECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 236 hKQQAAESRHQAqveverlvqemETIRSGMQETGEKLDELRlyhrvvndrqhqiqgalyaanGEIARIEQNIRHIRANRE 315
Cdd:PRK02224 355 -EERAEELREEA-----------AELESELEEAREAVEDRR---------------------EEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 316 QLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKNchLSCKEEHIVEAGKLPQME---------SAAQADQVRLIG 386
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARE--RVEEAEALLEAGKCPECGqpvegsphvETIEEDRERVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 387 LREKLALARQNEKLLQN------QQAYAEKTLHQLVVRRE---RLLEEQSSQPEIDPVQLDELQMESAELAAMLEQKQHS 457
Cdd:PRK02224 480 LEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEERREdleELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42627761 458 LSTLETQAYTVQQE-------RDAILQIIQSLER----DMARANARcDVLQRLQDQIEDNQELN 510
Cdd:PRK02224 560 AAEAEEEAEEAREEvaelnskLAELKERIESLERirtlLAAIADAE-DEIERLREKREALAELN 622
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-117 |
5.80e-07 |
|
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: 50.44 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 5 EIKLAGFKTFVDPAVV-PVPGNLVGIVGPNGCGKSNVIDAVRWVLGEsRASALRgeslqdvifNGSATRKPIGRASVELV 83
Cdd:cd03227 1 KIVLGRFPSYFVPNDVtFGEGSLTIITGPNGSGKSTILDAIGLALGG-AQSATR---------RRSGVKAGCIVAAVSAE 70
|
90 100 110
....*....|....*....|....*....|....
gi 42627761 84 FDNSSGKAAGQWKSYSEIAIRRVIQRDGESSYYI 117
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILALASLKPRPLYI 104
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
237-453 |
8.25e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 237 KQQAAESRHQAQVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQGALYAANGEIARIEQNIRHIRANREQ 316
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 317 LDRQLAEAELQLQNHEQQlnEVNENLTSWQDKLEQAKNCHLSckeEHIVEAGKlpQMESAAQADQVRLIGLREKLALARQ 396
Cdd:COG4942 102 QKEELAELLRALYRLGRQ--PPLALLLSPEDFLDAVRRLQYL---KYLAPARR--EQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 42627761 397 NEKLLQNQQAYAEKTLHQLVVRRERLLEEQSSQPEIDPVQLDELQMESAELAAMLEQ 453
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-132 |
8.46e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.07 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 3 LTEIKLAGFKTFVDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVL-GESRASALRGESLQDVIFNGSAtrkpigRASVE 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGEV------RAQVK 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 42627761 82 LVFDNSSGKaagqwksysEIAIRRviqrdgESSYYINNIHVRRRDITDMFL 132
Cdd:cd03240 75 LAFENANGK---------KYTITR------SLAILENVIFCHQGESNWPLL 110
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-505 |
3.91e-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: 50.53 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 285 RQHQIQGALYAANGEIARIEQNIRHIRANREQLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKnchlsckEEHI 364
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR-------AELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 365 VEAGKLPQMESAAQadqvrLIGLREKLALARQNEKLLQNQQAYAekTLHQLVVRRERLLEEQSSQPEIDPVQLDELQMES 444
Cdd:COG4942 101 AQKEELAELLRALY-----RLGRQPPLALLLSPEDFLDAVRRLQ--YLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42627761 445 AELAAMLEQKQHSLSTLETQaytvQQERDailQIIQSLERDMARANARCDVLQRLQDQIED 505
Cdd:COG4942 174 AELEALLAELEEERAALEAL----KAERQ---KLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
662-1044 |
5.57e-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: 50.74 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 662 LQRQREIAQIREECEQIGQSVLSQQQTLAAvEQDDQQIAADIVQLRKVIeeIRTQQHDRQIQIVRLTQQIERVAQQQAQL 741
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQA-TIDTRTSAFRDLQGQLAH--AKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 742 EIELADLAVQIEEESSQKQQAETELV-VCEAERVELEAQVNQAESACQSSGRALASQRSRVQR-----LSDRLHETAFGE 815
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEQIHLqETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpLTRRMQRGEQTY 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 816 QDCQNRVIDCERRIGMITRNSVILTENMQRLQHA-----------RADLDEST-LTADTVHWQIQRDQHEQALMAVRHEL 883
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltqcdnrsKEDIPNLQnITVRLQDLTEKLSEAEDMLACEQHAL 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 884 ENMDDTLREMEQARMYAEQRLQEcgEAVGQARLREQEAEMTEARFADKLAESGETMLEMVPQFVNEsPAKLQTRINRLTG 963
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQE--LALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA-LQKMQSEKEQLTY 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 964 EVTALGPVNLAALQELEALKSRRIHLEEQSHDLREAITTLE-------QAIRQIDRETRERLQE-TFDQVNQNLAGLFAS 1035
Cdd:TIGR00618 695 WKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAaredalnQSLKELMHQARTVLKArTEAHFNNNEEVTAAL 774
|
....*....
gi 42627761 1036 IFGGGVAEL 1044
Cdd:TIGR00618 775 QTGAELSHL 783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
713-1020 |
6.56e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 713 IRTQQHDRQIQIVRLTQQIERVAQQQ-----AQLEIELADLAVQIEEESSQKQQAE-----------------TELVVCE 770
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARetrdeadevleeheerrEELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 771 AERVELEAQVNQAESACQSSGRALASQRSRVQRLSDR----LHETAFGEQD-----------------CQNRVIDCERRI 829
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddlLAEAGLDDADaeavearreeledrdeeLRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 830 GMITRNSVILTENMQRLQHARADLDE--STLTADTVHWQIQRDQHEQALMAVRHELENMDDTLREMEQARMYAEQRLQEC 907
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREeaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 908 GEAVGQARLREQEAEMTEARFADKLAEsGETMLEM-----VPQFVNESP------------AKLQTRINRLTGEVTALGP 970
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEE-AEALLEAgkcpeCGQPVEGSPhvetieedrervEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 42627761 971 vNLAALQELEALKSRRIHLEEQSHDLREAITTLEQAIRQiDRETRERLQE 1020
Cdd:PRK02224 497 -RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEE-KRERAEELRE 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
665-1016 |
6.63e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 665 QREIAQIREECEQIGQsVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRtQQHDRQIQIVRLTQQIERVAQQQAQLEI- 743
Cdd:COG4717 108 EAELEELREELEKLEK-LLQLLPLYQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEq 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 744 -------ELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESACQSSgrALASQRSRVQRLSDRLHETAFGEQ 816
Cdd:COG4717 186 lslateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA--ALEERLKEARLLLLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 817 DCQNRVIDCERRIGMITRNSVILTENMQRLQHARADLDESTLTADTVHWQIQRDQHEQALMAVRHELENMDDTLREMEQA 896
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 897 RMYAE--QRLQECGEAVGQARLREQEAEMtEARFADKLAESGETMLEMVPQFvnESPAKLQTRINRLTGEVTALGPVNLA 974
Cdd:COG4717 344 DRIEElqELLREAEELEEELQLEELEQEI-AALLAEAGVEDEEELRAALEQA--EEYQELKEELEELEEQLEELLGELEE 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 42627761 975 ALQ--ELEALKSRRIHLEEQSHDLREAITTLEQAIRQIDRETRE 1016
Cdd:COG4717 421 LLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
657-1143 |
7.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 657 AVHGILQRQREIAQIREECEQIGQSVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQ-QHDRQIQIVRLTQQIERVA 735
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 736 QQQAQLEIELADLAVQIEEESSQKQQAETELVV-CEAERVELEAQVNQAESA------CQSSGRALASQRSRVQRLSDRL 808
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAaALEERLKEARLLLLIAAAllallgLGGSLLSLILTIAGVLFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 809 HETAFGEQDCQNRVIDCERRIGMITRNSVILTENMQRLQHARADLDESTLTADTVHWQIQRDQHEQALMAVRHELENMDD 888
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 889 TLREMEQARMYA------EQRLQECGEAVGQARLREQEAEMTEARFADKLAESGETMLEMVPQFVNESPAKLQTRINRLT 962
Cdd:COG4717 366 EELEQEIAALLAeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 963 GEVTALGpVNLAALQ----------ELEALKSRRIHLEEQSHDLREAITTLeQAIRQIDRETRERLQETF-DQVNQNLAG 1031
Cdd:COG4717 446 EELEELR-EELAELEaeleqleedgELAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYREERlPPVLERASE 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1032 LFASIFGGGVAELVlsgediLDAGVQLNAHPPGKRNSSIHLLSGGEKALTALALVFSLFRL---NPAPFcLLDEVDAPLD 1108
Cdd:COG4717 524 YFSRLTDGRYRLIR------IDEDLSLKVDTEDGRTRPVEELSRGTREQLYLALRLALAELlagEPLPL-ILDDAFVNFD 596
|
490 500 510
....*....|....*....|....*....|....*
gi 42627761 1109 DSNSVRFCELVKRMSGETQFLFISHNKITMQMAQQ 1143
Cdd:COG4717 597 DERLRAALELLAELAKGRQVIYFTCHEELVELFQE 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
184-559 |
8.72e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 184 LADARGNLQRVDDILEELDKQQQHLEAQAECAVRYQDLHRQLTAAQHTLWTLhkQQAAESRHQAQVEVERLVQEMETIRS 263
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 264 GMQETGEKLDELRLYHRvvnDRQHQIQGALYAANGEIARIEQNIRHIRANREQLDRQLAEAELQLQNHEQQLNEVNENLT 343
Cdd:COG4717 161 LEEELEELEAELAELQE---ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 344 SWQDKLEQAKNCHLSC--------------KEEHIVEAGKLPQMESAAQADqVRLIGLREKLALARQNEKLlqnQQAYAE 409
Cdd:COG4717 238 AAALEERLKEARLLLLiaaallallglggsLLSLILTIAGVLFLVLGLLAL-LFLLLAREKASLGKEAEEL---QALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 410 KTLHQLvvRRERLLEEQSSQPEIDPVQLDELQMESAELAAMLEQKQHSLSTLETQAYtvQQERDAILQIIQSLERDMARA 489
Cdd:COG4717 314 EELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL--EQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42627761 490 NArcdvlQRLQDQIEDNQELNAWMARL-QLNLLPRLWQQISIESGWETALEAvLRERIQAVTvDRLEQMLE 559
Cdd:COG4717 390 AL-----EQAEEYQELKEELEELEEQLeELLGELEELLEALDEEELEEELEE-LEEELEELE-EELEELRE 453
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
29-119 |
1.04e-05 |
|
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: 48.74 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 29 IVGPNGCGKSNVIDAVRWVLGEsRASALRGESLQDvifngsatrkpigRASVELVFDNSSGKAAGQWKSY------SEIA 102
Cdd:cd03241 26 LTGETGAGKSILLDALSLLLGG-RASADLIRSGAE-------------KAVVEGVFDISDEEEAKALLLElgieddDDLI 91
|
90
....*....|....*..
gi 42627761 103 IRRVIQRDGESSYYINN 119
Cdd:cd03241 92 IRREISRKGRSRYFING 108
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
652-861 |
1.08e-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: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 652 FAPDSAVHGILQRQREIAQIREECEQIGQSVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQQHDRQIQIVRLTQQI 731
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 732 ERVAQQQAQLEIELADLAVQIEEESSQK-------------------------QQAETELVVCEAERVELEAQVNQAESA 786
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42627761 787 CQSSGRALASQRSRVQRLSDRLHETAFGEQDCQNRVIDCERRIGMITRNSVILTENMQRLQHARADLDESTLTAD 861
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1029-1134 |
1.30e-05 |
|
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: 46.47 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1029 LAGLFASIFGggvaELVLSGEDILDAGVQLNAhppgKRNSSIHLLSGGEKALTALALVFslfrLNPAPFCLLDEVDAPLD 1108
Cdd:cd00267 45 IAGLLKPTSG----EILIDGKDIAKLPLEELR----RRIGYVPQLSGGQRQRVALARAL----LLNPDLLLLDEPTSGLD 112
|
90 100
....*....|....*....|....*..
gi 42627761 1109 DSNSVRFCELVKRMSGE-TQFLFISHN 1134
Cdd:cd00267 113 PASRERLLELLRELAEEgRTVIIVTHD 139
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
34-456 |
2.02e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 48.53 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 34 GCGKSNVIDAVRWVLGEsRASAlrgeslqDVIFNGSAtrkpigRASVELVFDNSSGKAAGQW-------KSYSEIAIRRV 106
Cdd:COG0497 32 GAGKSILLDALGLLLGG-RADA-------SLVRHGAD------KAEVEAVFDLSDDPPLAAWleengldLDDGELILRRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 107 IQRDGESSYYINNIHVRR---RDITDMFLgtgvsgrgyAIIEQgmisriiearpqelrtfleeaagitryhekrHETgLR 183
Cdd:COG0497 98 ISADGRSRAFINGRPVTLsqlRELGELLV---------DIHGQ-------------------------------HEH-QS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 184 LADARGnlQRvdDILEELDKQQQHLEAQAECAVRYQDLHRQLTAAQhtlwtlHKQQAAESRH---QAQV----------- 249
Cdd:COG0497 137 LLDPDA--QR--ELLDAFAGLEELLEEYREAYRAWRALKKELEELR------ADEAERARELdllRFQLeeleaaalqpg 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 250 EVERLVQE------METIRSGMQETGEKLDElrlyhrvvndRQHQIQGALYAANGEIARIEQNIRHIRANREQLDR---Q 320
Cdd:COG0497 207 EEEELEEErrrlsnAEKLREALQEALEALSG----------GEGGALDLLGQALRALERLAEYDPSLAELAERLESaliE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 321 LAEAELQLQNH-------EQQLNEVNENLTSWQDkleqaknchLSCKeeHIVEAGKLPQMESAAQADQVRLIGLREKLA- 392
Cdd:COG0497 277 LEEAASELRRYldslefdPERLEEVEERLALLRR---------LARK--YGVTVEELLAYAEELRAELAELENSDERLEe 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42627761 393 LARQNEKLLQNQQAYAEKtLHQLvvRRE--RLLEEQSSQpeidpvQLDELQMESAELAAMLEQKQH 456
Cdd:COG0497 346 LEAELAEAEAELLEAAEK-LSAA--RKKaaKKLEKAVTA------ELADLGMPNARFEVEVTPLEE 402
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
198-520 |
2.14e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 198 LEELDKQQQHLEAQaecavrYQDLHRQLTAAQHTLwtlhKQQAAESRhqAQVEVERLVQEMETIRSGMQETGEKLDELRL 277
Cdd:PRK04863 316 LAELNEAESDLEQD------YQAASDHLNLVQTAL----RQQEKIER--YQADLEELEERLEEQNEVVEEADEQQEENEA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 278 YHRVVNDRQHQIQGALyaANGEIARIEQNIRHIRANreQLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKNCHL 357
Cdd:PRK04863 384 RAEAAEEEVDELKSQL--ADYQQALDVQQTRAIQYQ--QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 358 SCKEEHIVEAGKLPQMESAAQAdqVRLIG-----------LREKLALAR------QNEKLLQNQQAYAEKTL--HQLVVR 418
Cdd:PRK04863 460 SLEQKLSVAQAAHSQFEQAYQL--VRKIAgevsrseawdvARELLRRLReqrhlaEQLQQLRMRLSELEQRLrqQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 419 RERLLEEQSSQPEIDPVQLDELQmesAELAAMLEQKQHSLSTLETQAYTVQQERDAILQIIQSLERDMARANARCDVLQR 498
Cdd:PRK04863 538 LLAEFCKRLGKNLDDEDELEQLQ---EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR 614
|
330 340
....*....|....*....|....*.
gi 42627761 499 LQDQ----IEDNQELNAWMARLQLNL 520
Cdd:PRK04863 615 LREQsgeeFEDSQDVTEYMQQLLERE 640
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
697-1032 |
2.28e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.59 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 697 QQIAADIVQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVEL 776
Cdd:pfam07111 313 EKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 777 EAQVNQAESACQSSGRALASQRSRVQRLSDRLHETAFGEQDCQNRVIDCERRI----GMITRNSVI-------------- 838
Cdd:pfam07111 393 QQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVhtikGLMARKVALaqlrqescpppppa 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 839 ------LTENMQRLQHARADLD-ESTLTADTVHWQIQRDQHEQALmavrhELENMDDTLREMEQARMYAEQRLQECGEAV 911
Cdd:pfam07111 473 ppvdadLSLELEQLREERNRLDaELQLSAHLIQQEVGRAREQGEA-----ERQQLSEVAQQLEQELQRAQESLASVGQQL 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 912 GQARLREQEAEMTEARFADKLAESGETMLEMVPQFVNESPAKLQTRINRLTGEVTALGPVNLAALQELEALKSRRIHLEE 991
Cdd:pfam07111 548 EVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKE 627
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 42627761 992 QSHDLREaitTLEQAIRQIDRETRERLQETFDQVNQNLAGL 1032
Cdd:pfam07111 628 RNQELRR---LQDEARKEEGQRLARRVQELERDKNLMLATL 665
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
665-801 |
2.61e-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: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 665 QREIAQIREECEQIGQSVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQQHD----RQIQIvrLTQQIERVAQQQAQ 740
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKEYEA--LQKEIESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42627761 741 LEIELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESACQSSGRALASQRSRV 801
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-492 |
2.81e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDPAVVPVPGNLVgIVGPNGCGKSNVIDAVRWVLgesrASALRGESLQDVIfngsatRKPIGRASV 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINI-ITGKNGAGKSSIVDAIRFAL----FTDKRTEKIEDMI------KKGKNNLEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 81 ELVFdNSSGKAAGQWKSYSE----IAIRRVIQRDGE---------SSYYINNIHVRRRDItdmFLGTGVSGrgyaiieQG 147
Cdd:PRK01156 70 ELEF-RIGGHVYQIRRSIERrgkgSRREAYIKKDGSiiaegfddtTKYIEKNILGISKDV---FLNSIFVG-------QG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 148 MISRIIEARPQELRTFLEEAAGITRYHEKRHETGLRLADARGNLQRVDDILEELDKQQQHLEaqaecavryqDLHRQLT- 226
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----------NIKKQIAd 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 227 -AAQHTLwTLHKQQAAESRHQAQVEverlvqEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQGALyAANGEIARIEQ 305
Cdd:PRK01156 209 dEKSHSI-TLKEIERLSIEYNNAMD------DYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMEL-EKNNYYKELEE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 306 NIRHIRANREQLDRQLAEAELQLQNHEQQLNEVNENLTSwqdkleqakncHLSCKEEHIVEAGKLPQMESAAQADQVRLI 385
Cdd:PRK01156 281 RHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA-----------EINKYHAIIKKLSVLQKDYNDYIKKKSRYD 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 386 GLREKLALARQNEkllQNQQAYAeKTLHQLVVRRERLLEEQSSQPEIDPVQLDELQMESAELAAMLEQKQHSLSTLETQA 465
Cdd:PRK01156 350 DLNNQILELEGYE---MDYNSYL-KSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKV 425
|
490 500
....*....|....*....|....*..
gi 42627761 466 YTVQQERDAILQIIQSLERDMARANAR 492
Cdd:PRK01156 426 SSLNQRIRALRENLDELSRNMEMLNGQ 452
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
29-992 |
2.83e-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: 48.50 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 29 IVGPNGCGKSNVIDAVRWVLGESRASALRGESLqdvIFNGSATRKPIGRASVELVFDN--------------SSGKAAGQ 94
Cdd:TIGR00606 33 LVGPNGAGKTTIIECLKYICTGDFPPGTKGNTF---VHDPKVAQETDVRAQIRLQFRDvngeecavvrsmvcTQKTKKTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 95 WKSYSEIAIRrviQRDGEssyyINNIHVRRRDI-TDMFLGTGVSGR--GYAIIEQGMISRIIEARPQELRTFLEEAAGIT 171
Cdd:TIGR00606 110 FKTLEGVITR---YKHGE----KVSLSSKCAEIdREMISHLGVSKAvlNNVIFCHQEDSNWPLSEGKALKQKFDEIFSAT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 172 RYHE----------------KRHETGLRLADArgNLQRVDDILEELDKQQQHLEAQAECAVRYQD----LHRQLTAAQHT 231
Cdd:TIGR00606 183 RYIKaletlrqvrqtqgqkvQEHQMELKYLKQ--YKEKACEIRDQITSKEAQLESSREIVKSYENeldpLKNRLKEIEHN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 232 LWTLHK-QQAAESRHQAQVEVERLVQEMETIRSGM-QETGEKLDELRLYH-RVVNDRQHQiqgaLYAANGEIARIEQNIR 308
Cdd:TIGR00606 261 LSKIMKlDNEIKALKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHqRTVREKERE----LVDCQRELEKLNKERR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 309 HIRANREQLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKNCHLSCKEEHIVEAGKL--PQMESAAQADQVRLIG 386
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLviERQEDEAKTAAQLCAD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 387 LREKLALARQN-----------EKLLQNQQAYAEKTLHQLVVRRERLLEEQSSQPEIdpVQLDElQMESAELAAMLEQKQ 455
Cdd:TIGR00606 417 LQSKERLKQEQadeirdekkglGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI--LELDQ-ELRKAERELSKAEKN 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 456 HSLSTLETQAYTVQQERDAILQIIQSLERDMARAN----ARCDVLQRLQDQIEDNQEL--NAWMARLQLNLLPRLWQQIS 529
Cdd:TIGR00606 494 SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhttTRTQMEMLTKDKMDKDEQIrkIKSRHSDELTSLLGYFPNKK 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 530 IESGWETALEA---VLRERIQAVT--VDRLEQML--------EWEAQRPSAKWAVCELVPDRPVSNDTDqRTWKPLSTLL 596
Cdd:TIGR00606 574 QLEDWLHSKSKeinQTRDRLAKLNkeLASLEQNKnhinneleSKEEQLSSYEDKLFDVCGSQDEESDLE-RLKEEIEKSS 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 597 SCRSP--AVQAVLGNWLYGVFVTDSLTAALADRSLLTSGEML-VTAEGHSITSCGVSYFAPDSAVHGILQRQREIAQIRE 673
Cdd:TIGR00606 653 KQRAMlaGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQeFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 674 ECEQigQSVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQ--------------QHDRQIqIVRLTQQIE----RVA 735
Cdd:TIGR00606 733 PGRQ--SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpeeesakvcLTDVTI-MERFQMELKdverKIA 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 736 QQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVE-LEAQVNQAESACQSSGRALASQR-------SRVQRLSDR 807
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRkLIQDQQEQIQHLKSKTNELKSEKlqigtnlQRRQQFEEQ 889
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 808 LHETAFGEQDCQNRVIDCERRIG--------MITRNSVILTENMQRLQHARADLDESTLTADTVHWQIQ------RDQHE 873
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSpletflekDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKdienkiQDGKD 969
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 874 QALMAVRHELENMDDTLREMEQARMYAEQRLQECGEAVGQARLREQ--EAEMTEARFADKLAESGETMLEMVPQFVNESP 951
Cdd:TIGR00606 970 DYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlQDNLTLRKRENELKEVEEELKQHLKEMGQMQV 1049
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 42627761 952 AKLQTRINRLTGEVTALGPVNLAALQELEALKSRRIHLEEQ 992
Cdd:TIGR00606 1050 LQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKE 1090
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
314-1030 |
3.34e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 314 REQLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKnCHLSCKEEHIveagklpQMESAAQADQVRliglREKlal 393
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSV-IDLQTKLQEM-------QMERDAMADIRR----RES--- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 394 arQNEKLLQNQqayAEKTLHQLVVRR---ERLLEEQSSQpeIDPVQLDELQMESA--ELAAML---EQ-------KQHSL 458
Cdd:pfam15921 138 --QSQEDLRNQ---LQNTVHELEAAKclkEDMLEDSNTQ--IEQLRKMMLSHEGVlqEIRSILvdfEEasgkkiyEHDSM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 459 STLETQAYTvqqerDAILQIIQSLERDMARANARC----DVLQRLQDQIEDNQELnawmarLQLNLLPRLWQQISIESGW 534
Cdd:pfam15921 211 STMHFRSLG-----SAISKILRELDTEISYLKGRIfpveDQLEALKSESQNKIEL------LLQQHQDRIEQLISEHEVE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 535 ETAL-EAVLRERIQAVTVDRLEQMLEWEAQRPSAKWaVCELvpdrpvsNDTDQRTWKPLSTLLSCRSPAVQAVLGNWLYG 613
Cdd:pfam15921 280 ITGLtEKASSARSQANSIQSQLEIIQEQARNQNSMY-MRQL-------SDLESTVSQLRSELREAKRMYEDKIEELEKQL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 614 VFVTDSLTAALADRSLLT--SGEMlvtaeghsitscgvsyfapDSAVHGIL----QRQREIAQIREECEQIGQSVLSQQQ 687
Cdd:pfam15921 352 VLANSELTEARTERDQFSqeSGNL-------------------DDQLQKLLadlhKREKELSLEKEQNKRLWDRDTGNSI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 688 TLAAV--EQDDQQIaaDIVQLRKVIEEIRTQ---QHDRQIQIVR-LTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQ 761
Cdd:pfam15921 413 TIDHLrrELDDRNM--EVQRLEALLKAMKSEcqgQMERQMAAIQgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMT 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 762 AETElvvcEAERVELEAQVNQAESACQSSGRALASQRSRVQRLSDRLHETAFGEQDCQNRVIDCER-RIGMITRNSVI-- 838
Cdd:pfam15921 491 LESS----ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAlKLQMAEKDKVIei 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 839 ---LTENMQRL--QHARadldestlTADTVhwQIQRDQHEQALMAVRHELENM-------DDTLREME------------ 894
Cdd:pfam15921 567 lrqQIENMTQLvgQHGR--------TAGAM--QVEKAQLEKEINDRRLELQEFkilkdkkDAKIRELEarvsdlelekvk 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 895 -----QARMYA--------EQRLQECGEAVGQARLREQEAEMTEARFADKLAESGETMLEMVPQFVNESPAKLQTRiNRL 961
Cdd:pfam15921 637 lvnagSERLRAvkdikqerDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR-NTL 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42627761 962 TGEVTALGPVNLAALQELEALKSRRIHLEEqshdLREAITTLEQAIRQIDREtRERLQETFDQVNQNLA 1030
Cdd:pfam15921 716 KSMEGSDGHAMKVAMGMQKQITAKRGQIDA----LQSKIQFLEEAMTNANKE-KHFLKEEKNKLSQELS 779
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-49 |
3.39e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.91 E-value: 3.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDPAV-VPVPGNLVGIVGPNGCGKSNVIDAVRWVLG 49
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIdFDNPPRLTVLVGENGSGKTTLLEAIALALS 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
728-1032 |
4.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 728 TQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNqaesacqssgraLASQRSRVQRLSDR 807
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID------------VASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 808 LHEtafgeqdcqnrvidcerrigmITRNSVILTENMQRLQHARADLDESTLTADTVhwQIQRDQHEQALMAVRHELENMD 887
Cdd:COG4913 677 LER---------------------LDASSDDLAALEEQLEELEAELEELEEELDEL--KGEIGRLEKELEQAEEELDELQ 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 888 DTLREMEQarMYAEQRLQECGEAVGQARLREQEAEMTEA-----RFADKLAESGETMLEmvpqfvnespaKLQTRINRLT 962
Cdd:COG4913 734 DRLEAAED--LARLELRALLEERFAAALGDAVERELRENleeriDALRARLNRAEEELE-----------RAMRAFNREW 800
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42627761 963 GEVTALGPVNLAALQELEALKSR--RIHLEEQSHDLREAITTLEQA-----IRQIDREtRERLQETFDQVNQNLAGL 1032
Cdd:COG4913 801 PAETADLDADLESLPEYLALLDRleEDGLPEYEERFKELLNENSIEfvadlLSKLRRA-IREIKERIDPLNDSLKRI 876
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-120 |
4.29e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 46.96 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 3 LTEIKLAGFKTFVDPAVV------PVPGNLVGIVGPNGCGKSNVIDAVRWVLGESRASALRGESL-QDVIFNGSATRKPi 75
Cdd:COG1106 2 LISFSIENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLvEPFLLDSESKNEP- 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 42627761 76 grASVELVFDNSsgkaaGQWKSYSEIAIRRVIQRdgESSYYINNI 120
Cdd:COG1106 81 --SEFEILFLLD-----GVRYEYGFELDKERIIS--EWLYFLSTA 116
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
719-1013 |
7.53e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 719 DRQIQIVRLTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERVELE-------AQVNQAESACQSSG 791
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleserAARNKAEKQRRDLG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 792 RALASQRSrvqRLSDRLHETAfGEQDCQNR----VIDCERRIGMITRNSVILTENMqRLQHARAdLDESTLTADtvhwQI 867
Cdd:pfam01576 299 EELEALKT---ELEDTLDTTA-AQQELRSKreqeVTELKKALEEETRSHEAQLQEM-RQKHTQA-LEELTEQLE----QA 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 868 QRDQH--EQALMAVRHELENMDDTLREMEQARMYAEQRLQECGEAVGQARLREQEAEMTEARFADKLAEsGETMLEMVPQ 945
Cdd:pfam01576 369 KRNKAnlEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELESVSS 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42627761 946 FVNESPAKLqtriNRLTGEVTALGPvNLAALQELE--------ALKSRRIHLEEQSHDLREAITTLEQAIRQIDRE 1013
Cdd:pfam01576 448 LLNEAEGKN----IKLSKDVSSLES-QLQDTQELLqeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQ 518
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
238-476 |
2.33e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 238 QQAAESRHQAQVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQGALYAANGEIARIEQNIRHIRANREQL 317
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 318 DRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKNCHLSCKEEHIVEAGKLPQMESAAQADQVRLIGLREKLALARQN 397
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42627761 398 EKLLQNQQAYAEKTLHQLVVRRERLLEEQSSQPEIDPVQLDELQMESAELAAMLEQKQHSLSTLETQAYTVQQERDAIL 476
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-125 |
2.58e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 44.76 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 2 RLTEIKLAGFKTFVDpAVVPVPGNLVGIVGPNGCGKSNVIDAVrWVLgeSRASALRGESLQDVIFNGSAtrkpigRASVE 81
Cdd:COG1195 1 RLKRLSLTNFRNYES-LELEFSPGINVLVGPNGQGKTNLLEAI-YLL--ATGRSFRTARDAELIRFGAD------GFRVR 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 42627761 82 LVFDNSSGKaagqwksySEIAIRrvIQRDGESSYYINNIHVRRR 125
Cdd:COG1195 71 AEVERDGRE--------VRLGLG--LSRGGKKRVRINGKPVRRL 104
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1067-1145 |
4.15e-04 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 42.37 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1067 NSSIH--LLSGGEKALTALALVFslfrLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMSGETQFLFISHNKITMQMAQQL 1144
Cdd:cd03228 89 SGTIRenILSGGQRQRIAIARAL----LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRI 164
|
.
gi 42627761 1145 I 1145
Cdd:cd03228 165 I 165
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
663-915 |
4.76e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 663 QRQREIAQIREECEQIGQSVLSQQQTLAAVE-------QDDQQIAadivQLRKVIEEIRTQQHDRQIQIVRLTQQIERVA 735
Cdd:PRK04863 894 DRVEEIREQLDEAEEAKRFVQQHGNALAQLEpivsvlqSDPEQFE----QLKQDYQQAQQTQRDAKQQAFALTEVVQRRA 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 736 ----QQQAQLEIELADLAVQIEEESSQKQQaetelvvceaERVELEAQVNQAESACQSSGRALASQRSRVQRLSDRLHET 811
Cdd:PRK04863 970 hfsyEDAAEMLAKNSDLNEKLRQRLEQAEQ----------ERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 812 afgEQDCQNrvidcerrIGmitrnsVILTENMQrlqhARADLDESTLTADTVHWQIQRDQHEQALMAVRHELENMDDTLR 891
Cdd:PRK04863 1040 ---KQELQD--------LG------VPADSGAE----ERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
250 260
....*....|....*....|....
gi 42627761 892 EMEqaRMYAEQRlqecgEAVGQAR 915
Cdd:PRK04863 1099 KLE--RDYHEMR-----EQVVNAK 1115
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
984-1134 |
5.47e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.77 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 984 SRRIHLEEQSHDLREAIttleQAIRQIDRETRERLQETFDQVNQNLAGLFASIFGGGVAELVLSGEDILDagvQLNAHpp 1063
Cdd:COG4637 187 GRTPVLAPDGSNLAAVL----ATLRETHPERFERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKGLDR---PFPAR-- 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42627761 1064 gkrnssihLLSGGekALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMSGETQFLFISHN 1134
Cdd:COG4637 258 --------ELSDG--TLRFLALLAALLSPRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHS 318
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
179-510 |
6.14e-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: 44.34 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 179 ETGLRLADA-RGNLQRVDDILEELDKQQ---QHLEA-----QAECAvryQDLHRQLTAAQHTLWTLHKQQAAESRHQAQV 249
Cdd:pfam15921 398 EQNKRLWDRdTGNSITIDHLRRELDDRNmevQRLEAllkamKSECQ---GQMERQMAAIQGKNESLEKVSSLTAQLESTK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 250 EVERLVQEMETIRSGMQETGEkldelrlyhRVVNDRQHQIQG---ALYAANGEIARIE-------QNIRHIRANREQLDR 319
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSE---------RTVSDLTASLQEkerAIEATNAEITKLRsrvdlklQELQHLKNEGDHLRN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 320 QLAEAE-LQLQNHEQQ-----LNEVNENLTSW--------------QDKLEQAKN-CHLSCKEEHIVEA---GKLPQME- 374
Cdd:pfam15921 546 VQTECEaLKLQMAEKDkvieiLRQQIENMTQLvgqhgrtagamqveKAQLEKEINdRRLELQEFKILKDkkdAKIRELEa 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 375 --SAAQADQVRLIG-----LREKLALARQNEKLLqNQQAYAEKTLHQLVVRRERLLEEQSSQPEIDPVQLDELQMESAEL 447
Cdd:pfam15921 626 rvSDLELEKVKLVNagserLRAVKDIKQERDQLL-NEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSA 704
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42627761 448 AAMLEQKQHSLSTLE--------------TQAYTVQQERDAILQIIQSLERDMARANARCDVLQRLQDQIedNQELN 510
Cdd:pfam15921 705 QSELEQTRNTLKSMEgsdghamkvamgmqKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKL--SQELS 779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
238-352 |
7.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 238 QQAAESRHQAQVEVERLVQEMETIR------SGMQETGEKLDELRLYHRVVNDRQHQIQgALYAANGEIARIEQNIRHIR 311
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQerrealQRLAEYSWDEIDVASAEREIAELEAELE-RLDASSDDLAALEEQLEELE 698
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 42627761 312 ANREQLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQA 352
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
158-509 |
8.18e-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: 43.57 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 158 QELRTFL---EEAAGITRYHEKRHETG------------LRLADA-----RGNLQRVDDILEELDKQQQH-LEAQAEcav 216
Cdd:pfam15921 187 QEIRSILvdfEEASGKKIYEHDSMSTMhfrslgsaiskiLRELDTeisylKGRIFPVEDQLEALKSESQNkIELLLQ--- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 217 RYQDLHRQLTAAQHTLWTLHKQQAAESRHQA---QVEVErLVQEMETIRSGM--------QETGEKL-DELRLYHRVVND 284
Cdd:pfam15921 264 QHQDRIEQLISEHEVEITGLTEKASSARSQAnsiQSQLE-IIQEQARNQNSMymrqlsdlESTVSQLrSELREAKRMYED 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 285 RQHQIQGALYAANGEIARIEQNIRHIRANREQLDRQLAEAELQLQNHEQQLN-EVNENLTSW-QDKLEQAKNCHLSCK-E 361
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlEKEQNKRLWdRDTGNSITIDHLRRElD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 362 EHIVEAGKLPQMESAAQAD---QVRliglREKLALARQNEKL--LQNQQAYAEKTLHQLvvrrERLLEEQSSQpeidPVQ 436
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSEcqgQME----RQMAAIQGKNESLekVSSLTAQLESTKEML----RKVVEELTAK----KMT 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 437 LDELQMESAELAAMLEQKQHSLSTLETQAYTVQQERDAILQIIQSLERD---MARANARCD-----------VLQRLQDQ 502
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEalklqmaekdkVIEILRQQ 570
|
....*..
gi 42627761 503 IEDNQEL 509
Cdd:pfam15921 571 IENMTQL 577
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
665-816 |
8.71e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 665 QREIAQIREECEQIGQSVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQLEIE 744
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42627761 745 LADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESACQSSGRALASQRSRVQRLSDRLHETAFGEQ 816
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1066-1175 |
9.01e-04 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 42.32 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1066 RNSSIHLLSGGEKALTALALVFSLfrlnpAPFCL-LDEVDAPLDDSNSVRFCELVKRMSGE-TQFLFISHNkitMQMAQQ 1143
Cdd:COG1122 128 ADRPPHELSGGQKQRVAIAGVLAM-----EPEVLvLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHD---LDLVAE 199
|
90 100 110
....*....|....*....|....*....|..
gi 42627761 1144 LigvtmreqgVSRVVTVDIGKIMAAGDlPASV 1175
Cdd:COG1122 200 L---------ADRVIVLDDGRIVADGT-PREV 221
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-350 |
1.30e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 153 IEARPQELRTFLEEAAGITRYHEKRHETGLRLADARGNLQRVDDILEELDKQQQHLEAQAECA-VRYQDLHRQLTAAQHT 231
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKrEAAAEAEEEAEEAREE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 232 LWTLHKQQAA-ESRHQA-------QVEVERLVQEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQGALYAANGE---- 299
Cdd:PRK02224 574 VAELNSKLAElKERIESlerirtlLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEeare 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 42627761 300 --------IARIEQNIRHIRANREQLDRQLAEAELQLQNHEqQLNEVNENLTSWQDKLE 350
Cdd:PRK02224 654 dkeraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREALENRVEALE 711
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
304-505 |
1.45e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 304 EQNIRHIRANREQLDRQLAEAELQLQNHEQQLNEVNENLT---------------SWQDKLEQAKNCHLSCKE------E 362
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSalnrllprlnlladeTLADRVEEIREQLDEAEEakrfvqQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 363 HIVEAGKLPQMESAAQADQVRLIGLREKLALARQNEKLLQnQQAYAektLHQLVVRRERLLEEQSSQPEIDPVQLDELqm 442
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAK-QQAFA---LTEVVQRRAHFSYEDAAEMLAKNSDLNEK-- 989
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42627761 443 esaeLAAMLEQKQHSLSTLETQAYTVQQERDAILQIIQSLErdmARANARCDVLQRLQDQIED 505
Cdd:PRK04863 990 ----LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLK---SSYDAKRQMLQELKQELQD 1045
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1073-1156 |
1.89e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1073 LSGGEKALTALALVFSLFRL--NPAPFCLLDEVDAPLDDSN-SVRFCELVKRMSGETQFLFI--SHNKITMQMAQQLIGV 1147
Cdd:cd03240 116 CSGGEKVLASLIIRLALAETfgSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKNFQLIviTHDEELVDAADHIYRV 195
|
....*....
gi 42627761 1148 TMREQGVSR 1156
Cdd:cd03240 196 EKDGRQKSR 204
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
723-937 |
1.98e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 723 QIVRLTQQIERVAQQQAQLEIELADLAVQIEEESSQKQQAETELVVCEAERV------ELEAQVNQAESACQSSGRALAS 796
Cdd:PRK11281 67 QTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAQTLDQLQNAQNDLAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 797 QRSRVQRLSDRLHetafgeqdcqnrvidcerrigmitRNSVILTENMQRLQHARADLDESTLT-ADTVHWQIQRDQHEQA 875
Cdd:PRK11281 147 YNSQLVSLQTQPE------------------------RAQAALYANSQRLQQIRNLLKGGKVGgKALRPSQRVLLQAEQA 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42627761 876 LMAV-----RHELENmDDTLREMEQA-RMYA-------EQRLQECGEAVGQARLREQEAEMTEARFADKLAESGE 937
Cdd:PRK11281 203 LLNAqndlqRKSLEG-NTQLQDLLQKqRDYLtariqrlEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQA 276
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-514 |
2.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDPAVVPVPGNLVgIVGPNGCGKSNVIDAVRWVLgesrASALRGEslQDVIFNGSATRKPIGRASV 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNV-IYGPNEAGKSTLLAFIRAML----LERLEKE--ADELFKPQGRKPELNLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 81 ELVfdnssgKAAGQWKSYSEIAIRRVIQRDGESSYYINNIHVRRRDITDMFLGTGVSGRGYAIIEQgmisriIEARPQEL 160
Cdd:COG4717 74 KEL------EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE------LEALEAEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 161 RTFLEEAAGITRYHEKRHETGLRLADARGNLQRVDDILEEL--DKQQQHLEAQAECAVRYQDLHRQLTAAQHTLwtlhkQ 238
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEELQQRLAELEEEL-----E 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 239 QAAESRHQAQVEVERLVQEMETirsgmQETGEKLDELRL-------------YHRVVNDRQHQIQGALYAANGEIArieq 305
Cdd:COG4717 217 EAQEELEELEEELEQLENELEA-----AALEERLKEARLllliaaallallgLGGSLLSLILTIAGVLFLVLGLLA---- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 306 nIRHIRANREQLDRQLAEAELQLQNHEQQLNEvnenltswQDKLEQAKNCHLScKEEHIVEAGKLPQMESAAQADQVRLI 385
Cdd:COG4717 288 -LLFLLLAREKASLGKEAEELQALPALEELEE--------EELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 386 GLREKLALAR---QNEKLLQNQQAYAEKTL---HQLVVRRERLLEEQSS-----QPEIDPVQLDELQMESAELAAMLEQK 454
Cdd:COG4717 358 ELEEELQLEEleqEIAALLAEAGVEDEEELraaLEQAEEYQELKEELEEleeqlEELLGELEELLEALDEEELEEELEEL 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 455 QHSLSTLETQAYTVQQERDAILQIIQSLERDMARANARcDVLQRLQDQIEdnQELNAWMA 514
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGELAELL-QELEELKAELR--ELAEEWAA 494
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
666-810 |
2.37e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 666 REIAQIREECEQIgqsvlsqQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQL--EI 743
Cdd:COG1579 17 SELDRLEHRLKEL-------PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42627761 744 ELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESACQSSGRALASQRSRVQRLSDRLHE 810
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1069-1132 |
2.46e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 40.66 E-value: 2.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42627761 1069 SIHLLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSNSVRFCELVKRMS---GETQFLFIS 1132
Cdd:cd03277 123 DPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETAckeGTSQYFLIT 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
314-509 |
2.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 314 REQLDRQLAEAELQLQNHEQQLNEVNENLTSWQDKLE--QAKNCHLSCKEEHIVEAGKLPQMESAAQADQVRLIGLREKL 391
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 392 ALARQNEKLLQNQQAYA---------EKTLHQLVVRRERLLEE-QSSQPEIdpVQLDElQMESAElAAMLEQKQHSLSTL 461
Cdd:COG3206 243 AALRAQLGSGPDALPELlqspviqqlRAQLAELEAELAELSARyTPNHPDV--IALRA-QIAALR-AQLQQEAQRILASL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 42627761 462 ETQAYTVQQERDAILQIIQSLERDMARANARCDVLQRLQDQIEDNQEL 509
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
663-929 |
3.37e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 663 QRQREIAQIREECEQIGQSVLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQQHDRQIQIVRLTQQIERVAQQQAQLE 742
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 743 IELADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESAcqSSGRALASQRSRVQRLSDRLHETAFGEQDCQNRV 822
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 823 IDCERRIGMITRNSVILTENMQRLQHARADLDESTLTADTVHWQIQRDQHEQALMAVRHELENMDDTLREMEQARMYAEQ 902
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250 260
....*....|....*....|....*..
gi 42627761 903 RLQECGEAVGQARLREQEAEMTEARFA 929
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAA 320
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-44 |
3.93e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.15 E-value: 3.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 42627761 5 EIKLAGFKTFVDPAVVPV-----PGNLVGIVGPNGCGKSNVIDAV 44
Cdd:cd00267 1 EIENLSFRYGGRTALDNVsltlkAGEIVALVGPNGSGKSTLLRAI 45
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
29-87 |
4.00e-03 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 39.89 E-value: 4.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 29 IVGPNGCGKSNVIDAVRWVLGeSRASAL-RGESLQDVIFNGSATrkpigrASVELVFDNS 87
Cdd:cd03276 26 IVGNNGSGKSAILTALTIGLG-GKASDTnRGSSLKDLIKDGESS------AKITVTLKNQ 78
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
666-808 |
4.64e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 666 REIAQIREECEQIGQSVLSQQQTLAAVEQDDQQIAADIVQLRkviEEIRTQQHDRQiqivRLTQQIERVAQQQAQLEIEL 745
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLR---ASLSAAEAERS----RLQALLAELAGAGAAAEGRA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42627761 746 ADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESACQSSGRALASQRSRVQRLSDRL 808
Cdd:PRK09039 119 GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
315-509 |
4.94e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 315 EQLDRQLAEAEL---QLQNHEQQLNEVNENLTSWQDKLEQAKNCHLSckeehiveAGKLPQMESAAQADQVRLIGLREKL 391
Cdd:PRK11281 73 DKIDRQKEETEQlkqQLAQAPAKLRQAQAELEALKDDNDEETRETLS--------TLSLRQLESRLAQTLDQLQNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 392 ALArqNEKL--LQNQQAYAEKTLHQLVVR----RERLLEEQSSQPEIDPVQLDELQMESAELAAMLEQKQHSLstletQA 465
Cdd:PRK11281 145 AEY--NSQLvsLQTQPERAQAALYANSQRlqqiRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSL-----EG 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 42627761 466 YTVqqerdaiLQIIQSLERDMARANarcdvLQRLQDQIEDNQEL 509
Cdd:PRK11281 218 NTQ-------LQDLLQKQRDYLTAR-----IQRLEHQLQLLQEA 249
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
175-523 |
5.60e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 175 EKRHETGLRLADARGNLQ-RVDDILEELDKQQQHLEAQAEcavRYQDLHRQLTAAQHTLWT-LHKQQAAESRHQAQVEVE 252
Cdd:pfam12128 481 EAANAEVERLQSELRQARkRRDQASEALRQASRRLEERQS---ALDELELQLFPQAGTLLHfLRKEAPDWEQSIGKVISP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 253 RLVQEME-----TIRSGMQET---GEKLDELRLYH-------RVVNDRQHQIQGALYAANGEIARIEQNIRHIRANREQL 317
Cdd:pfam12128 558 ELLHRTDldpevWDGSVGGELnlyGVKLDLKRIDVpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 318 DRQLAEAELQLQNHEQQLNEVNENLTSWQDKLEQAKNCHLSCKEEHIVEAGKlpqmesaaqadQVRLIGLREKLALARQN 397
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEA-----------QLKQLDKKHQAWLEEQK 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 398 EKLLQNQQAYAEKTlhqlvvrreRLLEEQSSqpeidpVQLDELqmeSAELAAMLEQKQHSLSTLETQAYTVQQERDAILQ 477
Cdd:pfam12128 707 EQKREARTEKQAYW---------QVVEGALD------AQLALL---KAAIAARRSGAKAELKALETWYKRDLASLGVDPD 768
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 42627761 478 IIQSLERDMAranarcDVLQRLQDQIEDNQELNAWMARLQLNLLPR 523
Cdd:pfam12128 769 VIAKLKREIR------TLERKIERIAVRRQEVLRYFDWYQETWLQR 808
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1058-1138 |
5.62e-03 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 39.50 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1058 LNAHPPGKRNSSIhlLSGGEKALTALALVFSLFRLNPAPFCLLDEVDAPLDDSN---SVRFceLVKRMSGE--TQFLFIS 1132
Cdd:cd03276 97 LTSNKAAVRDVKT--LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNrkiSTDL--LVKEAKKQpgRQFIFIT 172
|
....*.
gi 42627761 1133 HNKITM 1138
Cdd:cd03276 173 PQDISG 178
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-90 |
5.84e-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: 39.56 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 1 MRLTEIKLAGFKTFVDPAVVPVPG----NLVGIVGPNGCGKSNVIDAVRWVL-GESRASAlRGESLQDVIFNGSATrkpi 75
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFTGldnnGLFLICGPTGAGKSTILDAITYALyGKTPRYG-RQENLRSVFAPGEDT---- 75
|
90
....*....|....*
gi 42627761 76 grASVELVFDNSSGK 90
Cdd:cd03279 76 --AEVSFTFQLGGKK 88
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-508 |
6.23e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 185 ADARGNLQRVDDILEELDKQQQHLEAQAEcavRYQDLHRQLTAAQHTLWTLHKQQAAESRHQAQ---------VEVERLV 255
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELRE---ERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpVEGSPHV 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 256 QEMETIRSGMQETGEKLDELRLYHRVVNDRQHQIQgalyaangEIARIEQNIRHIRANREQLDRQLAEAELQLQNHEQQL 335
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 336 NEVNENL----TSWQDKLEQAKNCHLSCkEEHIVEAGKLPQMESAAQADQVRLIGLREKLALARQNEKLLQNQQAYAEKT 411
Cdd:PRK02224 540 EELRERAaeleAEAEEKREAAAEAEEEA-EEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 412 LHQLVVRRERLLE--EQSSQ--PEIDPVQLDELQMESAELAAMLEQKQHSLSTLETQAYTVQQERDAILQIIQSLE--RD 485
Cdd:PRK02224 619 AELNDERRERLAEkrERKREleAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelRE 698
|
330 340
....*....|....*....|....
gi 42627761 486 -MARANARCDVLQRLQDQIEDNQE 508
Cdd:PRK02224 699 rREALENRVEALEALYDEAEELES 722
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-53 |
6.30e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 6.30e-03
10 20
....*....|....*....|....*...
gi 42627761 26 LVGIVGPNGCGKSNVIDAVRWVLGESRA 53
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDAL 28
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-173 |
8.72e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 39.59 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 3 LTEIKLAGFKTFvDPAVVPVPGNLVGIVGPNGCGKSNVIDAVRWVlgeSRASALRGESLQDVIFNGsatrKPIGRASVEL 82
Cdd:cd03242 1 LKSLELRNFRNY-AELELEFEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELIRWG----AEEAKISAVL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 83 VFDNSSGKAAGQWKSYSeiaiRRVIQrdgessyyINNIHVRRrdiTDMFLGTGvsgrgyaiieqgmisRIIEARPQELRT 162
Cdd:cd03242 73 ERQGGELALELTIRSGG----GRKAR--------LNGIKVRR---LSDLLGVL---------------NAVWFAPEDLEL 122
|
170
....*....|.
gi 42627761 163 FLEEAAGITRY 173
Cdd:cd03242 123 VKGSPADRRRF 133
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
413-855 |
9.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 413 HQLVVRRERLLEEQSSQPEIDPVQLDELQMESAELAAMLEQKQHSLSTLET---------QAYTVQQERDAILQIIQSLE 483
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREeleklekllQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 484 RDMARANARCDVLQRLQDQIEDNQELNAwMARLQLNLLPRLWQQiSIESGWETALEAV--LRERIQavtvdRLEQMLEWE 561
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELA-ELQEELEELLEQLSL-ATEEELQDLAEELeeLQQRLA-----ELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 562 AQRPSAKWAVCELVPDRPVSNDTDQRTWKPLSTLLScrspavqavlgnwLYGVFVTDSLTAALADRSLLTSGEMLVTAeg 641
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLI-------------AAALLALLGLGGSLLSLILTIAGVLFLVL-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 642 hSITSCGVSYFAPDSAVHGILQRQREIAQIREECEQigqsvLSQQQTLAAVEQDDQQIAADIVQLRKVIEEIRTQQHDRQ 721
Cdd:COG4717 284 -GLLALLFLLLAREKASLGKEAEELQALPALEELEE-----EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42627761 722 IQIVRLtqQIERVAQQQAQLeieLADLAVQIEEESSQKQQAETELVVCEAERVELEAQVNQAESACQSSGRAL--ASQRS 799
Cdd:COG4717 358 ELEEEL--QLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 42627761 800 RVQRLSDRLHETAFGEQDCQNRVIDCERRIGMItRNSVILTENMQRLQHARADLDE 855
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQL-EEDGELAELLQELEELKAELRE 487
|
|
| |
