|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1151 |
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: 799.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 2 RLTHIKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQDVIFNGAATRRPAPRASVE 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 82 LVFDNSDHSLQGAwgQYAEVSIKRQLTRQGESTYFINNQTVRRRDITDLFLGTGVGARGYAVIEQGMISRIIEARPEELR 161
Cdd:TIGR02168 81 LVFDNSDGLLPGA--DYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 162 AYIEEAAGVSKYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQLNQQQDLLDYAQWQ--- 238
Cdd:TIGR02168 159 AIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEelr 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 239 ----QSLASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKrgvlreqIARLEEQIRHQQNLH 314
Cdd:TIGR02168 239 eeleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-------ISRLEQQKQILRERL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 315 QRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRI 394
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 395 RRELALKQQQLAHAEQTVAKHEERKGRLKQENQALNL-PDEAETAAAQEAAALLQSQQEHYEEQIIAAEEALHTAREAFQ 473
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 474 TTSNRFQSLKQQHITLQAQQQALSQILSQQQEAADF------WQATDHAATPQLWQHITAPAEWQHALSVILAERLHARA 547
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkallkNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 548 VP----------------HGFVPPAPLPQGQAAWL-SDDLSGGIKKSLPVQALLNQIQAQPPFQTALHHWLDGVLCAPDL 610
Cdd:TIGR02168 552 VEnlnaakkaiaflkqneLGRVTFLPLDSIKGTEIqGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 611 SYALAHQSDLGAHQIWLTPEGHQVDKVSVLLYAKSEQESLI-AQKARLDGIASELENLAPELSAAEAAFKQAEATVRSSE 689
Cdd:TIGR02168 632 DNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSIlERRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 690 VQHKNLMQQQQQHTRQYSQAQQRAAELLARTNQGQIRREHIERELAQLAEEQTVLQhtsdglsDDIATLQEAAAELEHQQ 769
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE-------ERLEEAEEELAEAEAEI 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 770 QTTAHSRQEQQGRLKQAQLALLEANRQYGLAEVAVHKLNQQKQNYQQQIA-------RLEQQTLDWQERQQELALAYE-T 841
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAaterrleDLEEQIEELSEDIESLAAEIEeL 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 842 EFQNDEQHIKLDELTEAVHTLDEEYIAVQEKLAQIQEQGREQYARVQALQTKLPQLQAATQTALLQQQEALINAKRYHQN 921
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 922 LTER----AADLDALEALAKESPKVLNSSIGSLTQQIEALGAVNLAALQELEEARERDGYYRSQSEDVQAAITLLEEAIA 997
Cdd:TIGR02168 945 LSEEysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 998 QIDDKTKERFKETFDAVNGKVQTFFPTLFGGGEATLKMI-GDDLLTAGVSIMARPPGKKNSTIHLLSGGEKALTAMSLVF 1076
Cdd:TIGR02168 1025 EIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTdPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLF 1104
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092727057 1077 ALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLYISHNRLTMEMAEQLVGVTMQEKGVSRVVAVDI 1151
Cdd:TIGR02168 1105 AIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1159 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 748.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQDVIFNGAATRRPAPRASV 80
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 81 ELVFDNSDHSLQGawgQYAEVSIKRQLTRQGESTYFINNQTVRRRDITDLFLGTGVGARGYAVIEQGMISRIIEARPEEL 160
Cdd:COG1196 81 SLTFDNSDGTLPI---DYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 161 RAYIEEAAGVSKYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQLNQQQDLLDYAQWQQS 240
Cdd:COG1196 158 RAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLREL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 241 LASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERD 320
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 321 KQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELAL 400
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 401 KQQQLAHAEQTVAKHEERKGRLKQENQALnlpdeaetaaaqeaaallqsqqehyEEQIIAAEEALHTAREAFQTTSNRFQ 480
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEEL-------------------------EEALAELEEEEEEEEEALEEAAEEEA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 481 SLKQQHITLQAQQQALSQILSQQQEAADFWQATDHAATPQLWQhitapaewqhalsvilaerlharavphgfvppaplpQ 560
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL------------------------------------L 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 561 GQAAWLSDDLSGGIKKslpvqallnqiqaqppfqtalhhwldgvlcapdlsyalahqsdlgahqiwltpeghqvdkvsvl 640
Cdd:COG1196 497 LEAEADYEGFLEGVKA---------------------------------------------------------------- 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 641 lyakseqeslIAQKARLDGIASELEnlapELSAAEAAFKQAEATVRSSEVQHKNlmqqqqqhtRQYSQAQQRAAELLART 720
Cdd:COG1196 513 ----------ALLLAGLRGLAGAVA----VLIGVEAAYEAALEAALAAALQNIV---------VEDDEVAAAAIEYLKAA 569
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 721 NQGQIRREHIERELAQLAEEQTVLQHTSDGLSDDIATLQEAAAELEHQQQTTAHSRQEQQGRLKQAQLALLEANRQYGLA 800
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 801 EVAVHKLNQQKQNYQQQIARLEQQTLDWQERQQELAlayetefqnDEQHIKLDELTEAVHTLDEEyiavQEKLAQIQEQG 880
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA---------ERLAEEELELEEALLAEEEE----ERELAEAEEER 716
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 881 REQYARVQALQTKLPQLQAATQTALLQQQEALinakryhqnlteraADLDALEALAKESPKVLNSSIGSLTQQIEALGAV 960
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELL--------------EEEALEELPEPPDLEELERELERLEREIEALGPV 782
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 961 NLAALQELEEARERDGYYRSQSEDVQAAITLLEEAIAQIDDKTKERFKETFDAVNGKVQTFFPTLFGGGEATLKMI-GDD 1039
Cdd:COG1196 783 NLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLTdPDD 862
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1040 LLTAGVSIMARPPGKKNSTIHLLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLY 1119
Cdd:COG1196 863 PLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIV 942
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|
gi 1092727057 1120 ISHNRLTMEMAEQLVGVTMQEKGVSRVVAVDIKQALEMAE 1159
Cdd:COG1196 943 ITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEELAE 982
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1144 |
2.28e-105 |
|
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: 358.51 E-value: 2.28e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 3 LTHIKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQDVIFNGaaTRRPAPRASVEL 82
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSK--SGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 83 VFDNSDHSLQGawgQYAEVSIKRQLTRQGESTYFINNQTVRRRDITDLFLGTGVGARGYAVIEQGMISRIIEARPEELRA 162
Cdd:pfam02463 80 TFDNEDHELPI---DKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 163 YIEEAAGVSKYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQL-----NQQQDLLDYAQW 237
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLeleeeYLLYLDYLKLNE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 238 QQSLASADKATAQHQSLQAQQDETVAQvQVLNDEVHALQTAEQSQQQTVHElsnKRGVLREQIARLEEQIRHQQNLHQRI 317
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKE-EEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKLERRKVDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 318 ERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQatlNAAFQTQQDEANRIRRE 397
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE---EELLAKKKLESERLSSA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 398 LALKQQQLAHAEQTVAKHEERKGRLKQENQALNLPDEAETAAAQEAAALLQSQQEHYEE--------------------- 456
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEekeelekqelkllkdelelkk 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 457 --------QIIAAEEALHTAREAFQTTSNRFQSLKQQHITLQAQQQALSQILSQQQEAADFWQATDHAATPQLWQHITAP 528
Cdd:pfam02463 470 sedllketQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 529 AEWQHALSVILAERLHARAvphgFVPPAPLPQGQAAWLSDDlsggikkslpVQALLNQIQAQPPFQTALHHWLDGVLCAP 608
Cdd:pfam02463 550 IVEVSATADEVEERQKLVR----ALTELPLGARKLRLLIPK----------LKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 609 DLSYALAHQSDLGAHQIWLTPEGHQVDKVSVLLYAKSEQESLIAQKARLDGIASEL--ENLAPELSAAEAAFKQAEATVR 686
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELtkELLEIQELQEKAESELAKEEIL 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 687 SSEVQHKNLMQQQQQHTRQYSQAQQRAAELLARTNQGQIRREHIERELAQLAEEQTVLQHTSDGLSDDI----ATLQEAA 762
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEekseLSLKEKE 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 763 AELEHQQQTTAHSRQEQQGRLKQAQLALLEANRQYGLAEVAVHKLNQQKQNYQQ----QIARLEQQTLDWQERQQELALA 838
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikeeELEELALELKEEQKLEKLAEEE 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 839 YETEFQNDEQHIKLDELTEAVHTLDEEYIaVQEKLAQIQEQGREQYARVQALQTKLPQLQAATQTALLQQQEALINAKRY 918
Cdd:pfam02463 856 LERLEEEITKEELLQELLLKEEELEEQKL-KDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 919 HQNLTERAADlDALEALAKESPKVLNSSIGSLTQQIEALGAVNLAALQELEEARERDGYYRSQSEDVQAAItllEEAIAQ 998
Cdd:pfam02463 935 EEPEELLLEE-ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK---KKLIRA 1010
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 999 IDDKTKERFKETFDAVNGKVQTFFPT---LFGGGEATLKMIG-DDLLTAGVSIMARPPGKKNSTIHLLSGGEKALTAMSL 1074
Cdd:pfam02463 1011 IIEETCQRLKEFLELFVSINKGWNKVffyLELGGSAELRLEDpDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALAL 1090
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1075 VFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLYISHNRLTMEMAEQLVGVTMQEKGVS 1144
Cdd:pfam02463 1091 IFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVS 1160
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-1150 |
3.07e-103 |
|
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: 352.83 E-value: 3.07e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 6 IKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQDVIFNGAATRrPAPRASVELVFD 85
Cdd:TIGR02169 5 IELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQ-SGNEAYVTVTFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 86 NSDHSLQGAWgqyaEVSIKRQLTRQG-ESTYFINNQTVRRRDITDLFLGTGVGARGYAVIEQGMISRIIEARPEELRAYI 164
Cdd:TIGR02169 84 NDDGKFPDEL----EVVRRLKVTDDGkYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERRKII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 165 EEAAGVSKYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQLNQQQDLLDYAQWQQSLASA 244
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 245 DKATAQHQSLQAQQDETVAQVQVLNDEVHAL-QTAEQSQQQTVHELSNKRGVLREQIARLEEQIRhqqnlhqRIERDKQA 323
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIeQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIA-------SLERSIAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 324 AQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQQ 403
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 404 QLahaEQTVAKHEERKGRLKQENQALNLPDEAETAAAQEAAALLQSQQEhYEEQIIAAEEALHTAREAFQTTSNRFQSLK 483
Cdd:TIGR02169 393 KL---EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 484 QQHITLQAQQQALSQILSQQQEAADFWQATDHAATP---------------------QLWQHITAPAEWQHALSVILAER 542
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEErvrggraveevlkasiqgvhgTVAQLGSVGERYATAIEVAAGNR 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 543 LHARAVPHGFV--------------PPAPLPQGQAAWLSDDLSGGIKKSLpVQALLNQIQAQPPFQTALHHWLDGVLCAP 608
Cdd:TIGR02169 549 LNNVVVEDDAVakeaiellkrrkagRATFLPLNKMRDERRDLSILSEDGV-IGFAVDLVEFDPKYEPAFKYVFGDTLVVE 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 609 DLSYALAHqsdLGAHQIwLTPEGHQVDK-----------VSVLLYAKSEQESLIAQKARLDGIASELENLAPELSAAEAA 677
Cdd:TIGR02169 628 DIEAARRL---MGKYRM-VTLEGELFEKsgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 678 FKQAEATVRSSEVQHKNLMQQQQQHTRQYSQAQQRAAELLARTNQGQIRREHIERELAQLAEEQTVLQhtsdglsDDIAT 757
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-------EDLHK 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 758 LQEAAAELEhqqQTTAHSRQEQQGRLKQAQLALLEANR-QYGLAEVAVHKLNQQKQNYQQQIARLEQQTLDWQERQQELA 836
Cdd:TIGR02169 777 LEEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 837 LAYET-EFQNDEQHIKLDELTEAVHTLDEEYIAVQEKLAQIQEQGREQYARVQalqtklpqlQAATQTALLQQQEALINA 915
Cdd:TIGR02169 854 KEIENlNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE---------ELEAQIEKKRKRLSELKA 924
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 916 KRyhQNLTERAADLDALEALAKESP------KVLNSSIGSLTQQIEALGAVNLAALQELEEARERDGYYRSQSEDVQAAI 989
Cdd:TIGR02169 925 KL--EALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 990 TLLEEAIAQIDDKTKERFKETFDAVNGKVQTFFPTLfGGGEATLKMIG-DDLLTAGVSIMARPPGKKNSTIHLLSGGEKA 1068
Cdd:TIGR02169 1003 KAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENpDDPFAGGLELSAKPKGKPVQRLEAMSGGEKS 1081
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1069 LTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLYISHNRLTMEMAEQLVGVTMQEKGVSRVVA 1148
Cdd:TIGR02169 1082 LTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNGESQVFG 1161
|
..
gi 1092727057 1149 VD 1150
Cdd:TIGR02169 1162 LK 1163
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1052-1145 |
4.68e-58 |
|
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: 198.46 E-value: 4.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1052 PGKKNSTIHLLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLYISHNRLTMEMAE 1131
Cdd:cd03278 104 PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
90
....*....|....
gi 1092727057 1132 QLVGVTMQEKGVSR 1145
Cdd:cd03278 184 RLYGVTMQESGVSK 197
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-156 |
1.23e-50 |
|
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: 177.27 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 3 LTHIKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQDVIFNGAATRRPAPRASVEL 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092727057 83 VFDNSDHSlqgawgqyaevsikrqltrqgestyfinnqtvrrrditdlflgtgvgargYAVIEQGMISRIIEAR 156
Cdd:cd03278 81 TFDNSDGR--------------------------------------------------YSIISQGDVSEIIEAP 104
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1061-1145 |
2.36e-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: 98.15 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1061 LLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQT-QFLYISHNRLTMEMAEQLVGVTMQ 1139
Cdd:cd03239 94 ILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTsQFIVITLKKEMFENADKLIGVLFV 173
|
....*.
gi 1092727057 1140 EkGVSR 1145
Cdd:cd03239 174 H-GVST 178
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1048-1150 |
6.42e-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: 6.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1048 MARPPGKKNSTIHLLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQT-QFLYISHNRLT 1126
Cdd:cd03275 142 SKNPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNfQFIVISLKEEF 221
|
90 100
....*....|....*....|....*
gi 1092727057 1127 MEMAEQLVGVTM-QEKGVSRVVAVD 1150
Cdd:cd03275 222 FSKADALVGVYRdQECNSSKVLTLD 246
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-153 |
1.60e-20 |
|
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: 92.36 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDPTTI-HVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQDVIF-NGAATRRpapRA 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYkRGQAGIT---KA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092727057 79 SVELVFDNSD--HSLQGaWGQYAEVSIKRQLTRQGESTYFINNQTVRRRDITDLFLGTGVGARG-YAVIEQGMISRII 153
Cdd:cd03273 78 SVTIVFDNSDksQSPIG-FENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNpHFLIMQGRITKVL 154
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-87 |
7.99e-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: 82.36 E-value: 7.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 3 LTHIKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQDvifNGAATRRPAPRASVEL 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFL---AGGGVKAGINSASVEI 77
|
....*
gi 1092727057 83 VFDNS 87
Cdd:cd03239 78 TFDKS 82
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
6-152 |
2.08e-17 |
|
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: 83.01 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 6 IKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAkQLRGESMQDVIfNGAATRRPAPR-ASVELVF 84
Cdd:cd03275 4 LELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSS-HLRSKNLKDLI-YRARVGKPDSNsAYVTAVY 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 85 DNSDhslqgawgqyAEVSIKRQLTRQGESTYFINNQTVRRRDITDLF--LGTGVGARGYAVIeQGMISRI 152
Cdd:cd03275 82 EDDD----------GEEKTFRRIITGGSSSYRINGKVVSLKEYNEELekINILVKARNFLVF-QGDVESI 140
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1057-1144 |
2.15e-17 |
|
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: 80.48 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1057 STIHLLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQT-QFLYISHNRLTMEMAEQLVG 1135
Cdd:cd03227 73 FTRLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKLIH 152
|
....*....
gi 1092727057 1136 VTMQEKGVS 1144
Cdd:cd03227 153 IKKVITGVY 161
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1045-1136 |
3.25e-17 |
|
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: 81.57 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1045 VSIMARPPGKKNSTIHLLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLYISHNR 1124
Cdd:cd03274 111 VEQIAQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRN 190
|
90
....*....|..
gi 1092727057 1125 LTMEMAEQLVGV 1136
Cdd:cd03274 191 NMFELADRLVGI 202
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
6-150 |
3.33e-16 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 79.61 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 6 IKLSGFKSFTDPTTI--HVPGQLVaVIGPNGCGKSNVIDAVRWVLGEASAkQLRGESMQDVIFNGAATRrpAPRASVELV 83
Cdd:cd03272 4 VIIQGFKSYKDQTVIepFSPKHNV-VVGRNGSGKSNFFAAIRFVLSDEYT-HLREEQRQALLHEGSGPS--VMSAYVEII 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092727057 84 FDNSDHSLQGAWGqyaEVSIKRQLTRQGEStYFINNQTVRRRDITDLFLGTGVG-ARGYAVIEQGMIS 150
Cdd:cd03272 80 FDNSDNRFPIDKE---EVRLRRTIGLKKDE-YFLDKKNVTKNDVMNLLESAGFSrSNPYYIVPQGKIN 143
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-177 |
2.78e-15 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 75.82 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 2 RLTHIKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGeasakqlrGESMQDVIFNGAATRRPAPRASVE 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALY--------GKARSRSKLRSDLINVGSEEASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 82 LVFDNSDHSLQgawgqyaevsIKRqltRQGESTYFINNQTVRRRDITDLFLGTGVGARgyavieqgmISRIIEARPEELR 161
Cdd:COG0419 73 LEFEHGGKRYR----------IER---RQGEFAEFLEAKPSERKEALKRLLGLEIYEE---------LKERLKELEEALE 130
|
170
....*....|....*.
gi 1092727057 162 AYIEEAAGVSKYKERR 177
Cdd:COG0419 131 SALEELAELQKLKQEI 146
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-404 |
4.71e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 177 RKETEGRLKDTREHLQRLGDLQNELA---RQVEKLEKQAETAERYKYLTAQLNQQQDLLDYAQWQQSLASADKATAQHQS 253
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEdarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 254 LQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRgvlreqIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQ 333
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR------LEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092727057 334 EQQQIRVQLEENelqaeekqteLAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELA-LKQQQ 404
Cdd:COG4913 374 PLPASAEEFAAL----------RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAsLERRK 435
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1058-1146 |
2.81e-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: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1058 TIHLLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLYISHNRLTMEMAEQLVGVT 1137
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
....*....
gi 1092727057 1138 MQEKgVSRV 1146
Cdd:cd03272 235 FRNK-VSTI 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-429 |
7.15e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDPTTIHVPGqlVAVI-GPNGCGKSNVIDAVRWVLGEASAKQlrgESMQDVIFNGAATrrpaprAS 79
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRLEDG--VTVIhGVNGSGKSSLLEACFFALYGSKALD---DTLDDVITIGAEE------AE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 80 VELVFDNSDhslqgawgqyAEVSIKRQLTRQGES-----------TYFINNQTVRRRDITDLFLGTGVGARGYAVIEQGM 148
Cdd:PRK02224 70 IELWFEHAG----------GEYHIERRVRLSGDRattakcvletpEGTIDGARDVREEVTELLRMDAEAFVNCAYVRQGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 149 ISRIIEARPEELRAYIEEAAGVSKYKERRKetegRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTA---QL 225
Cdd:PRK02224 140 VNKLINATPSDRQDMIDDLLQLGKLEEYRE----RASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGlesEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 226 NQQQDLLDYAQWQQSLASADKATAqhQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEE 305
Cdd:PRK02224 216 AELDEEIERYEEQREQARETRDEA--DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 306 QIRHQQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQ 385
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1092727057 386 TQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQAL 429
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-85 |
4.34e-12 |
|
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: 69.26 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDpTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGEsmqDviFNGAATRRPaPRASV 80
Cdd:COG3593 1 MKLEKIKIKNFRSIKD-LSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE---D--FYLGDDPDL-PEIEI 73
|
....*
gi 1092727057 81 ELVFD 85
Cdd:COG3593 74 ELTFG 78
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-883 |
5.91e-12 |
|
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: 70.38 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDPTTIH--VPGQLVAVIGPNGCGKSNVIDAVRWVLgeasAKQLRGESMQDVIFNGAATRRPAPrA 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDftALGPIFLICGKTGAGKTTLLDAITYAL----YGKLPRRSEVIRSLNSLYAAPSEA-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 79 SVELVFDNSDHSLQGAWGQYAEVSIK--------RQLTRQGESTYFINNQTVRRRDITDLFLGTGVGARGYAVIEQGMIS 150
Cdd:TIGR00618 76 FAELEFSLGTKIYRVHRTLRCTRSHRkteqpeqlYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 151 RIIEARPEELRAYIEEAAGVSKY-------KERRKETEGRLKDTREHLQRLGDLQNELARQV-------EKLEKQAETAE 216
Cdd:TIGR00618 156 QFLKAKSKEKKELLMNLFPLDQYtqlalmeFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYherkqvlEKELKHLREAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 217 RYKYLT-AQLNQQQDLLDYAQWQQSLASadKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGV 295
Cdd:TIGR00618 236 QQTQQShAYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 296 LREQIA-RLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEE--KQTELAEWAMQVAEHEERLPE 372
Cdd:TIGR00618 314 TELQSKmRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIscQQHTLTQHIHTLQQQKTTLTQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 373 LEEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQ--ENQALNLPDEAETAAAQEAAALLQSQ 450
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaiTCTAQCEKLEKIHLQESAQSLKEREQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 451 QEHYEEQIIAAEEALHTAREAFqttsnrfqslKQQHITLQAQQQALSQILSQQQEAADFWQATDHAATPQLWQHITAPAE 530
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLAR----------LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 531 WQHALSVILAERLHARAVphgfvppaplpQGQAAWLSDDLSGGIKKSLPVQALLNQIQAQppfQTALHHWLDGVLCAPDl 610
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASL-----------KEQMQEIQQSFSILTQCDNRSKEDIPNLQNI---TVRLQDLTEKLSEAED- 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 611 syalahqSDLGAHQIWLTPEGHQVDKVSVLLYAKSEQESLIAQKARLDGiasELENLAPElsaaeaafKQAEATVRSSEV 690
Cdd:TIGR00618 609 -------MLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA---LQLTLTQE--------RVREHALSIRVL 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 691 QHKNLMQQQQQHTRQYSQAQQRAA--ELLARTNQGQIRREHIERELAQLAEEQTVLQHTSDG-LSDDIATLQEAAAELEH 767
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKEQLTYwkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSdLAAREDALNQSLKELMH 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 768 QQQTTAHSRQEQQGRLKQAQLALLEANRQYGLAEVAVHKLNQQKQNYQQQIARLEQQTLDW-QERQQELALAYETEFQND 846
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEiPSDEDILNLQCETLVQEE 830
|
890 900 910
....*....|....*....|....*....|....*...
gi 1092727057 847 EQ-HIKLDELTEAVHTLDEEYIAVQEKLAQIQEQGREQ 883
Cdd:TIGR00618 831 EQfLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-88 |
5.67e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 65.72 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 2 RLTHIKLSGFKSFTDpttIHVP-GQLVAVIGPNGCGKSNVIDAVRWV-------LGEASAKqlRGeSMQDVIFNGAatRR 73
Cdd:COG4637 1 MITRIRIKNFKSLRD---LELPlGPLTVLIGANGSGKSNLLDALRFLsdaarggLQDALAR--RG-GLEELLWRGP--RT 72
|
90
....*....|....*
gi 1092727057 74 PAPRASVELVFDNSD 88
Cdd:COG4637 73 ITEPIRLELEFAEED 87
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1058-1146 |
1.41e-10 |
|
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: 63.09 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1058 TIHLLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLYISHNRLTMEMAEQLVGVT 1137
Cdd:cd03273 163 SLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVLFRTR 242
|
....*....
gi 1092727057 1138 MQEkGVSRV 1146
Cdd:cd03273 243 FVD-GTSTV 250
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-216 |
1.51e-10 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 61.74 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 6 IKLSGFKSFTDpTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLG----EASAKQLRGESMQDVIFNGAATRrpapRASVE 81
Cdd:pfam13476 1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYgktsRLKRKSGGGFVKGDIRIGLEGKG----KAYVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 82 LVFDNSDhslqGAWGQYAEVSIKRQLTrQGESTYFINNQTVRRRDItdlflgtgvgargyavieQGMISRIIEARPEELR 161
Cdd:pfam13476 76 ITFENND----GRYTYAIERSRELSKK-KGKTKKKEILEILEIDEL------------------QQFISELLKSDKIILP 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1092727057 162 AYIEEAAGVSKYKErRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAE 216
Cdd:pfam13476 133 LLVFLGQEREEEFE-RKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEE 186
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-866 |
5.76e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 298 EQIARLEEQIRHQQNLHQRIERDKQAAQA--QMQRIHQEQQQIRVQLEENE-----LQAEEKQTELAEWAMQVAEHEERL 370
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 371 PELEEAQATLNAAFQTQQDEANRIRR--------ELALKQQQLAHAEQTVAKHEERKGRLKQENQALNLPDEAETAAAQE 442
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 443 AAALLQSQQEHYEEQIIAAEEALHTAREAFQTTSNRFQSLKQQHitlQAQQQALSQILSQQQEA-ADFWQATDHAATP-- 519
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI---ASLERRKSNIPARLLALrDALAEALGLDEAElp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 520 ---QLWQHITAPAEWQHAlsvilAERlharaVPHGF-----VPPAPLPQGQAAWLSDDLSGGI-------------KKSL 578
Cdd:COG4913 462 fvgELIEVRPEEERWRGA-----IER-----VLGGFaltllVPPEHYAAALRWVNRLHLRGRLvyervrtglpdpeRPRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 579 PVQALLNQIQAQPpfqTALHHWLDGVLCAPDLSYALAHQSDLGAHQIWLTPEG--------HQVDKVSvllyaKSEQESL 650
Cdd:COG4913 532 DPDSLAGKLDFKP---HPFRAWLEAELGRRFDYVCVDSPEELRRHPRAITRAGqvkgngtrHEKDDRR-----RIRSRYV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 651 IAQKARldgiaSELENLAPELSAAEAAFKQAEATVRSSEVQHKNLmqqqqqhtrqysQAQQRAAELLARTNQGQIRREHI 730
Cdd:COG4913 604 LGFDNR-----AKLAALEAELAELEEELAEAEERLEALEAELDAL------------QERREALQRLAEYSWDEIDVASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 731 ERELAQLAEEqtvLQHTSDGlSDDIATLQEAAAELEHQQQTTAHSRQEQQGRLKQAQLALLEANRQYGLAEVAVHKLNQQ 810
Cdd:COG4913 667 EREIAELEAE---LERLDAS-SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092727057 811 KQNYQQQ--IARLEQQTLDWQERQQELALAYETEFQNDEQHIKLDELTEAVHTLDEEY 866
Cdd:COG4913 743 ARLELRAllEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREW 800
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-117 |
7.23e-10 |
|
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: 58.91 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 5 HIKLSGFKSFTDPTTIH-VPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQdvifngaatrRPAPRASVELV 83
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTfGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVK----------AGCIVAAVSAE 70
|
90 100 110
....*....|....*....|....*....|....*
gi 1092727057 84 FDNSDHSLQGAWGQYAEVSIKRQL-TRQGESTYFI 117
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILALaSLKPRPLYIL 105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
153-425 |
9.06e-10 |
|
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: 63.27 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 153 IEARPEELRAYIEEAAGVSKYKERRKETEGRLK-----DTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQLNQ 227
Cdd:pfam01576 301 LEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 228 --QQDLLDYAQWQQSLASAD--------KATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLR 297
Cdd:pfam01576 381 alESENAELQAELRTLQQAKqdsehkrkKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 298 EQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERlpeLEEAQ 377
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK---LEEDA 537
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1092727057 378 ATLNAAFQTQQdeanRIRRELALKQQQLAHAEQTVAKHEERKGRLKQE 425
Cdd:pfam01576 538 GTLEALEEGKK----RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE 581
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-483 |
5.60e-09 |
|
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: 59.39 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 241 LASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERD 320
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 321 KQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELAL 400
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 401 KQQQLAHAEQTVAKHEERKGRLKQENQALNLPDEAETAAAQEAAALLQSQQEHYEEQIIAAEEALhtAREAFQTTSNRFQ 480
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA--AAAAERTPAAGFA 249
|
...
gi 1092727057 481 SLK 483
Cdd:COG4942 250 ALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
297-481 |
6.24e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 297 REQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQEQQQIR--VQLEENELQAEEKQTELAEWAMQVAEHEE---RLP 371
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 372 ELEEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALNLPDEAETAAAQEAAALLQSQQ 451
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190
....*....|....*....|....*....|
gi 1092727057 452 EHYEEQIIAAEEALHTAREAFQTTSNRFQS 481
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
645-993 |
6.38e-09 |
|
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: 60.35 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 645 SEQESLIAQKARLDGIASELEnlapELSAAEAAFKQAeatvRSSEVQHKNLMQQQQQHTRQYSQAQQRAAELLARTNQGQ 724
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELE----ELSARESDLEQD----YQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 725 IRREHIERELAQLAEEQTVLQHTSDGLSDDIATLQEAAAElehqQQTTAhsrqeqqGRLKQAQLALLEANRQYGLAEVAV 804
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDV----QQTRA-------IQYQQAVQALEKARALCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 805 HKLNQQKQNYQqqiARLEQQTLDWQERQQELALAYETEFQNDEQHIKLDELTEAVHTlDEEYIAVQEKLAQIQEQgREQY 884
Cdd:COG3096 437 ENAEDYLAAFR---AKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER-SQAWQTARELLRRYRSQ-QALA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 885 ARVQALQTKLPQLqaatQTALLQQQEALINAKRYHQNLTERAADLDALEALAKEspkvlnssigsLTQQIEALgavnlaa 964
Cdd:COG3096 512 QRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE-----------LEAQLEEL------- 569
|
330 340
....*....|....*....|....*....
gi 1092727057 965 LQELEEARERDGYYRSQSEDVQAAITLLE 993
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
154-371 |
6.50e-09 |
|
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: 59.39 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 154 EARPEELRAYIEEA-AGVSKYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQ-AETAERYKYLTAQLNQQQDL 231
Cdd:COG4942 26 EAELEQLQQEIAELeKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 232 LD---YAQWQQSLASADKATAQHQSLQaqqdETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIR 308
Cdd:COG4942 106 LAellRALYRLGRQPPLALLLSPEDFL----DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092727057 309 HQQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLP 371
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-84 |
9.42e-09 |
|
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: 56.92 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 3 LTHIKLSGFKSFTDpttIHVPG----QLVAVIGPNGCGKSNVIDAVRWVLGeASAKQLRGESMQDVIFNGaATRRPAPRA 78
Cdd:cd03274 3 ITKLVLENFKSYAG---EQVIGpfhkSFSAIVGPNGSGKSNVIDSMLFVFG-FRASKMRQKKLSDLIHNS-AGHPNLDSC 77
|
....*.
gi 1092727057 79 SVELVF 84
Cdd:cd03274 78 SVEVHF 83
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-429 |
1.17e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 186 DTREHLQRLGDLQNELARQVEKLEKQAETAE-RYKYLTAQLNQQQDLLDYAQWQQSLASADKATAQHQSLQAQQDETVAQ 264
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEaELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 265 VQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIER----------DKQAAQAQMQRIHQE 334
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrallEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 335 -QQQIRVQLEENELQAEEKQTEL--------AEWAMQVAEHEERLPELEEAQATLN-----------AAFQTQQDEANri 394
Cdd:COG4913 767 lRENLEERIDALRARLNRAEEELeramrafnREWPAETADLDADLESLPEYLALLDrleedglpeyeERFKELLNENS-- 844
|
250 260 270
....*....|....*....|....*....|....*
gi 1092727057 395 RRELALKQQQLAHAEQTVakheerKGRLKQENQAL 429
Cdd:COG4913 845 IEFVADLLSKLRRAIREI------KERIDPLNDSL 873
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
174-406 |
2.91e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.31 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 174 KERRKETEGR--LKDTREHLQRLGDLQNELARQVEKL--EKQAETAERYKYLTAQLNQQQDLLDYAQWQQSLASADKATA 249
Cdd:pfam12128 636 KASREETFARtaLKNARLDLRRLFDEKQSEKDKKNKAlaERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 250 QHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQ----QQTVHELSNKRGVLREQIARLEEQIRhqqNLHQRIERDKQAAQ 325
Cdd:pfam12128 716 KQAYWQVVEGALDAQLALLKAAIAARRSGAKAElkalETWYKRDLASLGVDPDVIAKLKREIR---TLERKIERIAVRRQ 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 326 A-------QMQRIHQEQQQIRVQLEENELQAEEKQTELAEwamQVAEHEERLPELEEAQATLNAafqtQQDEANRIRREL 398
Cdd:pfam12128 793 EvlryfdwYQETWLQRRPRLATQLSNIERAISELQQQLAR---LIADTKLRRAKLEMERKASEK----QQVRLSENLRGL 865
|
....*...
gi 1092727057 399 ALKQQQLA 406
Cdd:pfam12128 866 RCEMSKLA 873
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-395 |
4.79e-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: 56.70 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 174 KERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQ-AETAERYKYLTAQLNQQQDLLDYAQWQQSLASADKATAQHQ 252
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 253 ------SLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQA 326
Cdd:COG4942 106 laellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092727057 327 QMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIR 395
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-88 |
1.70e-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: 52.99 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 3 LTHIKLSGFKSFTDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVL-GEASAKQLRGESMQDVIFNGAAtrrpapRASVE 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGEV------RAQVK 74
|
....*..
gi 1092727057 82 LVFDNSD 88
Cdd:cd03240 75 LAFENAN 81
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-430 |
7.17e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDpTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLRGESMQDVifngaaTRRPAPRASV 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKS-SVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDF------TRIGGSGTEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 81 ELVFDNSD-------------HSLQGAWGQYAEVSIKRQLT------------------RQGESTYFINNQTVRRRDITD 129
Cdd:PRK03918 74 ELKFEKNGrkyrivrsfnrgeSYLKYLDGSEVLEEGDSSVRewverlipyhvflnaiyiRQGEIDAILESDESREKVVRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 130 LflgTGVGARGYAVIEQGMISRIIEARPEELRAYIEEAAGVskyKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLE 209
Cdd:PRK03918 154 I---LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENI---EELIKEKEKELEEVLREINEISSELPELREELEKLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 210 KQAETAERYKYLTAQLNQQQDLLdyaqwqqsLASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVhEL 289
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESL--------EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-KL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 290 SNKRGVLREQIARLEEQIrhqqnlhQRIERDKQAAQAQMQrihqeqqqirvQLEENELQAEEKQTELAEWAMQVAEHEER 369
Cdd:PRK03918 299 SEFYEEYLDELREIEKRL-------SRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEELEER 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092727057 370 LPELEEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKH----EERKGRLKQENQALN 430
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEiskiTARIGELKKEIKELK 425
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
645-1136 |
7.73e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 645 SEQESLIAQKARLDGIASELENLAPELSAAEAAFKQAEATVRSSEVQHKN----LMQQQQQHTRQYSQAQQRAAEL---L 717
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAELeseL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 718 ART----NQGQIRREHIERELAQLAEEQTVLQHTSDGLSDDIATLQEAAAELEHQQQTTAHSRQEQQGRLKQAQlALLEA 793
Cdd:PRK02224 373 EEAreavEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE-ALLEA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 794 NR-----QyglaEVAVHKLNQQKQNYQQQIARLEQQTLDWQERQQELALAYETEFQNDEQHIKLDELTEAVHTLDEEYIA 868
Cdd:PRK02224 452 GKcpecgQ----PVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 869 VQEKLAQIQEQGREQYARVQALQTKLPQLQAATQTALLQQQEALINAKRYHQNLTERAADLDALEALAKESPKVLN--SS 946
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADaeDE 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 947 IGSLTQQIEALGAVNLAALQELEEARER-----DGYYRSQSEDVQAAITLLEEAIAQIDDKTK----------------- 1004
Cdd:PRK02224 608 IERLREKREALAELNDERRERLAEKRERkreleAEFDEARIEEAREDKERAEEYLEQVEEKLDelreerddlqaeigave 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1005 ------ERFKETFDAVNGKVQTfFPTLFGGGEATLKMIGD---DLLTAGVSIMARP-------------------PGKKN 1056
Cdd:PRK02224 688 neleelEELRERREALENRVEA-LEALYDEAEELESMYGDlraELRQRNVETLERMlnetfdlvyqndayshielDGEYE 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1057 STIH----------LLSGGEKALTAMSLVFALFSL--------NPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQ--TQ 1116
Cdd:PRK02224 767 LTVYqkdgeplepeQLSGGERALFNLSLRCAIYRLlaegiegdAPLPPLILDEPTVFLDSGHVSQLVDLVESMRRLgvEQ 846
|
570 580
....*....|....*....|
gi 1092727057 1117 FLYISHNRLTMEMAEQLVGV 1136
Cdd:PRK02224 847 IVVVSHDDELVGAADDLVRV 866
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-483 |
8.60e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDPTTIHVPGqLVAVIGPNGCGKSNVIDAVRWVL-GEASAKQL-----RGESMQDV---------- 64
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTG-INIITGKNGAGKSSIVDAIRFALfTDKRTEKIedmikKGKNNLEVelefrigghv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 65 --IFNGAATRRPAPRASVELVFDNS----------DHSLQGAWGQYAEVSIKRQLTRQGESTYFINNQTVRRRDITDLFL 132
Cdd:PRK01156 80 yqIRRSIERRGKGSRREAYIKKDGSiiaegfddttKYIEKNILGISKDVFLNSIFVGQGEMDSLISGDPAQRKKILDEIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 133 GTGVGARGYAVIE------QGMISRIIEARpEELRAYIEEAAGVSKY----------KERRKE--------TEGRLKDTR 188
Cdd:PRK01156 160 EINSLERNYDKLKdvidmlRAEISNIDYLE-EKLKSSNLELENIKKQiaddekshsiTLKEIErlsieynnAMDDYNNLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 189 EHLQRLGDL--------------QNELARQVEKLEKQAETAERYKYLTAQ------------LNQQQDLLDYAQWQQSLA 242
Cdd:PRK01156 239 SALNELSSLedmknryeseiktaESDLSMELEKNNYYKELEERHMKIINDpvyknrnyindyFKYKNDIENKKQILSNID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 243 S-------ADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRgvlreqiARLEEQIRHQQNLHQ 315
Cdd:PRK01156 319 AeinkyhaIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLK-------KKIEEYSKNIERMSA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 316 RIERDKQAAQAQMQRIHQEQQQIRVQLEENElqaeekqTELAEWAMQVAEHEERLPELEEAQATLNA-------AFQTQQ 388
Cdd:PRK01156 392 FISEILKIQEIDPDAIKKELNEINVKLQDIS-------SKVSSLNQRIRALRENLDELSRNMEMLNGqsvcpvcGTTLGE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 389 DEANRIRR----ELALKQQQLAHAEQTVAKHEERKGRLKQENQALNLPDEAETAAAQEAAALLQSQQEHYEEQIIAAEEA 464
Cdd:PRK01156 465 EKSNHIINhyneKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDK 544
|
570
....*....|....*....
gi 1092727057 465 lHTAREAFQttsNRFQSLK 483
Cdd:PRK01156 545 -HDKYEEIK---NRYKSLK 559
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-49 |
8.82e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 51.92 E-value: 8.82e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDPT-TIHVPGQLVAVIGPNGCGKSNVIDAVRWVLG 49
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEiDFDNPPRLTVLVGENGSGKTTLLEAIALALS 50
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
643-1132 |
9.49e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 643 AKSEQESLIAQKARLDGIASELENLAPELSAAEAAFKQAEAtvrssEVQHKNLMQQQQQHTRQYSQAQQRAAELLARTNQ 722
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 723 GQIRREHIERELAQLAEEQTVLQHTSDGLS-DDIATLQEAAAELEHQQQTTAHSRQE------------------QQGRL 783
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEEleeaqeeleeleeeleqlENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 784 KQAQLALLEANRQYGLAEVAVHKLNQQKQNYQQQIARL-------------------EQQTLDWQERQQELALAYETEFQ 844
Cdd:COG4717 238 AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlgllallflllaREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 845 NDEQHIKLDELTEAVHTLDEEYIAVQEKLAQIQEQ-----GREQYARVQALQTKLPQLQAATQTALLQQQEALINAKRYH 919
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELlreaeELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 920 QNLTERAADLDA---------LEALAKESPKVLNSSIGSLTQQIEALGAVNLAALQELEEARERDGYYRSqSEDVQAAIT 990
Cdd:COG4717 398 QELKEELEELEEqleellgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQ 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 991 LLEEAIAQID----------------DKTKERFKETF-DAVNGKVQTFFPTLFGGGEATLKMIGDDlltagvSIMARPPG 1053
Cdd:COG4717 477 ELEELKAELRelaeewaalklalellEEAREEYREERlPPVLERASEYFSRLTDGRYRLIRIDEDL------SLKVDTED 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1054 KKNSTIHLLSGGEKALTAMSLVFAL---FSLNPAPFcLLDEVDAPLDDANTSRFCNLVKEMSAQTQFLYISHNRLTMEMA 1130
Cdd:COG4717 551 GRTRPVEELSRGTREQLYLALRLALaelLAGEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVELF 629
|
..
gi 1092727057 1131 EQ 1132
Cdd:COG4717 630 QE 631
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
196-419 |
1.14e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 196 DLQNelarQVEKLEKQAETAERYKYLTAQLNQQQDLLD--------YAQWQQSLASADKATAQHQ----SLQAQQDETVA 263
Cdd:PRK11281 40 DVQA----QLDALNKQKLLEAEDKLVQQDLEQTLALLDkidrqkeeTEQLKQQLAQAPAKLRQAQaeleALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 264 QvqvlNDEVHALQTAEQSQQQTVHELSNkrgvLREQIARLEEQIRHQQNlhqRIERdkqaAQAQMQRIHQEQQQIRVQL- 342
Cdd:PRK11281 116 E----TLSTLSLRQLESRLAQTLDQLQN----AQNDLAEYNSQLVSLQT---QPER----AQAALYANSQRLQQIRNLLk 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 343 ----EENELQAEEKQTELAEWAMQVAEHEERLPELeEAQATLNAAFQTQQDEA----NRIRRELALKQ-----QQLAHAE 409
Cdd:PRK11281 181 ggkvGGKALRPSQRVLLQAEQALLNAQNDLQRKSL-EGNTQLQDLLQKQRDYLtariQRLEHQLQLLQeainsKRLTLSE 259
|
250
....*....|
gi 1092727057 410 QTVAKHEERK 419
Cdd:PRK11281 260 KTVQEAQSQD 269
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-131 |
1.44e-06 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 51.70 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDpTTIHVPGQLVAVIGPNGCGKSNVIDAVrWVLgeASAKQLRGESMQDVIfngaatRRPAPRASV 80
Cdd:PRK00064 1 MYLTRLSLTDFRNYEE-LDLELSPGVNVLVGENGQGKTNLLEAI-YLL--APGRSHRTARDKELI------RFGAEAAVI 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1092727057 81 ELVFDNSDHslqgawgqyaEVSIKRQLTRQGESTYFINNQTVRR-RDITDLF 131
Cdd:PRK00064 71 HGRVEKGGR----------ELPLGLEIDKKGGRKVRINGEPQRKlAELAGLL 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-424 |
1.93e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 156 RPEELRAYIEEAAGVS----KYKERRKETEgrLKDTREHLQRlgdlQNELARQVEKLEKQAETAERykylTAQLNQQQDL 231
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEeakkKAEEAKKADE--AKKKAEEAKK----ADEAKKKAEEAKKKADEAKK----AAEAKKKADE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 232 LDYAQWQQSLASADKATAQHQSLQAQQDETVAQVQVLN--DEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRH 309
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 310 QQNLHQRIERDK----QAAQAQMQRIHQEQ-----------QQIRVQLEENELQAEE----------KQTELAEWAMQVA 364
Cdd:PTZ00121 1595 EEVMKLYEEEKKmkaeEAKKAEEAKIKAEElkkaeeekkkvEQLKKKEAEEKKKAEElkkaeeenkiKAAEEAKKAEEDK 1674
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 365 EHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQ 424
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
34-401 |
3.56e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 51.23 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 34 GCGKSNVIDAVRWVLGEasakqlRGESmqDVIFNGAAtrrpapRASVELVFDNSDHSLQGAW-------GQYAEVSIKRQ 106
Cdd:COG0497 32 GAGKSILLDALGLLLGG------RADA--SLVRHGAD------KAEVEAVFDLSDDPPLAAWleengldLDDGELILRRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 107 LTRQGESTYFINNQTVRRRDITDLFlgtgvgargyavieqgmiSRIIE----------ARPEELRAYIEEAAGvskyker 176
Cdd:COG0497 98 ISADGRSRAFINGRPVTLSQLRELG------------------ELLVDihgqhehqslLDPDAQRELLDAFAG------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 177 rkeTEGRLKDTREHLQRLGDLQNELArqvEKLEKQAETAERYKYLTAQLNQ----------QQDLldyAQWQQSLASADK 246
Cdd:COG0497 153 ---LEELLEEYREAYRAWRALKKELE---ELRADEAERARELDLLRFQLEEleaaalqpgeEEEL---EEERRRLSNAEK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 247 -ATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQtvheLSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQ--- 322
Cdd:COG0497 224 lREALQEALEALSGGEGGALDLLGQALRALERLAEYDPS----LAELAERLESALIELEEAASELRRYLDSLEFDPErle 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092727057 323 AAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEwamqVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELALK 401
Cdd:COG0497 300 EVEERLALLRRLARKYGVTVEELLAYAEELRAELAE----LENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKK 374
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
257-429 |
3.82e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 257 QQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQR--IERDKQAAQAQMQRIHQE 334
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 335 QQQIR---VQLEENELQAEEKQTELAEWAMQV-AEHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQ 410
Cdd:COG4717 155 LEELReleEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170
....*....|....*....
gi 1092727057 411 TVAKHEERKgRLKQENQAL 429
Cdd:COG4717 235 ELEAAALEE-RLKEARLLL 252
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-48 |
4.76e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 50.04 E-value: 4.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1092727057 3 LTHIKLSGFKSFTDPTTI------HVPGQLVAVIGPNGCGKSNVIDAVRWVL 48
Cdd:COG1106 2 LISFSIENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFLR 53
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
645-1009 |
5.09e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 645 SEQESLIAQKARLDGIASELENLAPELSAAEAAFKQAEATVRSSEVQHKNLMQQQQQHTRQYSQAQQRAAELLARTNQG- 723
Cdd:PRK02224 227 EQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDd 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 724 -------------QIRREHIERELAQLAEEQTVLQHTSDGLSDDIATLQ-------EAAAELEHQQQTTAHSRQEQQGRL 783
Cdd:PRK02224 307 adaeavearreelEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEeraeelrEEAAELESELEEAREAVEDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 784 KQAQLALLEANRQYGLAEVAVHKLNQQKQNYQQQIARLEQQ--TLDWQERQQELALAYETEFQN---------------- 845
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREReaELEATLRTARERVEEAEALLEagkcpecgqpvegsph 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 846 ----DEQHIKLDELTEAVHTLDEEYIAVQEKLAQIqEQGREQYARVQALQTKlpqlqAATQTALLQQQEALINAKRYH-Q 920
Cdd:PRK02224 467 vetiEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEER-----REDLEELIAERRETIEEKRERaE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 921 NLTERAADLDAlEALAK---------------ESPKVLNSSIGSLTQQIEALGAVNlAALQELEEARERDGYYRSQSEDv 985
Cdd:PRK02224 541 ELRERAAELEA-EAEEKreaaaeaeeeaeearEEVAELNSKLAELKERIESLERIR-TLLAAIADAEDEIERLREKREA- 617
|
410 420
....*....|....*....|....
gi 1092727057 986 qaaitlleeaIAQIDDKTKERFKE 1009
Cdd:PRK02224 618 ----------LAELNDERRERLAE 631
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
777-996 |
6.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 777 QEQQGRLKQAQLALLEANRQYG-LAEVAVHKLNQQKQNYQQQIARLEQQTLDWQERQQELALAYETEFQNDEQhikLDEL 855
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIElLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE---LARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 856 TEAVHTLDEEYIAVQEKLAQIQEQGREQ-YARVQALQTKLPQLQAATQTALLQQQEALINAKRYHQNLTERAADLDALEA 934
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092727057 935 LAKESPKVLNSSIGSLTQQIEALGAVNLAALQELEEAR-ERDGYYRSQS---EDVQAAITLLEEAI 996
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaEIASLERRKSnipARLLALRDALAEAL 453
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1057-1130 |
6.48e-06 |
|
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: 47.24 E-value: 6.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092727057 1057 STIHLLSGGEKALTAMSLVFALfslNPaPFCLLDEVDAPLDDANTSRFCNLVKEMSAQ-TQFLYISHNRLTMEMA 1130
Cdd:cd00267 76 GYVPQLSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELA 146
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
174-398 |
8.14e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 174 KERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKY-LTAQLNQQQDLLDY--AQWQQSLASADKATAQ 250
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSeKQRELEEKQNEIEKlkKENQSYKQEIKNLESQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 251 HQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQMQR 330
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092727057 331 IHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRREL 398
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
704-911 |
8.66e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 704 RQYSQAQQRAAELLARTNQGQIRREHIERELAQLAEEQTVLQHTSDGLSDDIATLQEAAAELEHQQQTTAHSRQEQQGRL 783
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 784 KQaQLALLEANRQYGLAEVAVH-----KLNQQKQNYQQQIARLEQQTLDWQERQQEL-ALAYETEFQNDEQHIKLDELTE 857
Cdd:COG4942 107 AE-LLRALYRLGRQPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELaALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1092727057 858 AVHTLDEEYIAVQEKLAQIQEQGREQYARVQALQTKLPQLQAATQTALLQQQEA 911
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
170-467 |
1.24e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 170 VSKYKERRKETEGRLKDTREHLQRL-GDLQNELARQvEKLEKQaetaERYKYLTAQLNQQQDLLDyaQWQQSLASADKAT 248
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQGSdLDRTVQQVNQ-EKQEKQ----HELDTVVSKIELNRKLIQ--DQQEQIQHLKSKT 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 249 AQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSqqqTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQM 328
Cdd:TIGR00606 867 NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS---LIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 329 QRIHQEQQQIRVQL--------EENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQ-------QDEANR 393
Cdd:TIGR00606 944 NDIKEKVKNIHGYMkdienkiqDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQkiqerwlQDNLTL 1023
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092727057 394 IRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALnlpdEAETAAAQEAAALLQSQQEHYEEQIIAAEEALHT 467
Cdd:TIGR00606 1024 RKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL----EENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
146-430 |
1.41e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 146 QGMISRIIEARPEELRAYIEEAAGVSKYKERRKETEGRLKDTREHLQRLGD------LQNELARQVEKLEKQAETAERYK 219
Cdd:PRK10246 155 QGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAqasgvaLLTPEQVQSLTASLQVLTDEEKQ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 220 YLTAQLNQQQDLLDYAQwQQSLASADKATAQHQsLQAQQDETVAQVQV----LNDEVHALQTAEQSQQQTVHELSNKRGV 295
Cdd:PRK10246 235 LLTAQQQQQQSLNWLTR-LDELQQEASRRQQAL-QQALAAEEKAQPQLaalsLAQPARQLRPHWERIQEQSAALAHTRQQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 296 LREQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQE-QQQIRVQLEENEL--------QAEEKQTELAEWAMQVAEH 366
Cdd:PRK10246 313 IEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWlAEHDRFRQWNNELagwraqfsQQTSDREQLRQWQQQLTHA 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092727057 367 EERLPELEEAQATLN----AAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALN 430
Cdd:PRK10246 393 EQKLNALPAITLTLTadevAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN 460
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
31-130 |
1.46e-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: 47.97 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 31 GPNGCGKSNVIDAVRWVLGE-ASAKQLRGEsmqdvifngaatrrpAPRASVELVFDNSDHSLQGAWGQYA------EVSI 103
Cdd:cd03241 28 GETGAGKSILLDALSLLLGGrASADLIRSG---------------AEKAVVEGVFDISDEEEAKALLLELgiedddDLII 92
|
90 100
....*....|....*....|....*..
gi 1092727057 104 KRQLTRQGESTYFINNQTVRRRDITDL 130
Cdd:cd03241 93 RREISRKGRSRYFINGQSVTLKLLREL 119
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
165-429 |
1.99e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 165 EEAAGVSKYKERRKETEGRLKDTrehLQRLGDLQNELARQVEKLekQAETAERYKYLTAQLNQQQDLLDYAQWQQSLASA 244
Cdd:PRK10246 301 EQSAALAHTRQQIEEVNTRLQST---MALRARIRHHAAKQSAEL--QAQQQSLNTWLAEHDRFRQWNNELAGWRAQFSQQ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 245 DKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHelsNKRGVLREQIARLEEQIrhqQNLHQRIERdkqaA 324
Cdd:PRK10246 376 TSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQH---AEQRPLRQRLVALHGQI---VPQQKRLAQ----L 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 325 QAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEwAMQVAEHEERLPELEEAQATLNA----------------AFQTQQ 388
Cdd:PRK10246 446 QVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD-VKTICEQEARIKDLEAQRAQLQAgqpcplcgstshpaveAYQALE 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1092727057 389 DEANRIRR------------ELALKQQQLAHAEQTVAKHEERKGRLKQENQAL 429
Cdd:PRK10246 525 PGVNQSRLdalekevkklgeEGAALRGQLDALTKQLQRDESEAQSLRQEEQAL 577
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
142-433 |
2.94e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 142 AVIEQGMISRIIEARpEELRAYIEEAAGVSK-YKERRKETEGRLKDTREHLQRLgdlQNELARQVEKLEKQAETAERYky 220
Cdd:PRK04863 343 ALRQQEKIERYQADL-EELEERLEEQNEVVEeADEQQEENEARAEAAEEEVDEL---KSQLADYQQALDVQQTRAIQY-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 221 ltaqlNQQQDLLDYAQWQQSLAS--ADKATAQHQSLQAQQDE------------TVAQ------------VQVLNDEVHA 274
Cdd:PRK04863 417 -----QQAVQALERAKQLCGLPDltADNAEDWLEEFQAKEQEateellsleqklSVAQaahsqfeqayqlVRKIAGEVSR 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 275 lQTAEQSQQQTVHELSNKRGV------LREQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIhQEQQQIRVQLEENELQ 348
Cdd:PRK04863 492 -SEAWDVARELLRRLREQRHLaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQEELEARLES 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 349 AEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQ---QQLAHAEQTVAKHE--------- 416
Cdd:PRK04863 570 LSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFedsQDVTEYMQQLLEREreltverde 649
|
330
....*....|....*....
gi 1092727057 417 --ERKGRLKQENQALNLPD 433
Cdd:PRK04863 650 laARKQALDEEIERLSQPG 668
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-425 |
3.67e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 171 SKYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYK--YLTAQLNQQQDLLD----YAQWQQSLASA 244
Cdd:TIGR04523 127 NKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELnlLEKEKLNIQKNIDKiknkLLKLELLLSNL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 245 DKATAQHQSLQAQQDETVAQVQVLNDEVHALQtaeQSQQQTVHELSNkrgvlreqiarleeqirhqqnlhqrierdkqaA 324
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQ---QEINEKTTEISN--------------------------------T 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 325 QAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEaqatlnaafQTQQDEANRIRRELALKQQQ 404
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---------QKEQDWNKELKSELKNQEKK 322
|
250 260
....*....|....*....|.
gi 1092727057 405 LAHAEQTVAKHEERKGRLKQE 425
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQ 343
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
172-381 |
4.29e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 172 KYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQLNQQQdlldyaqwQQSLASADKATAQH 251
Cdd:pfam05557 24 EHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK--------KKYLEALNKKLNEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 252 QSLQAQQDETVAqvqVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQiarLEEQIRHQQNLHQRIerdkQAAQAQMQRI 331
Cdd:pfam05557 96 ESQLADAREVIS---CLKNELSELRRQIQRAELELQSTNSELEELQER---LDLLKAKASEAEQLR----QNLEKQQSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092727057 332 HQEQQQIRVQLEENELQAEEK------QTELAewamQVAEHEERLPELEEAQATLN 381
Cdd:pfam05557 166 AEAEQRIKELEFEIQSQEQDSeivknsKSELA----RIPELEKELERLREHNKHLN 217
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
263-888 |
4.48e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 263 AQVQVLNDEVHALQTAEQSQQQTVHELSNKrgvLREQIARLEEQIRHQQN-LHQRIERDKQAAQAQMQRIHQEQQQIRVQ 341
Cdd:pfam12128 258 LRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWKEKRDeLNGELSAADAAVAKDRSELEALEDQHGAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 342 LEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQT-QQDEANRIRRELA-LKQQQLAHAEQTVAKHEERK 419
Cdd:pfam12128 335 LDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRrRSKIKEQNNRDIAgIKDKLAKIREARDRQLAVAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 420 GRLKQENQALNLPDEAETAAAQEAAALLQSQQEHYEEQI--IAAEEALHTAREAFQTTSNRFQSLKQQHITLQAQQQALS 497
Cdd:pfam12128 415 DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 498 QILSQQQEAADFWQATDHAATPQLWQhitAPAEWQHALSvilaerlharavphgfvppaPLPQGQAAWLSDDLSG---GI 574
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEERQS---ALDELELQLF--------------------PQAGTLLHFLRKEAPDweqSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 575 KKSLPVQALLnqiqaqppfQTALHHWLDGVLCAPDLS-YALAHQSDLGAHQIWLTPEGHQVDKVSVLLYA-KSEQESLIA 652
Cdd:pfam12128 552 GKVISPELLH---------RTDLDPEVWDGSVGGELNlYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlQSAREKQAA 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 653 QKARLDGIASELENLAPELSAAEAAFKQAEATVRSSEVQHKNLMQQQqqhTRQYSQAQQRAAEllartnqgqiRREHIER 732
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK---NKALAERKDSANE----------RLNSLEA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 733 ELAQLA-EEQTVLQHTSDglsddiaTLQEAAAELEHQQQTTAHSRQEQQGRLKQAQLALLE-ANRQYGLAEVAVHKLNQQ 810
Cdd:pfam12128 690 QLKQLDkKHQAWLEEQKE-------QKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSgAKAELKALETWYKRDLAS 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 811 KQNYQQQIARLEQ------QTLDWQERQQELALAYEtEFQNDEQHIKLDELTEAVHTLDEEYIAVQEKLAQIQEQGREQY 884
Cdd:pfam12128 763 LGVDPDVIAKLKReirtleRKIERIAVRRQEVLRYF-DWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRR 841
|
....
gi 1092727057 885 ARVQ 888
Cdd:pfam12128 842 AKLE 845
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-126 |
4.50e-05 |
|
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: 46.52 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 3 LTHIKLSGFKSFtDPTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVlgeASAKQLRGESMQDVIfngaatRRPAPRASVEL 82
Cdd:cd03242 1 LKSLELRNFRNY-AELELEFEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELI------RWGAEEAKISA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1092727057 83 VFDNsdhslqgawgQYAEVSIKRQLTRQGESTYFINNQTVRRRD 126
Cdd:cd03242 71 VLER----------QGGELALELTIRSGGGRKARLNGIKVRRLS 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-505 |
5.82e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 151 RIIEARPEELRayieEAAGVSKYKERRKETEGRLKDTREHLQRLGDlQNELARQVEKLEKQAETAERYKYLTAQLNQQQD 230
Cdd:PTZ00121 1268 RQAAIKAEEAR----KADELKKAEEKKKADEAKKAEEKKKADEAKK-KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 231 LLDYAQWQQSLASADKATAQHQSLQA---QQDETVAQVQVLNDEVHALQTAEQSQQQTvhELSNKRGvlrEQIARLEEQI 307
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKKKADEAKKKA--EEDKKKA---DELKKAAAAK 1417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 308 RHQQNLHQRIERDKQAAQAQmqrihqEQQQIRVQLEENELQAEEKQTelAEWAMQVAEHEERLPELEEaqatlNAAFQTQ 387
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAK------KKAEEAKKADEAKKKAEEAKK--AEEAKKKAEEAKKADEAKK-----KAEEAKK 1484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 388 QDEANRIRRELALKQQQLAHAEQTVAKHEE-RKGRLKQENQALNLPDEAETAAAQEAAALLQSQQEHYEEQIIAAEEALH 466
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
330 340 350
....*....|....*....|....*....|....*....
gi 1092727057 467 TAREAFQTTSNRFQSLKQQHITLQAQQQALSQILSQQQE 505
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
519-615 |
9.96e-05 |
|
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: 42.99 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 519 PQLWQHITAPAEWQHALSVILAERLHARAV----------------PHGFVPPAPLPQGQAAWLSDDLSGGIKKSLP--V 580
Cdd:smart00968 5 GRVADLISVDPKYETALEAALGGRLQAVVVdteetakkaieflkknRLGRATFLPLDKIKPRSPAGSKLREALLPEPgfV 84
|
90 100 110
....*....|....*....|....*....|....*
gi 1092727057 581 QALLNQIQAQPPFQTALHHWLDGVLCAPDLSYALA 615
Cdd:smart00968 85 GPAIDLVEYDPELRPALEYLLGNTLVVDDLETARR 119
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-356 |
1.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 175 ERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQLNQQQDLLD-YAQWQQSLASADKATAQHQS 253
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 254 LQAQQDEtvaQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQ 333
Cdd:COG4717 151 LEERLEE---LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|...
gi 1092727057 334 EQQQIRVQLEENELQAEEKQTEL 356
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARL 250
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
158-433 |
1.06e-04 |
|
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: 46.87 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 158 EELRAYIEEAAGVSK-YKERRKETEGRLKDTREHLQRLG----DLQNELARQ----------VEKLEKQAE-------TA 215
Cdd:COG3096 357 EELTERLEEQEEVVEeAAEQLAEAEARLEAAEEEVDSLKsqlaDYQQALDVQqtraiqyqqaVQALEKARAlcglpdlTP 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 216 ERYKYLTAQLNQQQDLLDYA--QWQQSLASADKATAQHqslqaqqDETVAQVQVLNDEVHALQTAEQSQQQTVHELSnkr 293
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEvlELEQKLSVADAARRQF-------EKAYELVCKIAGEVERSQAWQTARELLRRYRS--- 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 294 gvLREQIARLEEQIRHQQNLHQRIERdKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPEL 373
Cdd:COG3096 507 --QQALAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSEL 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 374 EEAQATLNA----------AFQTQQDEANRIRRELALK---QQQLAHAEQTVAKHE-----------ERKGRLKQENQAL 429
Cdd:COG3096 584 RQQLEQLRArikelaarapAWLAAQDALERLREQSGEAladSQEVTAAMQQLLEREreatverdelaARKQALESQIERL 663
|
....
gi 1092727057 430 NLPD 433
Cdd:COG3096 664 SQPG 667
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-386 |
1.34e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 201 LARQVEKLEKQAETAERYKyltAQLNQQQDLLDYAQWQQSLasadkaTAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQ 280
Cdd:COG3206 180 LEEQLPELRKELEEAEAAL---EEFRQKNGLVDLSEEAKLL------LQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 281 SQQQTVHELSNKRGV--LREQIARLEEQIRHQ-----------QNLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEENEL 347
Cdd:COG3206 251 SGPDALPELLQSPVIqqLRAQLAELEAELAELsarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREA 330
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092727057 348 QAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQT 386
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
275-924 |
1.35e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 275 LQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQEQQQIRvqlEENELQAEEKQT 354
Cdd:TIGR00618 203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRA---RIEELRAQEAVL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 355 ELAEWAMQVAEHEERLPELEEAQATLNaafQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALNLPDE 434
Cdd:TIGR00618 280 EETQERINRARKAAPLAAHIKAVTQIE---QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 435 AETAAAQEAAALLQSQQEHYEEQiiaaeeALHTAREAFQTTSNRFQSLKQQhitLQAQQQALSQILSQQQEAADFWQATD 514
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQ------HIHTLQQQKTTLTQKLQSLCKE---LDILQREQATIDTRTSAFRDLQGQLA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 515 HAATPQLWQHITAPAEWQHALSVILAERLHARAVPHGFVPPAPLPQGQAAWLSDDLSGGIKKSLPVQALLNQIQAQPPFQ 594
Cdd:TIGR00618 428 HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLC 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 595 TALHHW----LDGVLCAPDLSYALAHQSDLGAHQIWLTPEGHQVDKVSVLLYAKSEQESLIAQ------------KARLD 658
Cdd:TIGR00618 508 GSCIHPnparQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQsfsiltqcdnrsKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 659 GIASELENLAPELSAAEAAFKQAEATVRSSEV--QHKNLMQQQQQHTRQYSQAQQRAAELLARTN----QGQIR------ 726
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRklQPEQDLQDVRLHLQQCSQELALKLTALHALQltltQERVRehalsi 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 727 REHIERELAQLAEEQTVLQHTSDGLSDDIATL---QEAAAELEHQQQTTAHSRQEQQGRL--KQAQLALLEANRQYGLAE 801
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLaqcQTLLRELETHIEEYDREFNEIENASssLGSDLAAREDALNQSLKE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 802 VAVHKLNQQKQNYQQQIARLEQQTLDWQERQQELALAYETEFQNDEQHIKLDELTEAVHTLDEE-------YIAVQEKLA 874
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdediLNLQCETLV 827
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1092727057 875 QIQEQGREQYARVQALQTKLPQLQAATQTALLQQQEALINAKRYHQNLTE 924
Cdd:TIGR00618 828 QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
150-341 |
1.61e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 150 SRIIEARPEELRAYIEEA-AGVSKYKERRK--ETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYkyLTAQLN 226
Cdd:COG3206 177 LEFLEEQLPELRKELEEAeAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ--LGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 227 QQQDLLDYAQWQQSLASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTA-EQSQQQTVHELSNKRGVLREQIARLEE 305
Cdd:COG3206 255 ALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1092727057 306 QIRHQQNL----------HQRIERDKQAAQAQMQRIHQEQQQIRVQ 341
Cdd:COG3206 335 QLAQLEARlaelpeleaeLRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
252-428 |
1.83e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 252 QSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQ---- 327
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 328 ------------------MQRIHQEQQQIRVQLEENELQAEEKQTELAEwamQVAEHEERLPELEEAQATLNAAFQTQQD 389
Cdd:COG3883 106 dvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEA---KLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092727057 390 EANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQA 428
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-512 |
1.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDpTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQLrgesmqDVIFNGAATRRPAPRASV 80
Cdd:COG4717 1 MKIKELEIYGFGKFRD-RTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERLEKEA------DELFKPQGRKPELNLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 81 ELVFDNSDHSLQGAWGQYAEVSIKRQLTRQGESTYFINNQTVRRRDITDLFLGTGVGARGYAVIEQGMisRIIEARPEEL 160
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL--AELPERLEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 161 RAYIEEaagvskYKERRKETEGRLKDTREHLQRLGDLQNELarQVEKLEKQAETAERYKYLTAQLNQQQDLLDYAQWQQS 240
Cdd:COG4717 152 EERLEE------LRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 241 LASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERD 320
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 321 KQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELAL 400
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 401 KQQQLAHAEQTVAKHEERKGRLKQENQALNLPDEAETAAAQEAAALLQSQQEHYEEQIIAAEEALHTAREAFQTTSNRFQ 480
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
490 500 510
....*....|....*....|....*....|..
gi 1092727057 481 SLKQQHiTLQAQQQALSQILSQQQEAADFWQA 512
Cdd:COG4717 464 QLEEDG-ELAELLQELEELKAELRELAEEWAA 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-396 |
2.53e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 156 RPEELRayieEAAGVSKYKERRKETEGRLKDTR--EHLQRLGDLQNELARQVEKLEK-----QAETAERYKYLTAQLNQQ 228
Cdd:PTZ00121 1553 KAEELK----KAEEKKKAEEAKKAEEDKNMALRkaEEAKKAEEARIEEVMKLYEEEKkmkaeEAKKAEEAKIKAEELKKA 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 229 QDLLDYAQWQQSLASADKATAQhQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKrgvlrEQIARLEEQIR 308
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA-----EALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 309 HQQNLHQRIERDKQAAQaQMQRIHQEQ----QQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAF 384
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAE-ELKKAEEENkikaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
250
....*....|..
gi 1092727057 385 QTQQDEANRIRR 396
Cdd:PTZ00121 1782 EEELDEEDEKRR 1793
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-89 |
2.74e-04 |
|
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: 43.41 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1 MRLTHIKLSGFKSFTDPTTIHVPG----QLVAVIGPNGCGKSNVIDAVRWVL-GEASAKQlRGESMQDVIFNGAATrrpa 75
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFTGldnnGLFLICGPTGAGKSTILDAITYALyGKTPRYG-RQENLRSVFAPGEDT---- 75
|
90
....*....|....
gi 1092727057 76 prASVELVFDNSDH 89
Cdd:cd03279 76 --AEVSFTFQLGGK 87
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
183-456 |
3.77e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 183 RLKDTREHLQRLGDLQNELARQVEKLEKQ-AETAErykyltaqlnQQQDLLDYAQWQQSLASADKataqHQSLQAQQDET 261
Cdd:COG5185 269 KLGENAESSKRLNENANNLIKQFENTKEKiAEYTK----------SIDIKKATESLEEQLAAAEA----EQELEESKRET 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 262 VAQVQVLNDEVHALQTAEQSQQQTVHElSNKRGVLREQIARLEEQIrhqQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQ 341
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKE-EIENIVGEVELSKSSEEL---DSFKDTIESTKESLDEIPQNQRGYAQEILAT 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 342 LEEN----ELQAEEKQTELAEWAMQVAEHEERLPELE--------EAQATLNAAFQTQQDEANR-IRRELALKQQQLAHA 408
Cdd:COG5185 411 LEDTlkaaDRQIEELQRQIEQATSSNEEVSKLLNELIselnkvmrEADEESQSRLEEAYDEINRsVRSKKEDLNEELTQI 490
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1092727057 409 EQTVA--KHEERKGRLKQENQALNLPDEAETAAAQEAAALLQSQQEHYEE 456
Cdd:COG5185 491 ESRVStlKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILA 540
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1058-1121 |
4.19e-04 |
|
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: 42.97 E-value: 4.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092727057 1058 TIHLLSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDANTSRFCNLVKEMSAQT---QFLYIS 1121
Cdd:cd03277 123 DPHHQSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEgtsQYFLIT 189
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
153-430 |
4.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 153 IEARPEELRAYIEEAA--------GVSKYKERRKETEGRLKDTREHLQRLG-DLQN------ELARQVEKLEKQAETA-E 216
Cdd:PRK02224 319 LEDRDEELRDRLEECRvaaqahneEAESLREDADDLEERAEELREEAAELEsELEEareaveDRREEIEELEEEIEELrE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 217 RYKYLTAQLNQQQDLLD------------YAQWQQSLASADKATAQHQSLQAQQDETVAQvQVLNDEVHALQTAEQSQQq 284
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEelreerdelrerEAELEATLRTARERVEEAEALLEAGKCPECG-QPVEGSPHVETIEEDRER- 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 285 tVHELSNKRGVLREQIARLEEqirhqqnlhqRIERDKQAAQAqmqrihqeqqqirvqleENELQAEEKQTELAEwaMQVA 364
Cdd:PRK02224 477 -VEELEAELEDLEEEVEEVEE----------RLERAEDLVEA-----------------EDRIERLEERREDLE--ELIA 526
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092727057 365 EHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALN 430
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE 592
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-471 |
5.13e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 151 RIIEAR-PEELRAYIE--EAAGVSKYKE-RRKETEGRLKDTREHLQrlgDLQNELARQVEKLEKQAETAERYKYLTAQLN 226
Cdd:PTZ00121 1177 KAEAARkAEEVRKAEElrKAEDARKAEAaRKAEEERKAEEARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 227 QQQDLLDYAQWQQSLASADKATAQHQSLQAQQDETVAQVqvlnDEvhaLQTAEQSQQqtVHELSNKRGVLR---EQIARL 303
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA----DE---AKKAEEKKK--ADEAKKKAEEAKkadEAKKKA 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 304 EEQIRHQQNLHQRIERDKQAAQAQMQRihQEQQQIRVQLEENELQAEEKQTE----LAEWAMQVAEHEERLPELEE-AQA 378
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAE--AEAAADEAEAAEEKAEAAEKKKEeakkKADAAKKKAEEKKKADEAKKkAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 379 TLNAAFQTQQDEANRIR-RELALKQQQLAHAEQTVAKHEER------KGRLKQENQALNLPDEAETAAAQEAAALLQSQQ 451
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKaDEAKKKAEEKKKADEAKKKAEEAkkadeaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
330 340
....*....|....*....|
gi 1092727057 452 EHYEEQIIAAEEALHTAREA 471
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEA 1502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-471 |
8.44e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 156 RPEELRAYIEEAAGVSKYK----ERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQLNQQQDL 231
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKkkaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 232 LDYAQWQQSLASADKATAQHQSLQAQQDETVAQVQVLNDEvhALQTAEQSQQqtVHELSNKRGVLR--EQIARLEEQIRH 309
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE--AKKKAEEKKK--ADEAKKKAEEAKkaDEAKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 310 QQNLHQRIERDKQAAQAQmqrihqEQQQIRVQLEENELQAEEKQTElAEWAMQVAEHEERLPELEEAQATLNAAFQTQQD 389
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAK------KKAEEAKKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 390 EANRIrrELALKQQQLAHAEQT-----VAKHEERKG--RLKQENQALNLPDEAETAAAQEAAALLQSQQEHYEEQIIAAE 462
Cdd:PTZ00121 1532 EAKKA--DEAKKAEEKKKADELkkaeeLKKAEEKKKaeEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
....*....
gi 1092727057 463 EALHTAREA 471
Cdd:PTZ00121 1610 EEAKKAEEA 1618
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-56 |
8.76e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 42.97 E-value: 8.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092727057 1 MRLTHIKLSGFKSFTDpTTIHVPGQLVAVIGPNGCGKSNVIDAVRWVLGEASAKQL 56
Cdd:pfam13175 1 MKIKSIIIKNFRCLKD-TEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFE 55
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
177-471 |
1.01e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 177 RKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERY-----------------KYLTAQLNQQQDLLD--YAQW 237
Cdd:PRK04863 781 RAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFigshlavafeadpeaelRQLNRRRVELERALAdhESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 238 QQSLASADKATAQHQSLQAQQ-------DETVAQ-VQVLNDEVHALQTAE---QSQQQTVHELSNKRGVLR---EQIARL 303
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALNRLLprlnllaDETLADrVEEIREQLDEAEEAKrfvQQHGNALAQLEPIVSVLQsdpEQFEQL 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 304 EEQirHQQNLHQRIERDKQA-------------AQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEwamQVAEHEERL 370
Cdd:PRK04863 941 KQD--YQQAQQTQRDAKQQAfaltevvqrrahfSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRARE---QLRQAQAQL 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 371 PELEEAQATLNAAFQTQQDEANRIRREL-ALKQQQLAHAE-QTVAKHEERKGRLKQENQALNlpdeaetaAAQEAAALLQ 448
Cdd:PRK04863 1016 AQYNQVLASLKSSYDAKRQMLQELKQELqDLGVPADSGAEeRARARRDELHARLSANRSRRN--------QLEKQLTFCE 1087
|
330 340
....*....|....*....|...
gi 1092727057 449 SQQEHYEEQIIAAEEALHTAREA 471
Cdd:PRK04863 1088 AEMDNLTKKLRKLERDYHEMREQ 1110
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
519-615 |
1.08e-03 |
|
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: 39.94 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 519 PQLWQHITAPAEWQHALSVILAERLHA----------RAVPH------GFVPPAPLPQGQAAWLSDdlsgGIKKSLPVQA 582
Cdd:pfam06470 6 GRLADLIEVDEGYEKAVEAALGGRLQAvvvddeddakRAIEFlkknklGRATFLPLDRLKPRPRRP----GADLKGGAGP 81
|
90 100 110
....*....|....*....|....*....|...
gi 1092727057 583 LLNQIQAQPPFQTALHHWLDGVLCAPDLSYALA 615
Cdd:pfam06470 82 LLDLVEYDDEYRKALRYLLGNTLVVDDLDEALE 114
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
288-418 |
1.29e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 288 ELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTElAEWAMQVAEHE 367
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEAAYEIAEAN 274
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092727057 368 ERLpeleEAQATLNAAFQTQQDEANRIRRELALKQQQL-----AHAEQTVAKHEER 418
Cdd:COG2268 275 AER----EVQRQLEIAEREREIELQEKEAEREEAELEAdvrkpAEAEKQAAEAEAE 326
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
649-879 |
1.48e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 649 SLIAQKARLDGIASELENLAPELSAAEAAFKQAEATVRSSEVQHKNLMQQQQQHTRQYSQAQQRAAELLARTNQGQIRRE 728
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 729 HIERELAQ----LAEEQTVLQHTSDGLSDDIATLQEAAAELEHQQQTTAHSRQEQQGRLKQAQLALLEANRQYGLAEVAV 804
Cdd:COG4942 94 ELRAELEAqkeeLAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092727057 805 HKLNQQKQNYQQQIARLEQQtldwQERQQELALAYETEFQNDEQhiKLDELTEAVHTLDEEYIAVQEKLAQIQEQ 879
Cdd:COG4942 174 AELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAA--ELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
231-560 |
1.48e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 231 LLDYAQWQQSL--ASADKATAQHQSLQAQQdetvAQVQVLNDEVHALQTAEQsQQQTVHELSNKRGVLREQIARLEEQIR 308
Cdd:PRK10929 22 APDEKQITQELeqAKAAKTPAQAEIVEALQ----SALNWLEERKGSLERAKQ-YQQVIDNFPKLSAELRQQLNNERDEPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 309 -----------HQQNLH---QRIERDKQAAQAQ---------MQRIHQEQQQIRVQLEENE--LQAEEK------QTELA 357
Cdd:PRK10929 97 svppnmstdalEQEILQvssQLLEKSRQAQQEQdrareisdsLSQLPQQQTEARRQLNEIErrLQTLGTpntplaQAQLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 358 EWAMQVAEHEERLPELEEAQATLNaafqtQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALnlpdeaet 437
Cdd:PRK10929 177 ALQAESAALKALVDELELAQLSAN-----NRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERAL-------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 438 aaaqEAAALLQSQQEHYEEQIIaaeealhtarEAFQTTSNRFQSLKQQhitlqaqQQALSQILSQQQEAAdfwqatdhAA 517
Cdd:PRK10929 244 ----ESTELLAEQSGDLPKSIV----------AQFKINRELSQALNQQ-------AQRMDLIASQQRQAA--------SQ 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1092727057 518 TPQLWQHITAPAEWQHALSV--ILAERLHARAVPhgfVPPAPLPQ 560
Cdd:PRK10929 295 TLQVRQALNTLREQSQWLGVsnALGEALRAQVAR---LPEMPKPQ 336
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
346-485 |
1.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 346 ELQaeEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQE 425
Cdd:COG1579 11 DLQ--ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 426 NQALNLpdeaetaaaQEAAALLQSQQEHYEEQIIAAEEALHTAREAFQTTSNRFQSLKQQ 485
Cdd:COG1579 89 KEYEAL---------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
264-419 |
1.54e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 264 QVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLE-EQIRHQQNLHQRIERDKQAAQAQmqriHQEQQQIRVQL 342
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEkERLAAQEQKKQAEEAAKQAALKQ----KQAEEAAAKAA 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092727057 343 EENELQAEEKQTELAEWAMQvAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERK 419
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKK 218
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
176-376 |
1.57e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 176 RRKETEGRLKDTREHLQRLGDLQNELARQVEKlekqaetaerYKYLTAQLNQQQDLLDYAQWQQSLASADkaTAQ-HQSL 254
Cdd:PRK10929 235 RQREAERALESTELLAEQSGDLPKSIVAQFKI----------NRELSQALNQQAQRMDLIASQQRQAASQ--TLQvRQAL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 255 -----QAQQ-DETVAQVQVLNDEVHALQTAEQSQQqtvheLSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQM 328
Cdd:PRK10929 303 ntlreQSQWlGVSNALGEALRAQVARLPEMPKPQQ-----LDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQ 377
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092727057 329 QRIHQEQQQIRVQLEENELQAEEKQT-ELAEWAMQVAEHEERLPELEEA 376
Cdd:PRK10929 378 NRILDAQLRTQRELLNSLLSGGDTLIlELTKLKVANSQLEDALKEVNEA 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-355 |
1.66e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 151 RIIEARPEELRAYIEEAAGVsKYKERRKETEGR-----LKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQL 225
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKM-KAEEAKKAEEAKikaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 226 NQQqdlldyaqwqqslASADKATAQhQSLQAQQDETVAQVQVLNDEVHAlQTAEQSQQQTVHELSNKRGVLREQiarlEE 305
Cdd:PTZ00121 1667 AKK-------------AEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKAE----EE 1727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1092727057 306 QIRHQQNLHQRIERDKQAAQaQMQRIHQEQQQIRVQLEENELQAEEKQTE 355
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1062-1145 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 1062 LSGGEKALTAMSLVFAL---FSLNpAPFCLLDEVDAPLDDAN-TSRFCNLVKEMSAQTQFLYI--SHNRLTMEMAEQLVG 1135
Cdd:cd03240 116 CSGGEKVLASLIIRLALaetFGSN-CGILALDEPTTNLDEENiEESLAEIIEERKSQKNFQLIviTHDEELVDAADHIYR 194
|
90
....*....|
gi 1092727057 1136 VTMQEKGVSR 1145
Cdd:cd03240 195 VEKDGRQKSR 204
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
227-415 |
1.77e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 227 QQQDLLDYaqwQQSLASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQ 306
Cdd:COG1579 5 DLRALLDL---QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 307 IRHQQNlhqriERDKQAAQAQMQRIHQEQQQirvqLEENELQAEEKQTELAEwamQVAEHEErlpELEEAQATLNAAFQT 386
Cdd:COG1579 82 LGNVRN-----NKEYEALQKEIESLKRRISD----LEDEILELMERIEELEE---ELAELEA---ELAELEAELEEKKAE 146
|
170 180
....*....|....*....|....*....
gi 1092727057 387 QQDEANRIRRELALKQQQLAHAEQTVAKH 415
Cdd:COG1579 147 LDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
852-1001 |
1.87e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 852 LDELTEAVHTLDEEYIAVQEKLAQIQEQGREQYARVQALQTKLPQLQAAT-----QTALLQQQEALINAKRYHQNLTEra 926
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAAlqpgeEEELEEERRRLSNAEKLREALQE-- 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092727057 927 adldALEALAKESPKVLnssigsltqqiEALGAvnlaALQELEEARERDGYYRSQSEDVQAAITLLEEAIAQIDD 1001
Cdd:COG0497 231 ----ALEALSGGEGGAL-----------DLLGQ----ALRALERLAEYDPSLAELAERLESALIELEEAASELRR 286
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
755-934 |
1.88e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 755 IATLQEAAAEleHQQQTTAHSRQEQQGRLKQAqLALLEANRQYGLAEVAVHKLNQQKQNYQQQIARLEQQTLDWQERQQE 834
Cdd:COG4913 251 IELLEPIREL--AERYAAARERLAELEYLRAA-LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 835 LALAYetefqNDEQHIKLDELTEAVHTLDEEYIAVQEKLAQIQEQGR--------------EQYARVQALQTKLPQLQAA 900
Cdd:COG4913 328 LEAQI-----RGNGGDRLEQLEREIERLERELEERERRRARLEALLAalglplpasaeefaALRAEAAALLEALEEELEA 402
|
170 180 190
....*....|....*....|....*....|....
gi 1092727057 901 TQTALLQQQEALINAKRYHQNLTeraADLDALEA 934
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELE---AEIASLER 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
296-430 |
1.94e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 296 LREQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEE 375
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1092727057 376 AQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALN 430
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
240-415 |
2.35e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 240 SLASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQS-QQQTVHELSNkrgvLREQIARLEEQIRHQQNLHQRIE 318
Cdd:pfam09787 38 GLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQElEAQQQEEAES----SREQLQELEEQLATERSARREAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 319 RDKQAAQAQMQRIHQEQQQIRVQLEEnelQAEEKQTELAEWAMQV----------AEHEERLPELEEAQATLNAAFQTQQ 388
Cdd:pfam09787 114 AELERLQEELRYLEEELRRSKATLQS---RIKDREAEIEKLRNQLtsksqssssqSELENRLHQLTETLIQKQTMLEALS 190
|
170 180
....*....|....*....|....*..
gi 1092727057 389 DEANRIRRELALKQQQLAHAEQTVAKH 415
Cdd:pfam09787 191 TEKNSLVLQLERMEQQIKELQGEGSNG 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
178-391 |
2.38e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 178 KETEGRLKDTREHLQRLGDLQNELARQVEKL-EKQAETAERYKYLTAQLNQQQDLLDYAQwqQSLASADKATAQHQSLQA 256
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELnEEYNELQAELEALQAEIDKLQAEIAEAE--AEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 257 QQDETVAQVQVL---------NDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQ 327
Cdd:COG3883 97 RSGGSVSYLDVLlgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092727057 328 MQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEA 391
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1062-1121 |
2.86e-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: 40.27 E-value: 2.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092727057 1062 LSGGEKALTAMSLVFALFSLNPAPFCLLDEVDAPLDDAN--TSRfCNLVKEMSAQ--TQFLYIS 1121
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNrkIST-DLLVKEAKKQpgRQFIFIT 172
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-83 |
3.17e-03 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 40.23 E-value: 3.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092727057 23 PGQLVAVIGPNGCGKSNVIDAVrwvlgeasAKQLRGESMQ-DVIFNGAATRRPAPRASVELV 83
Cdd:cd03213 34 PGELTAIMGPSGAGKSTLLNAL--------AGRRTGLGVSgEVLINGRPLDKRSFRKIIGYV 87
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
154-493 |
3.20e-03 |
|
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: 41.86 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 154 EARPEELRAYIEEAAGVSKYKERRKETEGRLKDTREHLQRLgdlQNELaRQVEKLEK-QAETAErykyLTAQLNQQQDLL 232
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLV---QTAL-RQQEKIERyQEDLEE----LTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 233 DYAQWQQSLASADKATAQ-------------HQSLQAQQDETVAQVQVLNdevhALQTAEQSQQQTVHELSNKRGVLREQ 299
Cdd:COG3096 371 EEAAEQLAEAEARLEAAEeevdslksqladyQQALDVQQTRAIQYQQAVQ----ALEKARALCGLPDLTPENAEDYLAAF 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 300 IARLEEQIRHQQNLHQRIeRDKQAAQAQMQRI----------------HQEQQQIRVQLEENELQAEEKQTelaeWAMQV 363
Cdd:COG3096 447 RAKEQQATEEVLELEQKL-SVADAARRQFEKAyelvckiageversqaWQTARELLRRYRSQQALAQRLQQ----LRAQL 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 364 AEHEERLPELEEAQATLNA---AFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALNlPDEAETAAA 440
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEfcqRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR-ARIKELAAR 600
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1092727057 441 QEAAALLQSQQEHYEEQIIAAEEALHTAREAFQTTSNRFQSLKQQHITLQAQQ 493
Cdd:COG3096 601 APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARK 653
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-415 |
3.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 145 EQGMISRIIEARPEELRAYIEEAAGVSKYKERRKET--------------EGRLKDTREHLQRLGDLQNELARQVEKLEK 210
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELkeeieelekeleslEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 211 QA-------ETAERYKYLTAQLNQQQDLL-----DYAQWQQSLASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTA 278
Cdd:PRK03918 281 KVkelkelkEKAEEYIKLSEFYEEYLDELreiekRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 279 EQSQQQTVHELSNKRGVLRE----QIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEE---------- 344
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpv 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1092727057 345 --NELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQ--QQLAHAEQTVAKH 415
Cdd:PRK03918 441 cgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKY 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
127-397 |
3.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 127 ITDLFLGTGVGARGYAVIEQGMISRIIEARPEELRAYIEEAAGVSKYKERRKETEGRLKDTREHLQRLGDLQNELA---- 202
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlell 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 203 ---RQVEKLEKQAETAERYKYLTAQLNQQQDLLDYAQwqqslASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAE 279
Cdd:COG4717 344 driEELQELLREAEELEEELQLEELEQEIAALLAEAG-----VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 280 QSQQQTVHELSnkrgvLREQIARLEEQIrhqqnlhqrierdkQAAQAQMQRIHQEQQQIrvqleENELQAEEKQTELAEW 359
Cdd:COG4717 419 EELLEALDEEE-----LEEELEELEEEL--------------EELEEELEELREELAEL-----EAELEQLEEDGELAEL 474
|
250 260 270
....*....|....*....|....*....|....*...
gi 1092727057 360 AMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRE 397
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
223-356 |
3.53e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 223 AQLNQQQDLLDY--AQWQQSLASADkataQHQSL-QAQQDETVAQVQVLNDEVHALQTAeqsqqqtvheLSNKRGVLREQ 299
Cdd:PRK11281 195 VLLQAEQALLNAqnDLQRKSLEGNT----QLQDLlQKQRDYLTARIQRLEHQLQLLQEA----------INSKRLTLSEK 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092727057 300 IArleEQIRHQQnlhqrierdkQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTEL 356
Cdd:PRK11281 261 TV---QEAQSQD----------EAARIQANPLVAQELEINLQLSQRLLKATEKLNTL 304
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
192-471 |
4.26e-03 |
|
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: 41.48 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 192 QRLGDLQNELARQVEKLEKQAETAErykyltaQLNQQQDLLDYAQWQQSLASadkataqhqslqaqqDETVAQ-VQVLND 270
Cdd:COG3096 843 QRRSELERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKLLPQANLLA---------------DETLADrLEELRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 271 EVHALQTAE---QSQQQTVHELSNKRGVLREQIARLEE-QIRHQQnLHQRIERDKQAAQAQ---MQRIHQ---------- 333
Cdd:COG3096 901 ELDAAQEAQafiQQHGKALAQLEPLVAVLQSDPEQFEQlQADYLQ-AKEQQRRLKQQIFALsevVQRRPHfsyedavgll 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 334 -EQQQIRVQLEENELQAEEKQTELAEwamQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRREL-ALKQQQLAHAEQT 411
Cdd:COG3096 980 gENSDLNEKLRARLEQAEEARREARE---QLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeELGVQADAEAEER 1056
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092727057 412 VAKH-EERKGRLKQENQALNlpdeaetaAAQEAAALLQSQQEHYEEQIIAAEEALHTAREA 471
Cdd:COG3096 1057 ARIRrDELHEELSQNRSRRS--------QLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
154-391 |
4.41e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 154 EARPEELRAYIEEAAgvsKYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKYLTAQLNQQQDLLD 233
Cdd:PRK02224 474 RERVEELEAELEDLE---EEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 234 yAQWQQSLASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEqSQQQTVHELSNKRGVLRE---QIARLEEQIRHQ 310
Cdd:PRK02224 551 -AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-TLLAAIADAEDEIERLREkreALAELNDERRER 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 311 qnLHQRIERDKQ-----------AAQAQMQRIHQEQQQIRVQLEEnelqAEEKQTELAEWAMQVAEHEERLPELEEAQAT 379
Cdd:PRK02224 629 --LAEKRERKREleaefdearieEAREDKERAEEYLEQVEEKLDE----LREERDDLQAEIGAVENELEELEELRERREA 702
|
250
....*....|....*
gi 1092727057 380 LNA---AFQTQQDEA 391
Cdd:PRK02224 703 LENrveALEALYDEA 717
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
174-393 |
4.75e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 41.36 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 174 KERRKETEGRLKDTREH-LQRLGDLQNEL-ARQVEKLEK--QAETA---ERYKYLTAQLN---QQQDLLD----YA---- 235
Cdd:NF012221 1564 KERAEADRQRLEQEKQQqLAAISGSQSQLeSTDQNALETngQAQRDailEESRAVTKELTtlaQGLDALDsqatYAgesg 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 236 -QWQQSLASADKATAQHQSLQAQQdetVAQVQVlndevhalqtaEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLH 314
Cdd:NF012221 1644 dQWRNPFAGGLLDRVQEQLDDAKK---ISGKQL-----------ADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAE 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 315 QRIerDKQAAQAQMQRIHQEQQQIRVQleenelQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNA--AFQTQQDEAN 392
Cdd:NF012221 1710 QDI--DDAKADAEKRKDDALAKQNEAQ------QAESDANAAANDAQSRGEQDASAAENKANQAQADAkgAKQDESDKPN 1781
|
.
gi 1092727057 393 R 393
Cdd:NF012221 1782 R 1782
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
184-405 |
4.85e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 184 LKDTREHLQRLGDL--------QNELARQVEKLEKQAETAERYKYLTAQLNQQQDLL-----DYAQWQQSLASADKATAq 250
Cdd:pfam15921 421 LDDRNMEVQRLEALlkamksecQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLrkvveELTAKKMTLESSERTVS- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 251 hqSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLR-----------------EQIARLEEQIRHQQNL 313
Cdd:pfam15921 500 --DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealklqmaekdKVIEILRQQIENMTQL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 314 HQRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANR 393
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ 657
|
250
....*....|..
gi 1092727057 394 IRRELALKQQQL 405
Cdd:pfam15921 658 LLNEVKTSRNEL 669
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
255-416 |
5.13e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 255 QAQQDETVAQVQVLNDEvhALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQAQMQRIHQE 334
Cdd:COG2268 196 EIIRDARIAEAEAERET--EIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 335 --QQQIRVQLEENELqaeEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELalkqqqLAHAEQTV 412
Cdd:COG2268 274 naEREVQRQLEIAER---EREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKG------LAEAEGKR 344
|
....
gi 1092727057 413 AKHE 416
Cdd:COG2268 345 ALAE 348
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-53 |
5.44e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 5.44e-03
10 20
....*....|....*....|....*...
gi 1092727057 26 LVAVIGPNGCGKSNVIDAVRWVLGEASA 53
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDAL 28
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
150-485 |
6.06e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 150 SRIIEARPEELRAYIEEAAGVSKYKERRKETEGRLKDTREHLQrlgdLQNELARQVEKLEK-QAETAErykyLTAQLNQQ 228
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLN----LVQTALRQQEKIERyQADLEE----LEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 229 QDLLDYAQWQQslasaDKATAQHQSLQAQQDETVAQvqvLNDEVHAL---QTAEQSQQQTVHELSNKRGVLreQIARLEe 305
Cdd:PRK04863 368 NEVVEEADEQQ-----EENEARAEAAEEEVDELKSQ---LADYQQALdvqQTRAIQYQQAVQALERAKQLC--GLPDLT- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 306 qirhQQNLHQRIERDKQAAQAQMQRIHQEQQQIRVQleENELQAEEKQTELAEwamQVAEHEERLPELEEAQATLnAAFQ 385
Cdd:PRK04863 437 ----ADNAEDWLEEFQAKEQEATEELLSLEQKLSVA--QAAHSQFEQAYQLVR---KIAGEVSRSEAWDVARELL-RRLR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 386 TQQDEANRirreLALKQQQLAHAEQTVAKHEERKGRLKQENQALNLPdeaetaaaQEAAALLQSQQEHYEEQIIAAEEAL 465
Cdd:PRK04863 507 EQRHLAEQ----LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKN--------LDDEDELEQLQEELEARLESLSESV 574
|
330 340
....*....|....*....|
gi 1092727057 466 HTAREAFQTTSNRFQSLKQQ 485
Cdd:PRK04863 575 SEARERRMALRQQLEQLQAR 594
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
246-419 |
6.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 246 KATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQIRHQQNLHQRIERDKQAAQ 325
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 326 AQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLNAAFQTQQDEANRIRRELALKQQQL 405
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170
....*....|....
gi 1092727057 406 AHAEQTVAKHEERK 419
Cdd:COG4372 167 AALEQELQALSEAE 180
|
|
| V_AnPalA_UmRIM20_like |
cd09236 |
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ... |
177-407 |
7.70e-03 |
|
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.
Pssm-ID: 185749 [Multi-domain] Cd Length: 353 Bit Score: 40.03 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 177 RKETEGRLKDTREHLQRLGDLQNELARQ--------VEKLEKQAETAE--RYKYLTAQLNQQ------QDLldYAQWQQS 240
Cdd:cd09236 62 RHAEEIRQEDGLERIRASLDDVARLAASdraileeaMDILDDEASEDEslRRKFGTDRWTRPdsheanPKL--YTQAAEY 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 241 LASADKATAQHQSLQAQQDETVAQVQVLNDEVHALQTAEQSQQQTV--HELSNKRGVLREQIARLEEQIRHQQnlhQRIE 318
Cdd:cd09236 140 EGYLKQAGASDELVRRKLDEWEDLIQILTGDERDLENFVPSSRRPSipPELERHVRALRVSLEELDRLESRRR---RKVE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 319 RDKQAAQA---------QMQRIHQEQQQIRVQLE------ENELQAEEK-QTELAEwamQVAEHEERLPELEEAqatlNA 382
Cdd:cd09236 217 RARTKARAddirpeilrEAARLEREYPATEVAPAhfedlfDKRLAKYDKdLDAVSE---EAQEQEEILQQIEVA----NK 289
|
250 260
....*....|....*....|....*.
gi 1092727057 383 AF-QTQQDEANRIRRELALKQQQLAH 407
Cdd:cd09236 290 AFlQSRKGDPATKERERALQSLDLAY 315
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
755-957 |
7.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 755 IATLQEAAAELEHQQQTTAHSRQEQQGRLKQAQLALLEANRQYglaevavHKLNQQKQNYQQQIARLEQQTLDWQERQQE 834
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY-------AELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 835 LalayETEFQNDEQHIKLDELTEAVHTLDEEYIAVQEKLAQIQEQGREQYARVQALQTKLPQLQAATQTALLQQQEALIN 914
Cdd:COG4717 121 L----EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1092727057 915 AKRYHQNLTERAADLDALEALAKESPKVLNSSIGSLTQQIEAL 957
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
172-427 |
8.03e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 172 KYKERRKETEGRLKDTREHLQRLGDLQNELARQVEKLEKQAETAERYKY-------LTAQLNQQQDLLDYAQWQQSLASA 244
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFdvcgsqdEESDLERLKEEIEKSSKQRAMLAG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 245 DKA---------TAQHQS---LQAQQDETVAQVQ-VLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIARLEEQirhqQ 311
Cdd:TIGR00606 661 ATAvysqfitqlTDENQSccpVCQRVFQTEAELQeFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGR----Q 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 312 NLHQRIERDKQAAQAQMQRIHQEQQQIRVQLEENELQ-----AEEKQTELAEWAMQVAEH-EERLPELEEAQATLNAafQ 385
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAA--K 814
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1092727057 386 TQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQ 427
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
328-785 |
8.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 328 MQRIHQEQQQIRvQLEENELQAEEKQTELAEWAMQVAEHEERLPELEEAQATLnaafqTQQDEANRIRRELALKQQQLAH 407
Cdd:COG4717 70 LKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 408 AEQTVAKHEERKGRLKQenqalnlpdeaetaaAQEAAALLQSQQEHYEEQIIAAEEAL-HTAREAFQTTSNRFQSLKQQH 486
Cdd:COG4717 144 LPERLEELEERLEELRE---------------LEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 487 ITLQAQQQALSQILSQQQEAADFWQATDHAATPQlwQHITAPAEWQHALSVILAERLHARAVPHGFVPPAPLPQGQAAWL 566
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 567 SDDLSGGIKKSLPVQALLNQIQAQPPF----QTALHHWLD--GVLCAPDLSYALAHQSDLGAHQIWLTPEGHQVDKVSVL 640
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALeeleEEELEELLAalGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 641 LYAKSEQESLIAQKARLDGIASELENLAPELSAAEAAFKQAEATVRS--SEVQHKNLMQQQQQHTRQYSQAQQRAAELLA 718
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092727057 719 RTNQGQIRREHIERELAQLAEEQTV--LQHTSDGLSDDIATLQEAAAEL----EHQQQTTAHSRQEQQGRLKQ 785
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRELAEEWAALklalELLEEAREEYREERLPPVLE 519
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
23-38 |
8.78e-03 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 39.26 E-value: 8.78e-03
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
752-975 |
8.79e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 752 SDDIATLQEAAAELEHQQQTTAHSRQEQQGRLKQAQLALLEANRQYGLAEVAVHKLNQQKQNYQQQIARLEQQTLDWQER 831
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 832 QQELALAYETEFQNDEQHIKLDELTEAVHTLD-EEYIAVQEKLAQIQEQGREQYARVQALQTKLPQLQAATQTALLQQQE 910
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092727057 911 ALinakryhqnlTERAADLDALEALAKESPKV---LNSSIGSLTQQIEALGAvNLAALQELEEARERD 975
Cdd:COG4942 179 LL----------AELEEERAALEALKAERQKLlarLEKELAELAAELAELQQ-EAEELEALIARLEAE 235
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
322-396 |
8.80e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 8.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092727057 322 QAAQAQMQRIHQEQQQIRVQLEENELQAEEKQTELAEWAMQVAEHEERLPELEE--AQATLNAAFQTQQDEANRIRR 396
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAqlEQLQEKAAETSQERKQKRKEI 221
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
183-430 |
9.25e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 39.67 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 183 RLKDTREHLQRLGDLQNELARQVEKLEKQAETAER-YKYLTAQLNQQQDLL---DYAQWQQSLASADKaTAQHQSLQAQQ 258
Cdd:pfam19220 49 RLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGeLEELVARLAKLEAALreaEAAKEELRIELRDK-TAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 259 DETVAQVQVLNDEVHALQTAEQSQQQTVHELSNKRGVLREQIA-----------RLEEQIRHQQNLHQRIERDKQAAQAQ 327
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLAlleqenrrlqaLSEEQAAELAELTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 328 MQRIHQEQQQIRVQLEEN-------ELQAEEKQTELAEWAMQV--------------AEHEERLPELEEAQATLNAAFQT 386
Cdd:pfam19220 208 RARLRALEGQLAAEQAEReraeaqlEEAVEAHRAERASLRMKLealtaraaateqllAEARNQLRDRDEAIRAAERRLKE 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1092727057 387 QQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQALN 430
Cdd:pfam19220 288 ASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLT 331
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
279-428 |
9.46e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.79 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092727057 279 EQSQQQTVHELSNKRGVLREQIAR--LEEQIRHQQNLhQRIERDKQAAQAQMQRIHQEQQQIRVQleenELQAEEKQTEL 356
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEelQQKQAAEQERL-KQLEKERLAAQEQKKQAEEAAKQAALK----QKQAEEAAAKA 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092727057 357 AEWAMQVAEHEERLPEL------EEAQATLNAAFQTQQDEANRIRRELALKQQQLAHAEQTVAKHEERKGRLKQENQA 428
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAaakkaaAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
|
| |
