|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1153 |
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: 1098.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 2 RLKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIFNGSSGRKPVSQASIE 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 82 LVFDNSETTLVGeyAAYAEISIRRKVTRDGQNSYYLNGTKCRRRDITDIFLGTGLGPRSYSIIEQGMISKLIEAKPEELR 161
Cdd:TIGR02168 81 LVFDNSDGLLPG--ADYSEISITRRLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYSIIEQGKISEIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 162 NFIEEAAGISKYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKYREYKAQERQLKARLSALRWRDLD 241
Cdd:TIGR02168 159 AIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 242 EQVRQRESVIGDQGVSHEALVAEQRNADASIERLRDGHHELSERFNQVQGRFYSVAGDIARVEQSIQHGQQRLRQLQDDF 321
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 322 KEAERTRLETESHLGHDRTLLATLGEELAMLEPEQEMTLAAAEEAAAALEEAELGMHGWQEQWDSFNSRSAEPRRQAEVQ 401
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 402 QARLQQLETSLERQAERQRKLVEEREQLGSDPQDAAMLELAEQLASSEMLLEELQLCEEQVIERLESAREQLQQATQAQQ 481
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 482 QAQGDLQRLGGRLASLEALQQAALEPGAGAAQ-WLHGQGLEQ-QPRLAEGLRVEPGWELAVETVLGADLQAVLVDDFND- 558
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKAlLKNQSGLSGiLGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAa 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 559 -LDFAGLEQGELR----LLLAVGAGATLPGSLLEKVEG------------------RIDLAPWLGQVRPVEDLAQALEQR 615
Cdd:TIGR02168 559 kKAIAFLKQNELGrvtfLPLDSIKGTEIQGNDREILKNiegflgvakdlvkfdpklRKALSYLLGGVLVVDDLDNALELA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 616 GSLGEGQSLVSRDGYWVGRHFLRVRRGGEAEGGVLARGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLR 695
Cdd:TIGR02168 639 KKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 696 RRTQDENRLHGELKASLSASRARAEQVELRRRRLQEELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARR 775
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 776 DTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQEELRLKLEEL 855
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 856 LERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQEQLLADGYDLQGVLAT 935
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 936 LEA--EASEQGTEQELEQLEARIQRLGAINLAAIEEYEQQSERKRYLDAQDADLVEALETLENVIRKIDKETRNRFKDTF 1013
Cdd:TIGR02168 959 LENkiEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTF 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1014 DQINAGLQALFPKVFGGGSAYLELT-GEDLLDTGVTIMARPPGKKNSTIHLLSGGEKALTALALVFAIFKLNPAPFCMLD 1092
Cdd:TIGR02168 1039 DQVNENFQRVFPKLFGGGEAELRLTdPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILD 1118
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24985991 1093 EVDAPLDDANVGRYARLVKEMSESVQFIYITHNKIAMEMADQLMGVTMHEPGCSRLVAVDV 1153
Cdd:TIGR02168 1119 EVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKGVSKIVSVDL 1179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1162 |
0e+00 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 791.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1 MRLKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIFNGSSGRKPVSQASI 80
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIPFEPGITAIVGPNGSGKSNIVDAIRWVLGEQSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 81 ELVFDNSETTLVGEYAayaEISIRRKVTRDGQNSYYLNGTKCRRRDITDIFLGTGLGPRSYSIIEQGMISKLIEAKPEEL 160
Cdd:COG1196 81 SLTFDNSDGTLPIDYD---EVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYSIIGQGMIDRIIEAKPEER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 161 RNFIEEAAGISKYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKYREYKAQERQLKARLSALRWRDL 240
Cdd:COG1196 158 RAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLREL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 241 DEQVRQRESVIGDQGVSHEALVAEQRNADASIERLRDGHHELSERFNQVQGRFYSVAGDIARVEQSIQHGQQRLRQLQDD 320
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 321 FKEAERTRLETESHLGHDRTLLATLGEELAMLEPEQEMTLAAAEEAAAALEEAELGMHGWQEQWDSFNSRSAEPRRQAEV 400
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 401 QQARLQQLETSLERQAERQRKLVEEREQLGSDPQDAAMLELAEQLASSEMLLEELQLCEEqvIERLESAREQLQQATQAQ 480
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE--EEALLELLAELLEEAALL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 481 QQAQGDLQRLGGRLASLEALQQAALEPGAGAAQ-WLHGQGLEQQPRLAEGLRVEPGWELAVETVLGADLQAVLVDDFNDL 559
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 560 DFAGLEQGELRLLLAVGAGATLPGSLLEKVEgridlapwlgqvrpvedLAQALEQRGSLGEGQSLVSRDgywvgrhflrv 639
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARA-----------------ALAAALARGAIGAAVDLVASD----------- 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 640 rrggeaeggvlargqeierlgqeqleqeaaleqldqqlqaLREQQLDLEEQREQLRRRTQDENRLHGELKaslsasRARA 719
Cdd:COG1196 608 ----------------------------------------LREADARYYVLGDTLLGRTLVAARLEAALR------RAVT 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 720 EQVELRRRRLQEELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDhahql 799
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER----- 716
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 800 avrlgsLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPqeelrlkleellerrmsVDEEMRLarlhmDEADRE 879
Cdd:COG1196 717 ------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE-----------------LPEPPDL-----EELERE 768
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 880 LRDaekrrtqaeqqaqllrgqleqlrlecqgldvrrktlqeqlladgydlqgvlatleaeaseqgteqeleqLEARIQRL 959
Cdd:COG1196 769 LER---------------------------------------------------------------------LEREIEAL 779
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 960 GAINLAAIEEYEQQSERKRYLDAQDADLVEALETLENVIRKIDKETRNRFKDTFDQINAGLQALFPKVFGGGSAYLELT- 1038
Cdd:COG1196 780 GPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLTd 859
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1039 GEDLLDTGVTIMARPPGKKNSTIHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMSESVQ 1118
Cdd:COG1196 860 PDDPLETGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQ 939
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....
gi 24985991 1119 FIYITHNKIAMEMADQLMGVTMHEPGCSRLVAVDVEAAMAMVDA 1162
Cdd:COG1196 940 FIVITHNKRTMEAADRLYGVTMQEPGVSRVVSVDLEEAEELAEA 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1152 |
3.04e-107 |
|
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: 364.00 E-value: 3.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIFNGSSGRKPVsQASIEL 82
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLSDLISNGKNGQSGN-EAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 83 VFDNSETTLVGEYaayaEISIRRKVTRDGQNS-YYLNGTKCRRRDITDIFLGTGLGPRSYSIIEQGMISKLIEAKPEELR 161
Cdd:TIGR02169 81 TFKNDDGKFPDEL----EVVRRLKVTDDGKYSyYYLNGQRVRLSEIHDFLAAAGIYPEGYNVVLQGDVTDFISMSPVERR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 162 NFIEEAAGISKYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKYREYKAQERQLKARLSALRWRDLD 241
Cdd:TIGR02169 157 KIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 242 EQVRQRESVIGDQGVSHEALVAEQRNADASIERLRDGHHELSERFN--------QVQGRFYSVAGDIARVEQSIQHGQQR 313
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeeqlRVKEKIGELEAEIASLERSIAEKERE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 314 LRQLQD----DFKEAERTRLETES---HLGHDRTLLATLGEELAMLEPEQEMTLAAAEEAAAALEEAELGMHGWQEQWDS 386
Cdd:TIGR02169 317 LEDAEErlakLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 387 FNSRSAEPRRQAEVQQARLQQLETSLERQAERQRKLVEEREQLgsdpqDAAMLELAEQLASSEmlleelqlceeqviERL 466
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL-----EEEKEDKALEIKKQE--------------WKL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 467 ESAREQLQQATQAQQQAQGDLQRLGGRLASLEaLQQAALEPGAGAAQWLHGQGLEQQPRLAEGL-----------RVEPG 535
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQ-RELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgSVGER 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 536 WELAVETVLGADLQAVLVDDFND----LDFAGLEQG------------ELRLLLAVGAGATLPGSLLEKVE--GRIDLAP 597
Cdd:TIGR02169 537 YATAIEVAAGNRLNNVVVEDDAVakeaIELLKRRKAgratflplnkmrDERRDLSILSEDGVIGFAVDLVEfdPKYEPAF 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 598 W--LGQVRPVEDLAQALEQRGSLgegqSLVSRDGYWVgrhflrvRRGGEAEGGVLAR--GQEIERLGQEQLEQEAA-LEQ 672
Cdd:TIGR02169 617 KyvFGDTLVVEDIEAARRLMGKY----RMVTLEGELF-------EKSGAMTGGSRAPrgGILFSRSEPAELQRLRErLEG 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 673 LDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSA-----SRARAEQVELRRRRLQEELSELEEQRALEH--E 745
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQleqeeEKLKERLEELEEDLSSLEQEIENVKSELKEleA 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 746 QLGEARLLLqEALELMAQDTEQREqLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQAA 825
Cdd:TIGR02169 766 RIEELEEDL-HKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 826 RLTERQEQLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLR 905
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 906 lecqgldVRRKTLQEQLLADGYDLQGVLATLEAEASEQGTEQELEQLEARIQRLGAINLAAIEEYEQQSERKRYLDAQDA 985
Cdd:TIGR02169 924 -------AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA 996
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 986 DLVEALETLENVIRKIDKETRNRFKDTFDQINAGLQALFPKVfGGGSAYLELTG-EDLLDTGVTIMARPPGKKNSTIHLL 1064
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELILENpDDPFAGGLELSAKPKGKPVQRLEAM 1075
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1065 SGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMSESVQFIYITHNKIAMEMADQLMGVTMHEPG 1144
Cdd:TIGR02169 1076 SGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADRAIGVTMRRNG 1155
|
....*...
gi 24985991 1145 CSRLVAVD 1152
Cdd:TIGR02169 1156 ESQVFGLK 1163
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1146 |
9.95e-106 |
|
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: 359.67 E-value: 9.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIFngSSGRKPVSQASIEL 82
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIH--SKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 83 VFDNSETTLVGEYAayaEISIRRKVTRDGQNSYYLNGTKCRRRDITDIFLGTGLGPRSYSIIEQGMISKLIEAKPEELRN 162
Cdd:pfam02463 80 TFDNEDHELPIDKE---EVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 163 FIEEAAGISKYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKYREYKAQERQLKARLSALRWRDLDE 242
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 243 QVRQRESVIGDQGVSHEALVAEQRNADASIERLRDGHHELSERFNQVQGRFYSVAGDIARVEQS---------------I 307
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSellklerrkvddeekL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 308 QHGQQRLRQLQDDFKEAERTRLETESHLGHDRTLLATLGEELAMLEPEQEMTLAAAEEAAAALEEAELGMHGWQEQWDSF 387
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 388 NSRSAEPRRQAEVQQARLQQLETSL-ERQAERQRKLVEEREQLGSDPQDAAMLELAEQLASSEmlleelQLCEEQVIERL 466
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLkEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK------LLKDELELKKS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 467 ESAREQLQQATQAQQQaqgDLQRLGGRLASLEALQQAALEPG----AGAAQWLHGQGLEQQPRLAEGLRVEPGWELAVET 542
Cdd:pfam02463 471 EDLLKETQLVKLQEQL---ELLLSRQKLEERSQKESKARSGLkvllALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 543 VLGADLQAVLVDDFNDLD----FAGLEQGELRLLLAVGAGATLPGSLLEKVEGRIDLAPWLGQVRPVEDLAQALEQRGSL 618
Cdd:pfam02463 548 AVIVEVSATADEVEERQKlvraLTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 619 GEGQSLVSRDGYWVGRHFLRVRRGGEAEGGVLARG-------QEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQR 691
Cdd:pfam02463 628 ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSevkaslsELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQR 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 692 EQLRRRTQDENRLHGELKASLSASRARAEQVELRRRRLQEELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQL 771
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 772 MARRDTLRE-SLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQalERLEQQAARLTERQEQLSLNLEEGEAPQEELRL 850
Cdd:pfam02463 788 VEEEKEEKLkAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE--EELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 851 KLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQllrgQLEQLRLECQGLDVRRKTLQEQLLADGYDLQ 930
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN----LLEEKENEIEERIKEEAEILLKYEEEPEELL 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 931 GVLATLEAEASE--QGTEQELEQLEARIQRLGAINLAAIEEYEQQSERKRYLDAQDADLVEALETLENVIRKIDKETRNR 1008
Cdd:pfam02463 942 LEEADEKEKEENnkEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1009 FKDTFDQINAGLQALFPKVFGGGSAYLELTG-EDLLDTGVTIMARPPGKKNSTIHLLSGGEKALTALALVFAIFKLNPAP 1087
Cdd:pfam02463 1022 FLELFVSINKGWNKVFFYLELGGSAELRLEDpDDPFSGGIEISARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAP 1101
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*....
gi 24985991 1088 FCMLDEVDAPLDDANVGRYARLVKEMSESVQFIYITHNKIAMEMADQLMGVTMHEPGCS 1146
Cdd:pfam02463 1102 FYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVTMVENGVS 1160
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1054-1147 |
4.30e-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: 4.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1054 PGKKNSTIHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMSESVQFIYITHNKIAMEMAD 1133
Cdd:cd03278 104 PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
90
....*....|....
gi 24985991 1134 QLMGVTMHEPGCSR 1147
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 |
9.94e-53 |
|
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: 183.44 E-value: 9.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIFNGSSGRKPVSQASIEL 82
Cdd:cd03278 1 LKKLELKGFKSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIFAGSETRKPANFAEVTL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24985991 83 VFDNSEttlvgeyaayaeisirrkvtrdgqnsyylngtkcrrrditdiflgtglgpRSYSIIEQGMISKLIEAK 156
Cdd:cd03278 81 TFDNSD--------------------------------------------------GRYSIISQGDVSEIIEAP 104
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1029-1140 |
1.17e-25 |
|
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: 105.08 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1029 GGGSAYLELTgedlLDTGVTIMarPPGKKNstiHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYAR 1108
Cdd:cd03239 69 GINSASVEIT----FDKSYFLV--LQGKVE---QILSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSD 139
|
90 100 110
....*....|....*....|....*....|...
gi 24985991 1109 LVKEMSESV-QFIYITHNKIAMEMADQLMGVTM 1140
Cdd:cd03239 140 MIKEMAKHTsQFIVITLKKEMFENADKLIGVLF 172
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-153 |
6.97e-25 |
|
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: 105.07 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1 MRLKCIRLAGFKSFVDPTTV-NFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIF-NGSSGrkpVSQA 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVIsGFDPQFNAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIYkRGQAG---ITKA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24985991 79 SIELVFDNSE--TTLVGeYAAYAEISIRRKVTRDGQNSYYLNGTKCRRRDITDIFLGTGLGPRS-YSIIEQGMISKLI 153
Cdd:cd03273 78 SVTIVFDNSDksQSPIG-FENYPEITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNpHFLIMQGRITKVL 154
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1050-1153 |
3.67e-22 |
|
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: 96.87 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1050 MARPPGKKNSTIHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMS-ESVQFIYITHNKIA 1128
Cdd:cd03275 142 SKNPPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEF 221
|
90 100
....*....|....*....|....*.
gi 24985991 1129 MEMADQLMGVTM-HEPGCSRLVAVDV 1153
Cdd:cd03275 222 FSKADALVGVYRdQECNSSKVLTLDL 247
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1034-1138 |
6.07e-19 |
|
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: 86.58 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1034 YLELTGEdlldtgVTIMARPPGKKNSTIHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEM 1113
Cdd:cd03274 104 FLILQGE------VEQIAQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKER 177
|
90 100
....*....|....*....|....*
gi 24985991 1114 SESVQFIYITHNKIAMEMADQLMGV 1138
Cdd:cd03274 178 TKNAQFIVISLRNNMFELADRLVGI 202
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-169 |
4.95e-18 |
|
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: 85.00 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFKSFVDPTTV-NFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAkNLRGESMTDVIFNGSSGRkpVSQASIE 81
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIePFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYT-HLREEQRQALLHEGSGPS--VMSAYVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 82 LVFDNSETTLVgeyAAYAEISIRRKVTRDgQNSYYLNGTKCRRRDITDIFLGTGLGpRS--YSIIEQGMISKLIEAKPEE 159
Cdd:cd03272 78 IIFDNSDNRFP---IDKEEVRLRRTIGLK-KDEYFLDKKNVTKNDVMNLLESAGFS-RSnpYYIVPQGKINSLTNMKQDE 152
|
170
....*....|
gi 24985991 160 LRNfIEEAAG 169
Cdd:cd03272 153 QQE-MQQLSG 161
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1059-1146 |
6.89e-18 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 82.02 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1059 STIHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMS-ESVQFIYITHNKIAMEMADQLMG 1137
Cdd:cd03227 73 FTRLQLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIH 152
|
....*....
gi 24985991 1138 VTMHEPGCS 1146
Cdd:cd03227 153 IKKVITGVY 161
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-87 |
9.16e-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: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESmtdVIFNGSSGRKPVSQASIEL 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSL---LFLAGGGVKAGINSASVEI 77
|
....*
gi 24985991 83 VFDNS 87
Cdd:cd03239 78 TFDKS 82
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1060-1141 |
6.95e-17 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 81.54 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1060 TIHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMSESVQFIYITHNKIAMEMADQLMGVT 1139
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVK 234
|
..
gi 24985991 1140 MH 1141
Cdd:cd03272 235 FR 236
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-120 |
4.97e-16 |
|
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: 79.15 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAkNLRGESMTDVIFNGSSGRKPVSQASIEL 82
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSS-HLRSKNLKDLIYRARVGKPDSNSAYVTA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 24985991 83 VFDNSEttlvGEYAAYaeisirRKVTRDGQNSYYLNGT 120
Cdd:cd03275 80 VYEDDD----GEEKTF------RRIITGGSSSYRINGK 107
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-209 |
1.39e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 73.89 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 2 RLKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKnlRGESMTDVIFNGSsgrkpvSQASIE 81
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS--RSKLRSDLINVGS------EEASVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 82 LVFDNSETTLvgeyaayaeisirrKVTRDgqnsyylngtkcrrrditdiflgtglgprsysiieQGMISKLIEAKPEELR 161
Cdd:COG0419 73 LEFEHGGKRY--------------RIERR-----------------------------------QGEFAEFLEAKPSERK 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24985991 162 NFIEEAAGISKYKERRRETENRIRRTQENLARLTDLREELERQLERLH 209
Cdd:COG0419 104 EALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLS 151
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-227 |
6.29e-14 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 71.37 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 6 IRLAGFKSFvDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIFNGSSGRKPVSQASIELVFD 85
Cdd:pfam13476 1 LTIENFRSF-RDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 86 NSETTLVGeyaayaEISIRRKVTRDGQNSYYLNGTKCRRRDITdiflgtglgprsysiieQGMISKLIEAKPEELRNFIe 165
Cdd:pfam13476 80 NNDGRYTY------AIERSRELSKKKGKTKKKEILEILEIDEL-----------------QQFISELLKSDKIILPLLV- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24985991 166 eaagiskYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKYREYKAQERQ 227
Cdd:pfam13476 136 -------FLGQEREEEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
524-613 |
3.58e-12 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 64.17 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 524 PRLAEGLRVEPGWELAVETVLGADLQAVLVDDF-----------------------NDLDFAGLEQGELRLLLAVGAGAt 580
Cdd:smart00968 5 GRVADLISVDPKYETALEAALGGRLQAVVVDTEetakkaieflkknrlgratflplDKIKPRSPAGSKLREALLPEPGF- 83
|
90 100 110
....*....|....*....|....*....|....*..
gi 24985991 581 lPGSLLEKVEG----RIDLAPWLGQVRPVEDLAQALE 613
Cdd:smart00968 84 -VGPAIDLVEYdpelRPALEYLLGNTLVVDDLETARR 119
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-85 |
1.92e-11 |
|
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: 66.95 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1 MRLKCIRLAGFKSFVDpTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGEsmtDviFNGSSGRKPVSqASI 80
Cdd:COG3593 1 MKLEKIKIKNFRSIKD-LSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE---D--FYLGDDPDLPE-IEI 73
|
....*
gi 24985991 81 ELVFD 85
Cdd:COG3593 74 ELTFG 78
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-1023 |
4.31e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 177 RRETENRIRRTQENLARLTDLREELE---RQLERLHRQAQAAEKYREYKAQERQLKARLSALRWrdldeQVRQREsvigd 253
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEdarEQIELLEPIRELAERYAAARERLAELEYLRAALRL-----WFAQRR----- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 254 qgvsHEALVAEQRNADASIERLRDGHHELSERFNQVQGRfysvagdIARVEQSI-QHGQQRLRQLQDDFKEAERTRLETE 332
Cdd:COG4913 290 ----LELLEAELEELRAELARLEAELERLEARLDALREE-------LDELEAQIrGNGGDRLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 333 SHLGHDRTLLATLGEELAMLEpeqemtlaaaeeaaaaleeaelgmhgwqeqwDSFNSRSAEPRRQAEVQQARLQQLETSL 412
Cdd:COG4913 359 RRRARLEALLAALGLPLPASA-------------------------------EEFAALRAEAAALLEALEEELEALEEAL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 413 ERQAERQRKLVEEREQLgsdpqdaamlelaeqlassemlleelqlceEQVIERLESAReqlqqatqaqQQAQGDLQRLGG 492
Cdd:COG4913 408 AEAEAALRDLRRELREL------------------------------EAEIASLERRK----------SNIPARLLALRD 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 493 RLAslEALQQAALEPgagaaqwlhgqgleqqPRLAEGLRVEPG---WELAVETVLGADLQAVLVDD---------FNDLD 560
Cdd:COG4913 448 ALA--EALGLDEAEL----------------PFVGELIEVRPEeerWRGAIERVLGGFALTLLVPPehyaaalrwVNRLH 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 561 FAGLEQGE-LRLLLAVGAGATL-PGSLLEKVEGRI-DLAPWLGQ----------VRPVEDLAQalEQRGSLGEGQslvSR 627
Cdd:COG4913 510 LRGRLVYErVRTGLPDPERPRLdPDSLAGKLDFKPhPFRAWLEAelgrrfdyvcVDSPEELRR--HPRAITRAGQ---VK 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 628 DGYWVGRHFLRVRRGGEAEGGVLARGQeIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQdenrlhge 707
Cdd:COG4913 585 GNGTRHEKDDRRRIRSRYVLGFDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-------- 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 708 lkasLSASRARAEQVELRRRRlqeelseleeqraleheqlgearllLQEALELMAQDTEQREQLMARRDTLRESLDRVRQ 787
Cdd:COG4913 656 ----YSWDEIDVASAEREIAE-------------------------LEAELERLDASSDDLAALEEQLEELEAELEELEE 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 788 EARqhkdhahQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQ-LSLNLEEgeapqeelrlkleellerrmsvdeem 866
Cdd:COG4913 707 ELD-------ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEE-------------------------- 753
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 867 RLARLHMDEADRELRDA-EKRRTQAEQQAQLLRGQLEqlrlecqgldvrrKTLQEQLLADGYDLQGVLATLEAeaseqgt 945
Cdd:COG4913 754 RFAAALGDAVERELRENlEERIDALRARLNRAEEELE-------------RAMRAFNREWPAETADLDADLES------- 813
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24985991 946 eqeLEQLEARIQRLGAINLAaieEYEQQSerKRYLDAQdadlveALETLENVIRKIDKEtRNRFKDTFDQINAGLQAL 1023
Cdd:COG4913 814 ---LPEYLALLDRLEEDGLP---EYEERF--KELLNEN------SIEFVADLLSKLRRA-IREIKERIDPLNDSLKRI 876
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-920 |
2.77e-10 |
|
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: 64.99 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1 MRLKCIRLAGFKSFVDPTTVNF--PSNMAAVVGPNGCGKSNIIDAVRWVMgessAKNLRGESMTDVIFNG-SSGRKPVSQ 77
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDFtaLGPIFLICGKTGAGKTTLLDAITYAL----YGKLPRRSEVIRSLNSlYAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 78 ASIELVFDNSEttlvgeYAAYAEISIRRKVTRDGQNSYYLNGTKCRRRDITD---------IFLGTGLGPRSYS---IIE 145
Cdd:TIGR00618 77 AELEFSLGTKI------YRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAakkseteevIHDLLKLDYKTFTrvvLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 146 QGMISKLIEAKPEELRNFIEEAAGISKY-------KERRRETENRIRRTQENLARLTDLREELERQL-ERLHRQAQAAEK 217
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYtqlalmeFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYhERKQVLEKELKH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 218 YREYKAQERQLKARLSALRWRDLDEQVRQRESvigdqgvshEALVAEQRNADASIERlrdgHHELSERFNQvQGRFYSVA 297
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLL---------KQLRARIEELRAQEAV----LEETQERINR-ARKAAPLA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 298 GDIARVEQSIQHGQQRLRQLQDDFKEAERTRLETESHLGHDRTLLATLGEELAMLEPEQEMTLAAAEEAaaaleeaelgm 377
Cdd:TIGR00618 297 AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT----------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 378 hGWQEQWDSFNSRSAEPRRQAEVQQARLQQLetslerQAERQRKLVEEREQLGSDPQDAAMLELAEQLASSEMLLEELQL 457
Cdd:TIGR00618 366 -SIREISCQQHTLTQHIHTLQQQKTTLTQKL------QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 458 CEEQVIERLESAREQLQQATQAQQQAQGDLQRLGGRLASLEALQQAALEPGAGAAQWLhgQGLEQQPRLAEGLRVEPGWE 537
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL--LELQEEPCPLCGSCIHPNPA 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 538 LAVETVLGADLQAVlvddfndldfaglEQGELRLLLAVGAGATLPGSLLEKVEGRIDLApwlgqvrpvEDLAQALEQRGS 617
Cdd:TIGR00618 517 RQDIDNPGPLTRRM-------------QRGEQTYAQLETSEEDVYHQLTSERKQRASLK---------EQMQEIQQSFSI 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 618 LGEGQSLVSRDGYWVGRHFLRVRRGGEAEGGvlargQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRR 697
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNITVRLQDLTEKLSE-----AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 698 TQDENRLHGELKASLSASRARAEQVELRRRRLQEELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDT 777
Cdd:TIGR00618 650 ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS 729
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 778 LRESLdrvrqearQHKDHAHQLAvrLGSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQEELRLKLEELLE 857
Cdd:TIGR00618 730 LGSDL--------AAREDALNQS--LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24985991 858 RRMSVDEEMRLARLHmDEADRELRD--AEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQE 920
Cdd:TIGR00618 800 LLKTLEAEIGQEIPS-DEDILNLQCetLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1060-1120 |
1.32e-09 |
|
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: 60.00 E-value: 1.32e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24985991 1060 TIHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMSESVQFI 1120
Cdd:cd03273 163 SLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFI 223
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
524-613 |
2.77e-09 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 56.12 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 524 PRLAEGLRVEPGWELAVETVLGADLQAVLVDDFND----LDFA--------------GLEQGELRLLLAVGAGAtlpGSL 585
Cdd:pfam06470 6 GRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDakraIEFLkknklgratflpldRLKPRPRRPGADLKGGA---GPL 82
|
90 100 110
....*....|....*....|....*....|..
gi 24985991 586 LEKVEG----RIDLAPWLGQVRPVEDLAQALE 613
Cdd:pfam06470 83 LDLVEYddeyRKALRYLLGNTLVVDDLDEALE 114
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-107 |
3.75e-09 |
|
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: 58.00 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFKSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVM-GESSAKNLRGESMTDVIFNGSSGrkpvsqASIE 81
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKGGAHDPKLIREGEVR------AQVK 74
|
90 100
....*....|....*....|....*.
gi 24985991 82 LVFDNSETtlvGEYAAYAEISIRRKV 107
Cdd:cd03240 75 LAFENANG---KKYTITRSLAILENV 97
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
6-84 |
4.76e-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: 57.69 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 6 IRLAGFKSFVDPTTVN-FPSNMAAVVGPNGCGKSNIIDAVRWVMGeSSAKNLRGESMTDVIFNgSSGRKPVSQASIELVF 84
Cdd:cd03274 6 LVLENFKSYAGEQVIGpFHKSFSAIVGPNGSGKSNVIDSMLFVFG-FRASKMRQKKLSDLIHN-SAGHPNLDSCSVEVHF 83
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
225-1007 |
8.60e-09 |
|
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: 60.24 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 225 ERQLKARLSALRWR--DLDEQVRQRESVIGDQGVSHEALVAEQRNADASIERLRDGHHELSERF----NQVQGRFYSVAG 298
Cdd:pfam12128 229 DIQAIAGIMKIRPEftKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLrtldDQWKEKRDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 299 DIARVEQSIQHGQQRLRQLQDDFKEAERTRLET----ESHLGHDRTLLATLGEELAMLE-PEQEMTLAAAEEAAAALEEA 373
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIETaaadQEQLPSWQSELENLEERLKALTgKHQDVTAKYNRRRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 374 ELGMHGWQEQWDsfNSRSAEPRrQAEVQQARLQQLETSLERQAERQ-RKLVEEREQLGSDPQDAAmLELAEQLASSEMLL 452
Cdd:pfam12128 389 NRDIAGIKDKLA--KIREARDR-QLAVAEDDLQALESELREQLEAGkLEFNEEEYRLKSRLGELK-LRLNQATATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 453 EELQLCeeqviERLESAREQLQQATQAQQQAQGDLQRLGGRL-ASLEALQQA--ALEPGAGAAQWLHGQGLEQQPRLAEG 529
Cdd:pfam12128 465 QLENFD-----ERIERAREEQEAANAEVERLQSELRQARKRRdQASEALRQAsrRLEERQSALDELELQLFPQAGTLLHF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 530 LRVE-PGWE------LAVETVLGADLQAVLVD----DFNDLDFAGLEQGELRLLLAVGAGATLPgSLLEKVEGRIDLAPW 598
Cdd:pfam12128 540 LRKEaPDWEqsigkvISPELLHRTDLDPEVWDgsvgGELNLYGVKLDLKRIDVPEWAASEEELR-ERLDKAEEALQSARE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 599 LgQVRPVEDLAQALEQRGSLGEGQSLvSRDGYWVGRHFLRvRRGGEAEGGVLARGQEIERlgqEQLEQEAALEQLDQQLQ 678
Cdd:pfam12128 619 K-QAAAEEQLVQANGELEKASREETF-ARTALKNARLDLR-RLFDEKQSEKDKKNKALAE---RKDSANERLNSLEAQLK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 679 AL-REQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRrlqeelseleEQRALEHEQLGEARlllQEA 757
Cdd:pfam12128 693 QLdKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARR----------SGAKAELKALETWY---KRD 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 758 LELMAQDTEQREQLMARRDTLRESLDRV---RQEARQHKD-HAHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQ 833
Cdd:pfam12128 760 LASLGVDPDVIAKLKREIRTLERKIERIavrRQEVLRYFDwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 834 LSLNLEEGeapQEELRLKLEELLERRMSVDEEMR-LARLHMDEADRELR-DAEKRRTQAEQQAQLLRGQLEQLRLECQGL 911
Cdd:pfam12128 840 RRAKLEME---RKASEKQQVRLSENLRGLRCEMSkLATLKEDANSEQAQgSIGERLAQLEDLKLKRDYLSESVKKYVEHF 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 912 DVRRKTLQEQLLADGYDlqgvlaTLEAEASEQGTEQ-----ELEQLEARIQRLGAINLAAIEEYEQQSerkRYLDAQDAD 986
Cdd:pfam12128 917 KNVIADHSGSGLAETWE------SLREEDHYQNDKGirlldYRKLVPYLEQWFDVRVPQSIMVLREQV---SILGVDLTE 987
|
810 820
....*....|....*....|.
gi 24985991 987 LVEALETLENVIRKIDKETRN 1007
Cdd:pfam12128 988 FYDVLADFDRRIASFSRELQR 1008
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-84 |
6.14e-08 |
|
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: 53.52 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 6 IRLAGFKSFVDPTTVNFPS-NMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGEsmtdvifnGSSGRKPVSQASIELVF 84
Cdd:cd03227 2 IVLGRFPSYFVPNDVTFGEgSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS--------GVKAGCIVAAVSAELIF 73
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
655-1138 |
6.82e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 655 EIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRrlqeels 734
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE------- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 735 eleeqralEHEQLGEA--------RLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDhAHQLAVRLGSL 806
Cdd:PRK02224 444 --------EAEALLEAgkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERL 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 807 RAQHDStrqALERLEQQAARLTERQEQL-SLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHMDEAD-------- 877
Cdd:PRK02224 515 EERRED---LEELIAERRETIEEKRERAeELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeriesl 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 878 RELRDAEKRRTQAEQQAQLLRGQLEQLRlecQGLDVRRKTLQE-----QLLADGYDLQGVLatlEAEASEQGTEQELEQL 952
Cdd:PRK02224 592 ERIRTLLAAIADAEDEIERLREKREALA---ELNDERRERLAEkrerkRELEAEFDEARIE---EAREDKERAEEYLEQV 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 953 EARIQRL-----------GAINlAAIEEYEQQSERKRYLDAQDADLvEAL----ETLENVIRKIDKETRNRFKDTFDQIn 1017
Cdd:PRK02224 666 EEKLDELreerddlqaeiGAVE-NELEELEELRERREALENRVEAL-EALydeaEELESMYGDLRAELRQRNVETLERM- 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1018 agLQALFPKVFGGGS-AYLELTGEDLLdtgvTIMarppgKKNSTI---HLLSGGEKALTALALVFAIFKL--------NP 1085
Cdd:PRK02224 743 --LNETFDLVYQNDAySHIELDGEYEL----TVY-----QKDGEPlepEQLSGGERALFNLSLRCAIYRLlaegiegdAP 811
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24985991 1086 APFCMLDEVDAPLDDANVGRYARLVKEMSE--SVQFIYITHNKIAMEMADQLMGV 1138
Cdd:PRK02224 812 LPPLILDEPTVFLDSGHVSQLVDLVESMRRlgVEQIVVVSHDDELVGAADDLVRV 866
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
650-959 |
1.53e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 650 LARGQEIERLgQEQLEQ-----EAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGEL---KASLSASRARAEQ 721
Cdd:PRK04863 337 LNLVQTALRQ-QEKIERyqadlEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRAIQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 722 VElrrrrlqeelselEEQRALE--HEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLdRVRQEARQHKDHAHQL 799
Cdd:PRK04863 416 YQ-------------QAVQALEraKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKL-SVAQAAHSQFEQAYQL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 800 AVRLG---SLRAQHDSTRQALERLEQQ---AARLTERQEQLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHm 873
Cdd:PRK04863 482 VRKIAgevSRSEAWDVARELLRRLREQrhlAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQ- 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 874 DEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRR----------KTLQEQL---LADGYDLQGVLATL---- 936
Cdd:PRK04863 561 EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawlaaqdalARLREQSgeeFEDSQDVTEYMQQLlere 640
|
330 340
....*....|....*....|....
gi 24985991 937 -EAEASEQGTEQELEQLEARIQRL 959
Cdd:PRK04863 641 rELTVERDELAARKQALDEEIERL 664
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
654-1134 |
2.21e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 654 QEIERLGQE--QLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRRLQE 731
Cdd:COG4717 109 AELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 732 ELSELEEQRALEHEQLGEARLLLQEALElmaQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQ------------- 798
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQLENELEAAALEERLKEARLLLliaaallallglg 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 799 --------------------LAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQEELRLKLEELLER 858
Cdd:COG4717 266 gsllsliltiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 859 RMSVDEemRLARLHMDEADRELRDAEKRRTQAEQQAQL-----LRGQLEQLRlECQGLDVRRKTLQEQLLADGYDLQGVL 933
Cdd:COG4717 346 IEELQE--LLREAEELEEELQLEELEQEIAALLAEAGVedeeeLRAALEQAE-EYQELKEELEELEEQLEELLGELEELL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 934 ATL----------EAEASEQGTEQELEQLEARIQRLGAI--NLAAIEEYEQQSERKRYLDAQDADLVEALETLeNVIRKI 1001
Cdd:COG4717 423 EALdeeeleeeleELEEELEELEEELEELREELAELEAEleQLEEDGELAELLQELEELKAELRELAEEWAAL-KLALEL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1002 DKETRNRFKDTF-DQINAGLQALFPKVFGGgsAYLELtgedLLDTGVTIMARPPGKKNSTIHLLSGGEKALTALALVFAI 1080
Cdd:COG4717 502 LEEAREEYREERlPPVLERASEYFSRLTDG--RYRLI----RIDEDLSLKVDTEDGRTRPVEELSRGTREQLYLALRLAL 575
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24985991 1081 ---FKLNPAPFcMLDEVDAPLDDANVGRYARLVKEMSESVQFIYITHNKIAMEMADQ 1134
Cdd:COG4717 576 aelLAGEPLPL-ILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVELFQE 631
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
667-924 |
2.75e-07 |
|
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: 55.34 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 667 EAALEQLDQQ-------LQALREQQLDLEEQREQLRRRTQDENRLHGElkASLSASRARAEQVELRRRRLQEELSELEEQ 739
Cdd:COG3096 835 EAELAALRQRrselereLAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQ--ANLLADETLADRLEELREELDAAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 740 RaleheQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQ------EARQHKDH-AHQLAV-RLGSLRAQHD 811
Cdd:COG3096 913 Q-----QHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQqifalsEVVQRRPHfSYEDAVgLLGENSDLNE 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 812 STRQALERLEQQAARLTERQEQLSLNLEEG-----------EAPQEELRLKLEELLERRMSVDEEMR-LARLHMDEADRE 879
Cdd:COG3096 988 KLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrDAKQQTLQELEQELEELGVQADAEAEeRARIRRDELHEE 1067
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 24985991 880 LRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQEQLLA 924
Cdd:COG3096 1068 LSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
654-924 |
2.84e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 654 QEIERLGQEQLEQEAALEQLD-------QQLQALREQQLDL-------------------EEQREQLRRRTQDEN--RLH 705
Cdd:PRK04863 837 AELRQLNRRRVELERALADHEsqeqqqrSQLEQAKEGLSALnrllprlnlladetladrvEEIREQLDEAEEAKRfvQQH 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 706 G----ELKASLSASRARAEQVELRRRRLQEELSELEEQ----RALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDT 777
Cdd:PRK04863 917 GnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAkqqaFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQ 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 778 LRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQqaarlteRQEQLSLNLEEGEAPQeelrlkleelle 857
Cdd:PRK04863 997 AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ-------ELQDLGVPADSGAEER------------ 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24985991 858 rrmsvdeemrlARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQEQLLA 924
Cdd:PRK04863 1058 -----------ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
675-979 |
3.31e-07 |
|
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: 54.96 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 675 QQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSA--------------SRARAEQVELRRRRLQEELSELEEQR 740
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGhlavafapdpeaelAALRQRRSELERELAQHRAQEQQLRQ 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 741 ALEH--EQLGEARLLLQEAlELMAQDTeqreqLMARRDTLRESLDRVRQEAR---QHKDHAHQLAVRLGSLR---AQHDS 812
Cdd:COG3096 865 QLDQlkEQLQLLNKLLPQA-NLLADET-----LADRLEELREELDAAQEAQAfiqQHGKALAQLEPLVAVLQsdpEQFEQ 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 813 TRQALERLEQQAARLTERQEQLSLNLEEGEApqeelrlkleelleRRMSVDEEMRLARLHMDEADRE-LRDAEKRRTQAE 891
Cdd:COG3096 939 LQADYLQAKEQQRRLKQQIFALSEVVQRRPH--------------FSYEDAVGLLGENSDLNEKLRArLEQAEEARREAR 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 892 QQAQLLRGQLEQLRLECQGLDVRRKTLQEQLLADGYDLQ--GVLATLEAEASEQGTEQEL-EQLEARIQRLGAINLA-AI 967
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEelGVQADAEAEERARIRRDELhEELSQNRSRRSQLEKQlTR 1084
|
330
....*....|..
gi 24985991 968 EEYEQQSERKRY 979
Cdd:COG3096 1085 CEAEMDSLQKRL 1096
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1059-1125 |
6.09e-07 |
|
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: 50.32 E-value: 6.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24985991 1059 STIHLLSGGEKALTALALVFAifkLNPaPFCMLDEVDAPLDDANVGRYARLVKEMSES-VQFIYITHN 1125
Cdd:cd00267 76 GYVPQLSGGQRQRVALARALL---LNP-DLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHD 139
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-332 |
6.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1 MRLKCIRLAGFKSFVDpTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIFNGSSGrkpvsqASI 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKS-SVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSG------TEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 81 ELVFDNSETTLV-----GEYAAYAEISIRRKVTRDGQNS------------YYLNGTKCRRRDITDIFLG---------- 133
Cdd:PRK03918 74 ELKFEKNGRKYRivrsfNRGESYLKYLDGSEVLEEGDSSvrewverlipyhVFLNAIYIRQGEIDAILESdesrekvvrq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 134 -TGLGPRSYSIIEQGMISKLIEAKPEELRNFIEEAAGIskyKERRRETENRIRRTQENLARLTDLREELERQLERLHRQA 212
Cdd:PRK03918 154 iLGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENI---EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 213 QAAEKYREYKAQERQLKARLSAlRWRDLDEQVRQRESVIgDQGVSHEALVAEQRNADASIERLRDGHHELSERFNQVQGR 292
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEG-SKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE 308
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 24985991 293 FYSVAGDIARVEQSIQHGQQRLRQLQDDFKEAERTRLETE 332
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-93 |
6.32e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 53.01 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 2 RLKCIRLAGFKSFVDpTTVNFpSNMAAVVGPNGCGKSNIIDAVRWVmGESSAKNLRGE-----SMTDVIFNGSSGRKPvs 76
Cdd:COG4637 1 MITRIRIKNFKSLRD-LELPL-GPLTVLIGANGSGKSNLLDALRFL-SDAARGGLQDAlarrgGLEELLWRGPRTITE-- 75
|
90
....*....|....*..
gi 24985991 77 QASIELVFDNSETTLVG 93
Cdd:COG4637 76 PIRLELEFAEEDERDLR 92
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
659-833 |
9.47e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 659 LGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRRLQEELSELE- 737
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPn 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 738 --EQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQhkdhAHQLAVRLGSLRAQHDSTRQ 815
Cdd:COG3206 290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVARE 365
|
170 180
....*....|....*....|
gi 24985991 816 ALERLEQ--QAARLTERQEQ 833
Cdd:COG3206 366 LYESLLQrlEEARLAEALTV 385
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
602-961 |
1.03e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 53.10 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 602 VRPVEDLAQALEQRGSLGEGQSLVSR---------DGYWVGRHFLRVRRGGEAEGGVLARGQEIERLGQEQLEQEAALEQ 672
Cdd:COG3903 545 LRLAAALAPFWFLRGLLREGRRWLERalaaageaaAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALL 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 673 LDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRRLQEELSELEEQRALEHEQLGEARL 752
Cdd:COG3903 625 LLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALA 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 753 LLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQE 832
Cdd:COG3903 705 AAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAA 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 833 QLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLD 912
Cdd:COG3903 785 ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAA 864
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24985991 913 VRRKTLQEQLLADGYDLQGVLATLEAEASEQGTEQELEQLEARIQRLGA 961
Cdd:COG3903 865 AAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAA 913
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
660-998 |
2.40e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 660 GQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQD--------ENRLH--GELKASLSASRARAEQVElrRRRL 729
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEadevleehEERREelETLEAEIEDLRETIAETE--RERE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 730 QEELSELEEQRALehEQLGEARLLLQEALELMAQDTE----QREQLMARRDTLRESLDRVRQEARQHKDHAhqlavrlgs 805
Cdd:PRK02224 276 ELAEEVRDLRERL--EELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEA--------- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 806 lraqhDSTRQALERLEQQAARLTERQEQLSLNLEEGEApqeelrlKLEELLERRMSVDEEMRLARLHMDEADRELRDAEK 885
Cdd:PRK02224 345 -----ESLREDADDLEERAEELREEAAELESELEEARE-------AVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 886 RRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQEQLLAD-----GYDLQG---VLATLEAEASEQGTEQELEQLEARIQ 957
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLEAGkcpecGQPVEGsphVETIEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24985991 958 RLGAINLAAIEEYEQQSERKRYLDAQDaDLVEALETLENVI 998
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEERRE-DLEELIAERRETI 532
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1064-1147 |
2.58e-06 |
|
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: 49.52 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1064 LSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANvgryaR------LVKEMSESV--QFIYITHNKIAMEMADQL 1135
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN-----RkistdlLVKEAKKQPgrQFIFITPQDISGLASSDD 184
|
90
....*....|..
gi 24985991 1136 MGVTMHEPGCSR 1147
Cdd:cd03276 185 VKVFRMKDPRGP 196
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
635-959 |
2.67e-06 |
|
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: 51.88 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 635 HFLRVRRGGEAEGGVLARGQEIERLGQEQLEQEAALEQLDQQLQALREQqldleeqreqlRRRTQDEnrlHGELKASLsA 714
Cdd:COG3096 335 HLNLVQTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEAR-----------LEAAEEE---VDSLKSQL-A 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 715 SRARAEQVELRRrrlqeELSELEEQRALE--HEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDrVRQEARQH 792
Cdd:COG3096 400 DYQQALDVQQTR-----AIQYQQAVQALEkaRALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLS-VADAARRQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 793 KDHAHQLAVRL--GSLRAQ-HDSTRQALER---LEQQAARLT--ERQ----EQLSLNLEEGEAPQEELRLKLEELLERRM 860
Cdd:COG3096 474 FEKAYELVCKIagEVERSQaWQTARELLRRyrsQQALAQRLQqlRAQlaelEQRLRQQQNAERLLEEFCQRIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 861 SVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLR---LECQGLDVRRKTLQEQLLADGYDLQGVLATL- 936
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAaraPAWLAAQDALERLREQSGEALADSQEVTAAMq 633
|
330 340 350
....*....|....*....|....*....|
gi 24985991 937 -------EAEASEQGTEQELEQLEARIQRL 959
Cdd:COG3096 634 qllererEATVERDELAARKQALESQIERL 663
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-528 |
3.42e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1 MRLKCIRLAGFKSFVDpTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNlrgESMTDVIFNGSSgrkpvsQASI 80
Cdd:PRK02224 1 MRFDRVRLENFKCYAD-ADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALD---DTLDDVITIGAE------EAEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 81 ELVFdnseTTLVGEY-------AAYAEISIRRKVTRDGQNSYylNGTKCRRRDITDIFLGTGLGPRSYSIIEQGMISKLI 153
Cdd:PRK02224 71 ELWF----EHAGGEYhierrvrLSGDRATTAKCVLETPEGTI--DGARDVREEVTELLRMDAEAFVNCAYVRQGEVNKLI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 154 EAKPEELRNFIEEAAGISK---YKER-----------RRETENRIRRTQENLA---------RLTDLRE---ELERQLER 207
Cdd:PRK02224 145 NATPSDRQDMIDDLLQLGKleeYRERasdarlgvervLSDQRGSLDQLKAQIEekeekdlheRLNGLESelaELDEEIER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 208 LHRQAQAA-----------EKYREYKAQERQLKARLSALRWR---------DLDEQVRQRESVIGDQGVSHEALVAEQRN 267
Cdd:PRK02224 225 YEEQREQAretrdeadevlEEHEERREELETLEAEIEDLRETiaeterereELAEEVRDLRERLEELEEERDDLLAEAGL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 268 ADASIERLRDGHHELSERFNQVQGRFYSVAGDIARVEQSIQHGQQRLRQLQDDFKEAERTRLETESHLGHDRTLLATLGE 347
Cdd:PRK02224 305 DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 348 ELAMLEPEQEMTLAAAEEAAAALEEAELGMHGWQEQWDSFNSRSAEPRRQAEVQQARL----------------QQLETS 411
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaealleagkcpecgQPVEGS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 412 -----LERQAERQRKLVEEREQLGSDPQD-AAMLELAEQLASSEMLLEELQLCEEQVIERLESAREQLQQATQAqqqaqg 485
Cdd:PRK02224 465 phvetIEEDRERVEELEAELEDLEEEVEEvEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER------ 538
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 24985991 486 dLQRLGGRLASLEALQQAALEpgagAAQWLHGQGLEQQPRLAE 528
Cdd:PRK02224 539 -AEELRERAAELEAEAEEKRE----AAAEAEEEAEEAREEVAE 576
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
657-835 |
6.34e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 657 ERLGQEQLEQEAALEQLDQQLQALREQ----------------QLDLEEQREQLRRRTQDENRLHGELKASLSASRARAE 720
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEleeaeaaleefrqkngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 721 QVELRRRRLQEELSELEEQRALE--HEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQhkdhahQ 798
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA------S 317
|
170 180 190
....*....|....*....|....*....|....*..
gi 24985991 799 LAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQLS 835
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
489-883 |
7.63e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 50.40 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 489 RLGGRLASLEALQQAALEPGAGAAQWLHgQGLEQQPRLAEGLRVEPGWELAVETVLGADLQAVLVDDfnDLDFAGLEQGE 568
Cdd:COG3903 542 ELALRLAAALAPFWFLRGLLREGRRWLE-RALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAA--AAAAAAAAAAA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 569 LRLLLAVGAGATLPGSLLEKVEGRIDLAPWLGQVRPVEDLAQALEQRGSLGEGQSLVSRDGYWVGRHFLRVRRGGEAEGG 648
Cdd:COG3903 619 AAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAA 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 649 VLARGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRR 728
Cdd:COG3903 699 AAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLA 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 729 LQEELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRA 808
Cdd:COG3903 779 LAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAAL 858
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24985991 809 QHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHMDEADRELRDA 883
Cdd:COG3903 859 AAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
6-47 |
1.24e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 48.89 E-value: 1.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 24985991 6 IRLAGFKSFVDPTTVNF------PSNMAAVVGPNGCGKSNIIDAVRWV 47
Cdd:COG1106 5 FSIENFRSFKDELTLSMvasglrLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
652-1023 |
1.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 652 RGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRrrtqdenrlhgelkaslsasRARAEQVELRRRRLQE 731
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE--------------------ELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 732 ELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKD--------HAHQLAVRL 803
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslateeELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 804 GSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMR---------------- 867
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGgsllsliltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 868 ---LARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRkTLQEQLLADGYDLQGVLATLEAEASEQG 944
Cdd:COG4717 282 vlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP-DLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 945 TEQELEQLEARIQRL-GAINLAAIEEYEQQSERKRyldaQDADLVEALETLENVIRKIDKETRNRFKD-TFDQINAGLQA 1022
Cdd:COG4717 361 EELQLEELEQEIAALlAEAGVEDEEELRAALEQAE----EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEE 436
|
.
gi 24985991 1023 L 1023
Cdd:COG4717 437 L 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
654-834 |
1.38e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 654 QEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRRLQEEL 733
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 734 SELEEQRALEHEQLGEARLLLQealELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDST 813
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQYLK---YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180
....*....|....*....|.
gi 24985991 814 RQALERLEQQAARLTERQEQL 834
Cdd:COG4942 198 QKLLARLEKELAELAAELAEL 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
146-332 |
1.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 146 QGMISKLIEAKPEELRNFIEEAAgisKYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKYREYKAQE 225
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAE---EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 226 RQLKArlSALRWRDLDEQVRQRESVIGDQgvshEALVAEQRNADASIERLRDGH-HELSERFNQVQGRFYSVAGDIARVE 304
Cdd:COG4717 139 AELAE--LPERLEELEERLEELRELEEEL----EELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELE 212
|
170 180
....*....|....*....|....*...
gi 24985991 305 QSIQHGQQRLRQLQDDFKEAERTRLETE 332
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAA 240
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
388-790 |
2.42e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 48.86 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 388 NSRSAEPRRQAEVQQARLQQLETSLERQAERQRKLVEEREQLGSDPQDAAMLELAEQLASSEMLLEELQLCEEQVIERLE 467
Cdd:COG3903 527 NLRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 468 SAREQLQQATQAQQQAQGDLQRLGGRLASLEALQQAALEPGAGAAQWLHGQGLEQQPRLAEGLRVEPGWELAVETVLGAD 547
Cdd:COG3903 607 AAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAA 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 548 LQAVLVDDFNDLDFAGLEQGELRLLLAVGAGATLPGSLLEKVEGRIDLAPWLGQVRPVEDLAQALEQRGSLGEGQSLVSR 627
Cdd:COG3903 687 LAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAA 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 628 DGYWVGRHFLRVRRGGEAEGGVLARGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGE 707
Cdd:COG3903 767 AAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAA 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 708 LKASLSASRARAEQVELRRRRLQEELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQ 787
Cdd:COG3903 847 AAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAA 926
|
...
gi 24985991 788 EAR 790
Cdd:COG3903 927 AAA 929
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
768-1023 |
2.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 768 REQLMARRDTLrESLDRVRQEARQHKDhAHQLAVRLgslRAQhdstRQALERLEQQAARLTERQEQLSLnLEEGEAPQEE 847
Cdd:COG4913 214 REYMLEEPDTF-EAADALVEHFDDLER-AHEALEDA---REQ----IELLEPIRELAERYAAARERLAE-LEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 848 LRLKleellerrmsvdEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKtlqEQLLADgy 927
Cdd:COG4913 284 WFAQ------------RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL---EQLERE-- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 928 dlqgvLATLEAEASEQgtEQELEQLEARIQRLGAINLAAIEEYEQQSERkryLDAQDADLVEALETLENVIRKIDKEtRN 1007
Cdd:COG4913 347 -----IERLERELEER--ERRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAA-LR 415
|
250
....*....|....*.
gi 24985991 1008 RFKDTFDQINAGLQAL 1023
Cdd:COG4913 416 DLRRELRELEAEIASL 431
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-49 |
2.58e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 47.30 E-value: 2.58e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24985991 1 MRLKCIRLAGFKSFVDpTTVNF--PSNMAAVVGPNGCGKSNIIDAVRWVMG 49
Cdd:COG3950 1 MRIKSLTIENFRGFED-LEIDFdnPPRLTVLVGENGSGKTTLLEAIALALS 50
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
765-1005 |
3.07e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 765 TEQREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAP 844
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 845 QEELRLKLEELLERRMSVDEEMRLARLHMDEadrELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQEQlla 924
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPE---DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 925 dgydlQGVLATLEAEASEQgtEQELEQLEARIQRLGAINLAAIEEYEQQSERKRyldAQDADLVEALETLENVIRKIDKE 1004
Cdd:COG4942 173 -----RAELEALLAELEEE--RAALEALKAERQKLLARLEKELAELAAELAELQ---QEAEELEALIARLEAEAAAAAER 242
|
.
gi 24985991 1005 T 1005
Cdd:COG4942 243 T 243
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
639-928 |
3.26e-05 |
|
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: 48.41 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 639 VRRGGEAEGGVLARGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRAR 718
Cdd:COG3096 419 VQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTAR 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 719 A------EQVELRRRRLQEELSELEEQRALEHEQlgEARLLLQEALELMAQD-------TEQREQLMARRDTLRESLDRV 785
Cdd:COG3096 499 EllrryrSQQALAQRLQQLRAQLAELEQRLRQQQ--NAERLLEEFCQRIGQQldaaeelEELLAELEAQLEELEEQAAEA 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 786 RQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQaarlterQEQLSLNLEEGEAPQEelrlkleellerrmsvdee 865
Cdd:COG3096 577 VEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL-------REQSGEALADSQEVTA------------------- 630
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24985991 866 mrlarlHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQEQ----LLADGYD 928
Cdd:COG3096 631 ------AMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERlggvLLSEIYD 691
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1064-1147 |
3.91e-05 |
|
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: 46.06 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1064 LSGGEKALTALALVFAIFKL--NPAPFCMLDEVDAPLDDANV-GRYARLVKEMSESV--QFIYITHNKIAMEMADQLMGV 1138
Cdd:cd03240 116 CSGGEKVLASLIIRLALAETfgSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKnfQLIVITHDEELVDAADHIYRV 195
|
....*....
gi 24985991 1139 TMHEPGCSR 1147
Cdd:cd03240 196 EKDGRQKSR 204
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
26-248 |
6.15e-05 |
|
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: 46.23 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 26 MAAVVGPNGCGKSNIIDAVRWV-----MGESSAKNLRGESMTDVIFNGSSGRKPVSQASIEL-VFDNSETTL-----VGE 94
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLadfdaLVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEIsEFLEDGVRYrygldLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 95 YAAYAEISIRRKVTRDGQNSYYLNGTK-CRRRDITDIFLGTGLGPRSYSIIEQGMISKLIEAKPEELRNFIEEAAGISKY 173
Cdd:pfam13304 81 EDVEEKLSSKPTLLEKRLLLREDSEERePKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24985991 174 KERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKY-REYKAQERQLKARLSALRWRDLDEQVRQRE 248
Cdd:pfam13304 161 LLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGiEKSLLVDDRLRERGLILLENGGGGELPAFE 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-350 |
6.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 167 AAGISKYKERRRE--TENRIRR-------TQENLARLTDLREELERQLERLHRQAQAAEKYREYKAQERQLKARLSALRW 237
Cdd:COG4913 579 RAGQVKGNGTRHEkdDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 238 RDLDeqVRQRESVIGDQGVSHEALVAEQ---RNADASIERLRDGHHELSERFNQVQGRFYSVAGDIARVEQSIQHGQQRL 314
Cdd:COG4913 659 DEID--VASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190
....*....|....*....|....*....|....*.
gi 24985991 315 RQLQDDFKEAERTRLETESHLGHDRTLLATLGEELA 350
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-120 |
6.66e-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: 46.04 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFkSFVDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGessaknlrGESMTDVIfngssgRKPVSQASIEL 82
Cdd:cd03241 1 LLELSIKNF-ALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLG--------GRASADLI------RSGAEKAVVEG 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24985991 83 VFDNSETTLVGEYAAYA------EISIRRKVTRDGQNSYYLNGT 120
Cdd:cd03241 66 VFDISDEEEAKALLLELgiedddDLIIRREISRKGRSRYFINGQ 109
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
805-994 |
6.83e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 805 SLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEgeapqeelrlklEELLERRMSVDEEMRLARLHMDEADRELRDAE 884
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEE------------FRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 885 KRRTQAEQQAQLLRGQLEQLRLECQglDVRRKTLQEQLLADGYDLQGVLATLEAEASE-----QGTEQELEQLEARIQRL 959
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALP--ELLQSPVIQQLRAQLAELEAELAELSARYTPnhpdvIALRAQIAALRAQLQQE 310
|
170 180 190
....*....|....*....|....*....|....*.
gi 24985991 960 GAINLAAIE-EYEQQSERKRYLDAQDADLVEALETL 994
Cdd:COG3206 311 AQRILASLEaELEALQAREASLQAQLAQLEARLAEL 346
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
674-1004 |
7.33e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 674 DQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARA------EQVELRRRRLQEELSELEEQRALEH--- 744
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeAELRQLNRRRVELERALADHESQEQqqr 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 745 EQLGEARLLLQEALELMAQ-DTEQREQLMARRDTLRESLDRVRQEAR---QHKDHAHQLAVRLGSLR----------AQH 810
Cdd:PRK04863 865 SQLEQAKEGLSALNRLLPRlNLLADETLADRVEEIREQLDEAEEAKRfvqQHGNALAQLEPIVSVLQsdpeqfeqlkQDY 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 811 DSTRQALERLEQQAARLTE-RQEQLSLNLEEgeAPQEELRLKLEELlerrmSVDEEMRLARLHMDEADRELRDAEKRRTQ 889
Cdd:PRK04863 945 QQAQQTQRDAKQQAFALTEvVQRRAHFSYED--AAEMLAKNSDLNE-----KLRQRLEQAEQERTRAREQLRQAQAQLAQ 1017
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 890 AEQQAQLLRGQLeqlrlecqglDVRRKTLQEqlLADGYDLQGVLATLEAEASEQGTEQELEQleariqrlgainlaaieE 969
Cdd:PRK04863 1018 YNQVLASLKSSY----------DAKRQMLQE--LKQELQDLGVPADSGAEERARARRDELHA-----------------R 1068
|
330 340 350
....*....|....*....|....*....|....*
gi 24985991 970 YEQQSERKRYLDAQDADLVEALETLENVIRKIDKE 1004
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
650-896 |
7.33e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 650 LARGQEIERLgqeQLEQEAALEQLDQQLQALREQQLdLEEQREqlrRRTQDENRLHGELKASlsasRARAEQVELRRrrl 729
Cdd:pfam17380 374 ISRMRELERL---QMERQQKNERVRQELEAARKVKI-LEEERQ---RKIQQQKVEMEQIRAE----QEEARQREVRR--- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 730 qeelseLEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDtlRESLDRVRQEARQHKDHAHQLAVRLGSLRAQ 809
Cdd:pfam17380 440 ------LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--KEKRDRKRAEEQRRKILEKELEERKQAMIEE 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 810 HDSTRQALERLEQQAARLTERQEQLSlnLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHMD-EADRELRDAEKRRT 888
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERErEMMRQIVESEKARA 589
|
....*...
gi 24985991 889 QAEQQAQL 896
Cdd:pfam17380 590 EYEATTPI 597
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
662-1010 |
9.13e-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: 46.76 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 662 EQLEQ-EAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVE----------LRRRRLQ 730
Cdd:pfam12128 464 LQLENfDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELElqlfpqagtlLHFLRKE 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 731 EELSELEEQRALEHEQLGEARL--------------LLQEALELMAQDTEQ----REQLMARRDTLRESLDRVRQEARQH 792
Cdd:pfam12128 544 APDWEQSIGKVISPELLHRTDLdpevwdgsvggelnLYGVKLDLKRIDVPEwaasEEELRERLDKAEEALQSAREKQAAA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 793 KDHAHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEG-EAPQEELRLKLEELLERRMSVDEEMRLARL 871
Cdd:pfam12128 624 EEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAQLKQLDKKHQAWLE 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 872 HMDEADRELrdaekrRTQAEQQAQLLRGQLE-QLRLECQGLDVRRKTLQEQLLADGYDLQGVLATLEA-EASEQGTEQEL 949
Cdd:pfam12128 704 EQKEQKREA------RTEKQAYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVdPDVIAKLKREI 777
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24985991 950 EQLEARIQRLgAINLAAIEEY-----EQQSERKRYLDAQDADLVEALETLENVIRKIDKETRNRFK 1010
Cdd:pfam12128 778 RTLERKIERI-AVRRQEVLRYfdwyqETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRA 842
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
611-995 |
1.20e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.55 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 611 ALEQRGSLGEGQSLVSRdgywVGRHFLRVRRGGEAEGGVLARGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQ 690
Cdd:COG3903 477 AAERLAEAGERAAARRR----HADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 691 REQLRRRTQDENRLHgeLKASLSASRARAEQVELRRRRLQEELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQ 770
Cdd:COG3903 553 PFWFLRGLLREGRRW--LERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALA 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 771 LMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQEELRL 850
Cdd:COG3903 631 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAA 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 851 KLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQEQLLADGYDLQ 930
Cdd:COG3903 711 LAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAA 790
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24985991 931 GVLATLEAEASEQGTEQELEQLEARIQRLGAINLAAIEEYEQQSERKRYLDAQDADLVEALETLE 995
Cdd:COG3903 791 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALA 855
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
594-995 |
2.35e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 45.62 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 594 DLAPWLGQVRPVEDLAQALEQRGSLGEGQSLVSRDGYWVGRH-----FLRVRRGGEAEGGVLARGQEIERLGQEQLEQEA 668
Cdd:COG3899 805 DYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLrealeLLREALEAGLETGDAALALLALAAAAAAAAAAA 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 669 ALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRRLQEELSELEEQRALEHEQLG 748
Cdd:COG3899 885 ALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAA 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 749 EARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQAARLT 828
Cdd:COG3899 965 AAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALA 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 829 ERQEQLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLEC 908
Cdd:COG3899 1045 LLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALA 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 909 QGLDVRRKTLQEQLLADGYDLQGVLATLEAEASEQGTEQELEQLEARIQRLGAINLAAIEEYEQQSERKRYLDAQDADLV 988
Cdd:COG3899 1125 LAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAA 1204
|
....*..
gi 24985991 989 EALETLE 995
Cdd:COG3899 1205 RLAALLA 1211
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
655-1008 |
2.65e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 655 EIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLrrrtQDENRLHGELKASLSASRARAEQVELRRRRLQEELS 734
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIY----AEQERMAMERERELERIRQEERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 735 ELEEQRALEHEQlgearlllqeaLELMAQDTEQREQLMARRDTlresldRVRQEARQHKdhAHQLAVRLGSLRAQHDSTR 814
Cdd:pfam17380 373 EISRMRELERLQ-----------MERQQKNERVRQELEAARKV------KILEEERQRK--IQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 815 Q-ALERLEQQAARLTERqeqlsLNLEEGEAPQeelrlkleellerrmsvdeemRLARLHMDEADRELRDAEKRRTQAEQQ 893
Cdd:pfam17380 434 QrEVRRLEEERAREMER-----VRLEEQERQQ---------------------QVERLRQQEEERKRKKLELEKEKRDRK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 894 aqllrgQLEQLrlecqgldvRRKTLQEQLLADGYdlqgvlATLEAEASEQGTEQELEQLEARIQRLGAINLAAIEEYEQQ 973
Cdd:pfam17380 488 ------RAEEQ---------RRKILEKELEERKQ------AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ 546
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24985991 974 --SERKRYLD-----AQDADLVEALETLENVIRKIDKETRNR 1008
Cdd:pfam17380 547 emEERRRIQEqmrkaTEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
175-357 |
2.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 175 ERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKYREYKAQER--QLKARLSALRwRDLDEQVRQRESV-- 250
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleQLEREIERLE-RELEERERRRARLea 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 251 -IGDQGV----SHEALVAEQRNADASIERLRDGHHELSERFNQVQGRFYSVAGDIARVEQSIqhgqQRLRQLQDDF-KEA 324
Cdd:COG4913 367 lLAALGLplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI----ASLERRKSNIpARL 442
|
170 180 190
....*....|....*....|....*....|...
gi 24985991 325 ERTRLETESHLGHDRTLLATLGEELAMLEPEQE 357
Cdd:COG4913 443 LALRDALAEALGLDEAELPFVGELIEVRPEEER 475
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-56 |
3.22e-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: 44.51 E-value: 3.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24985991 1 MRLKCIRLAGFKSFVDpTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNL 56
Cdd:pfam13175 1 MKIKSIIIKNFRCLKD-TEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKFFE 55
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
637-839 |
4.01e-04 |
|
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: 43.98 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 637 LRVRRGGEAEGGVLARGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRlhgELKASLSASR 716
Cdd:pfam09787 30 LKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQ---ELEEQLATER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 717 ARAEQVELRRRRLQEELseleeqRALEhEQLGEARLLLQEALELMAQDTE-QREQLMARRDTlRESLDRVRQEARQHKDH 795
Cdd:pfam09787 107 SARREAEAELERLQEEL------RYLE-EELRRSKATLQSRIKDREAEIEkLRNQLTSKSQS-SSSQSELENRLHQLTET 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24985991 796 AHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQE-QLSLNLE 839
Cdd:pfam09787 179 LIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSnGTSINME 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
167-332 |
4.79e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 167 AAGISKYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQ-AQAAEKYREYKAQERQLKARLSAL--RWRDLDEQ 243
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiAALARRIRALEQELAALEAELAELekEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 244 VRQRESVIGDQ--------GVSHEALVAEQRNADASIERLRDGHHELSERFNQVQgRFYSVAGDIARVEQSIQHGQQRLR 315
Cdd:COG4942 99 LEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAELE 177
|
170
....*....|....*..
gi 24985991 316 QLQDDfKEAERTRLETE 332
Cdd:COG4942 178 ALLAE-LEEERAALEAL 193
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-88 |
5.98e-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: 42.64 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1 MRLKCIRLAGFKSFVDPTTVNF----PSNMAAVVGPNGCGKSNIIDAVRWVM-GESSAKnlRGESMTDVIFNgsSGRKPv 75
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYALyGKTPRY--GRQENLRSVFA--PGEDT- 75
|
90
....*....|...
gi 24985991 76 sqASIELVFDNSE 88
Cdd:cd03279 76 --AEVSFTFQLGG 86
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
687-998 |
6.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 687 LEEQREQLRR-RTQDENRLHGELKASLSASRARAEQVElrrrrlqEELSELEEQRALEHEQLGEARLLL------QEALE 759
Cdd:PRK02224 182 LSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAELD-------EEIERYEEQREQARETRDEADEVLeeheerREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 760 LMAQDTEQREQLMARRDTLRESLdrvRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLE 839
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREEL---AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 840 EGEAPQEELRLKLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQ 919
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 920 ---EQLLADGYDLQGVLATLEAE-ASEQGTEQELEQL-------EARIQRLGAINLAAIEEYEQQSERkryLDAQDADLV 988
Cdd:PRK02224 412 dflEELREERDELREREAELEATlRTARERVEEAEALleagkcpECGQPVEGSPHVETIEEDRERVEE---LEAELEDLE 488
|
330
....*....|
gi 24985991 989 EALETLENVI 998
Cdd:PRK02224 489 EEVEEVEERL 498
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
754-1027 |
6.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 754 LQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQL--AVRLGSLRAQHDSTRQALERLEQQAARLTERQ 831
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 832 EQLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLArlhMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGL 911
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 912 DVRRKTLQ-EQLLADGYDLQGVLATLeaeASEQGTEQELEQLEARIQRLGAINLAAIEEYEQQSERKRYLDAQDADLVEA 990
Cdd:COG4717 233 ENELEAAAlEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270
....*....|....*....|....*....|....*..
gi 24985991 991 LETLENVIRKIDKETRNRFKDTFDQINAGLQALFPKV 1027
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
873-1133 |
7.15e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 873 MDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRLECQGLDVRRKTLQE---QLLADGYDLQGVLATLE-AEASEQGTEQE 948
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDdAKANRARLEST 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 949 LEQLEARIQRLGAinlaAIEEYEQQSERKRYLDAQDADLVEALETL-----ENVIRK-----IDKETRN---RFKDTFDQ 1015
Cdd:PRK01156 704 IEILRTRINELSD----RINDINETLESMKKIKKAIGDLKRLREAFdksgvPAMIRKsasqaMTSLTRKylfEFNLDFDD 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1016 INAGlQALFPKVFGGGSAyleltgedlldtgvtimarppgkknSTIHLLSGGEKALTALALVFAI--FKLNPAPFCMLDE 1093
Cdd:PRK01156 780 IDVD-QDFNITVSRGGMV-------------------------EGIDSLSGGEKTAVAFALRVAVaqFLNNDKSLLIMDE 833
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 24985991 1094 VDAPLDD------ANVGRYArlVKEMSESVQFIYITHNKIAMEMAD 1133
Cdd:PRK01156 834 PTAFLDEdrrtnlKDIIEYS--LKDSSDIPQVIMISHHRELLSVAD 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
666-926 |
7.20e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 666 QEAALEQLDQQLQALREQqldLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVelrrrrlqeelseleeqRALEHE 745
Cdd:COG4942 18 QADAAAEAEAELEQLQQE---IAELEKELAALKKEEKALLKQLAALERRIAALARRI-----------------RALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 746 QlgeaRLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQ-------HKDHAHQLAVRLGSLRAQHDSTRQALE 818
Cdd:COG4942 78 L----AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 819 RLEQQAARLTERQEQLSLNLEEGEApqeelrlkleelleRRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLR 898
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEA--------------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260
....*....|....*....|....*...
gi 24985991 899 GQLEQLRLECQGLDVRRKTLQEQLLADG 926
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
972-1125 |
1.01e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 972 QQSERKRYLDAQDADLVEALETLenviRKIDKETRNRFKDTFDQINAGLQALFPKVFGGGSAYLELTGEDLLDTgvtima 1051
Cdd:COG4637 184 QPAGRTPVLAPDGSNLAAVLATL----RETHPERFERILEALRDAFPGFEDIEVEPDEDGRVLLEFREKGLDRP------ 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24985991 1052 rppgkknSTIHLLSGGekALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMSESVQFIYITHN 1125
Cdd:COG4637 254 -------FPARELSDG--TLRFLALLAALLSPRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHS 318
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-217 |
1.32e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1 MRLKCIRLAGFKSFVDpTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSaknlRGESMTDVIfngssgRKPVSQASI 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDD-SEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDK----RTEKIEDMI------KKGKNNLEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 81 ELVFDNSETTLVgeyaayaeisIRRKVTRDGQNS-----YYLNGTKCRR--RDITDIFLGTGLGP-----RSYSIIEQGM 148
Cdd:PRK01156 70 ELEFRIGGHVYQ----------IRRSIERRGKGSrreayIKKDGSIIAEgfDDTTKYIEKNILGIskdvfLNSIFVGQGE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24985991 149 ISKLIEAKPEELRNFIEEAAGISKYKERRRETENRIRRTQENLARLTDLREELER---QLERLHRQAQAAEK 217
Cdd:PRK01156 140 MDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSsnlELENIKKQIADDEK 211
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
655-1023 |
1.47e-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: 43.02 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 655 EIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRR----TQDENRLHGELKASLSASRArAEQVELRRrrlq 730
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAResdlEQDYQAASDHLNLVQTALRQ-QEKIERYQ---- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 731 eelseleeqralehEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQearqhkdhahQLAVRLGSLRAQH 810
Cdd:COG3096 354 --------------EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKS----------QLADYQQALDVQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 811 DST---RQALERLEqQAARLTERQEQLSLNLEEGEA---PQEELRLKLEELLERRMSV--------DEEMRLARLHMDEA 876
Cdd:COG3096 410 TRAiqyQQAVQALE-KARALCGLPDLTPENAEDYLAafrAKEQQATEEVLELEQKLSVadaarrqfEKAYELVCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 877 DRE---------LRDAEKRRTQAEQQAQlLRGQLEQL-RLECQGLDVRRktLQEQL-------LADGYDLQGVLATLEA- 938
Cdd:COG3096 489 ERSqawqtarelLRRYRSQQALAQRLQQ-LRAQLAELeQRLRQQQNAER--LLEEFcqrigqqLDAAEELEELLAELEAq 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 939 ---------EASEQ--GTEQELEQLEARIQRLGAINLAAIEEYEQQSERKRYLDAQDADLVEALETLENVIRKIDKETRN 1007
Cdd:COG3096 566 leeleeqaaEAVEQrsELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVE 645
|
410
....*....|....*.
gi 24985991 1008 RfkdtfDQINAGLQAL 1023
Cdd:COG3096 646 R-----DELAARKQAL 656
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-126 |
1.77e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 41.51 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 3 LKCIRLAGFKSFvDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVmgeSSAKNLRGESMTDVIFNGssgrKPVSQASIEL 82
Cdd:cd03242 1 LKSLELRNFRNY-AELELEFEPGVTVLVGENAQGKTNLLEAISLL---ATGKSHRTSRDKELIRWG----AEEAKISAVL 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24985991 83 VFDNSETTLvgeyaayaEISIRRKVTRDGQnsyyLNGTKCRRRD 126
Cdd:cd03242 73 ERQGGELAL--------ELTIRSGGGRKAR----LNGIKVRRLS 104
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
654-827 |
2.03e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 654 QEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQdenrlhgELKAslSASRARAEQVELRRRRlqeel 733
Cdd:PRK04863 551 DDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ-------RLAA--RAPAWLAAQDALARLR----- 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 734 seleeqralehEQLGearlllqEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSlraqhdst 813
Cdd:PRK04863 617 -----------EQSG-------EEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGS-------- 670
|
170
....*....|....
gi 24985991 814 rqALERLEQQAARL 827
Cdd:PRK04863 671 --EDPRLNALAERF 682
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
659-803 |
2.77e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 659 LGQEQLEQEAALEQLDQQLQALrEQQLDLEEQR-EQLRRRTqdenrlhGELKASLSASRARAEQVELRRRRLQEELSELE 737
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAEL-ADLLSLERQGnQDLQDSV-------ANLRASLSAAEAERSRLQALLAELAGAGAAAE 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 738 EQRALEHEQLGEARLLLQEAL---ELMAQDTEQ-REQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRL 803
Cdd:PRK09039 116 GRAGELAQELDSEKQVSARALaqvELLNQQIAAlRRQLAALEAALDASEKRDRESQAKIADLGRRLNVAL 185
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
652-907 |
2.82e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 652 RGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGEL----KASLSASRARA-EQVELRR 726
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERirqeEIAMEISRMRElERLQMER 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 727 R----RLQEELSELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMARRDTLRE-SLDRVRQEARQHKdhaHQLAv 801
Cdd:pfam17380 388 QqkneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERArEMERVRLEEQERQ---QQVE- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 802 RLGSLRAQHDSTRQALERlEQQAARLTERQEQLSLNLEEGEAPQEELRLKLEELLerrmsVDEEMRLARLHMDEADRELR 881
Cdd:pfam17380 464 RLRQQEEERKRKKLELEK-EKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL-----LEKEMEERQKAIYEEERRRE 537
|
250 260 270
....*....|....*....|....*....|..
gi 24985991 882 DAEKRRTQAEQ------QAQLLRGQLEQLRLE 907
Cdd:pfam17380 538 AEEERRKQQEMeerrriQEQMRKATEERSRLE 569
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
655-970 |
2.85e-03 |
|
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: 41.65 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 655 EIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASlsASRARAEQVELRRRRLQEELS 734
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL--VRRLQRRVLLLTKERDGYRAI 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 735 ELEEQRALEHEQLGEARLLLQEALELMAQDTEQREQLMarrdtlRESLDRVRQEARQHKDHAHQLAVRLGSLRAQH---- 810
Cdd:pfam05557 362 LESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEM------EAQLSVAEEELGGYKQQAQTLERELQALRQQEslad 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 811 --------DSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQeelrlkleellerrmsvDEEMRLAR-LHMdeadRELR 881
Cdd:pfam05557 436 psyskeevDSLRRKLETLELERQRLREQKNELEMELERRCLQG-----------------DYDPKKTKvLHL----SMNP 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 882 DAEKRRTQAEQqaqllrgqLEQLRLECQGLDVRRKTLQEQLladgyDLQGVLATLEAEASEQGTEQ---ELEQLEARIQR 958
Cdd:pfam05557 495 AAEAYQQRKNQ--------LEKLQAEIERLKRLLKKLEDDL-----EQVLRLPETTSTMNFKEVLDlrkELESAELKNQR 561
|
330
....*....|..
gi 24985991 959 LGAINLAAIEEY 970
Cdd:pfam05557 562 LKEVFQAKIQEF 573
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
172-439 |
3.04e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 172 KYKERRRETEnRIRRtQENLARLTDLREELERQLERlhrqAQAAEKYREykaqerqlkaRLSALRWRDLDEQVRQREsvI 251
Cdd:pfam17380 354 RQEERKRELE-RIRQ-EEIAMEISRMRELERLQMER----QQKNERVRQ----------ELEAARKVKILEEERQRK--I 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 252 GDQGVSHEALVAEQRNAdasierlrdghhelseRFNQVQGRFYSVAGDIARVEQSIQHGQQRLRQLQDDFKEAERTRLET 331
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEA----------------RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 332 ESHLGHDRtllatLGEELAMLEPEQEMTLAAAEEAAAALEEAELgmhgwQEQWDSFNSRSAEPRRQAEVQQARLQQLETS 411
Cdd:pfam17380 480 EKEKRDRK-----RAEEQRRKILEKELEERKQAMIEEERKRKLL-----EKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
250 260
....*....|....*....|....*....
gi 24985991 412 LERQAERQ-RKLVEEREQLGSDPQDAAML 439
Cdd:pfam17380 550 ERRRIQEQmRKATEERSRLEAMEREREMM 578
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-512 |
3.09e-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: 41.29 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 260 ALVAEQRNADASIERLRDGHHELSERFNQVQGRFYSVAGDIARVEQSIQHGQQRLRQLQDDFKEAERTRLETESHLGHDR 339
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 340 TLLATLGEELAMLEPEQEMTLAAAEEAAAALeeaelgmhgwQEQWDSFNSRSAEPRRQAEVQQARLQQLETSLERQAERQ 419
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLS----------PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 420 RKLVEEREQLgsdpqDAAMLELAEQLASSEmlleELQLCEEQVIERLESAREQLQQATQAQQQAQGDLQRLGGRLASLEA 499
Cdd:COG4942 167 AELEAERAEL-----EALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|...
gi 24985991 500 LQQAALEPGAGAA 512
Cdd:COG4942 238 AAAERTPAAGFAA 250
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
154-333 |
3.29e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 154 EAKPEELRNFIEEAAgisKYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEKYREyKAQERQLKARLS 233
Cdd:pfam17380 431 EARQREVRRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR-KILEKELEERKQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 234 ALRwrdldEQVRQRESVIGDQGVSHEALVAEQRNADASIERLRDghHELSERfNQVQGRFYSVAGDIARVEqsiqhGQQR 313
Cdd:pfam17380 507 AMI-----EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQ--QEMEER-RRIQEQMRKATEERSRLE-----AMER 573
|
170 180
....*....|....*....|
gi 24985991 314 LRQLQDDFKEAERTRLETES 333
Cdd:pfam17380 574 EREMMRQIVESEKARAEYEA 593
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
656-767 |
3.52e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 656 IERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLR-RRTQDENRLHGELKASLSASRARAEQVELRRRRLQEELS 734
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQeEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGY 601
|
90 100 110
....*....|....*....|....*....|....*
gi 24985991 735 ELEEQRALE--HEQLGEARLLLQEALELMAQDTEQ 767
Cdd:PRK00409 602 ASVKAHELIeaRKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
654-994 |
3.83e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 654 QEIERLGQEQLEQEAALEQLDQQLQaLREQQldlEEQREQLrrrTQDENRLHGELKAS--LSASRARAEQVELRRRRlqe 731
Cdd:PRK10929 117 QLLEKSRQAQQEQDRAREISDSLSQ-LPQQQ---TEARRQL---NEIERRLQTLGTPNtpLAQAQLTALQAESAALK--- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 732 elseleeqraleheqlgeARLllqEALELmaqdteqrEQLMARRdtlRESLDRVRQEArqHKDHAHQLAVRLGSLRAQHD 811
Cdd:PRK10929 187 ------------------ALV---DELEL--------AQLSANN---RQELARLRSEL--AKKRSQQLDAYLQALRNQLN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 812 STRQalerleQQAARLTERQEQLSLNleEGEAPQeelrlkleellerrmSVDEEMRLarlhmdeaDRELRDAEKRRTQ-- 889
Cdd:PRK10929 233 SQRQ------REAERALESTELLAEQ--SGDLPK---------------SIVAQFKI--------NRELSQALNQQAQrm 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 890 ---AEQQAQlLRGQLEQLRlecQGLDVRRKtlQEQLLAD----GYDLQGVLATLEAEASEQGTEQELEQLeaRIQRLGAI 962
Cdd:PRK10929 282 dliASQQRQ-AASQTLQVR---QALNTLRE--QSQWLGVsnalGEALRAQVARLPEMPKPQQLDTEMAQL--RVQRLRYE 353
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24985991 963 NL----AAIEEYEQQ------SERKRYLDAQDADLVEALETL 994
Cdd:PRK10929 354 DLlnkqPQLRQIRQAdgqpltAEQNRILDAQLRTQRELLNSL 395
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
667-1023 |
3.94e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.43 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 667 EAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRRLQEELSELEEQRALEHEQ 746
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 747 LGEARLLLQEALELMAQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHDSTRQALERLEQQAAR 826
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 827 LTERQEQLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQQAQLLRGQLEQLRL 906
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 907 ECQGLDVRRKTLQEQLLADGYDLQGVLATLEAEASEQGTEQELEQLEARIQRLGAINLAAIEEYEQQSERKRYLDAQDAD 986
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350
....*....|....*....|....*....|....*..
gi 24985991 987 LVEALETLENVIRKIDKETRNRFKDTFDQINAGLQAL 1023
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEE 438
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1035-1142 |
4.00e-03 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 40.01 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1035 LELTG-EDLLDtgvtimaRPPgkknstiHLLSGGEKALTALALVFAifkLNPApfCM-LDEVDAPLDDANVGRYARLVKE 1112
Cdd:COG1122 119 LELVGlEHLAD-------RPP-------HELSGGQKQRVAIAGVLA---MEPE--VLvLDEPTAGLDPRGRRELLELLKR 179
|
90 100 110
....*....|....*....|....*....|..
gi 24985991 1113 MSES-VQFIYITHN-KIAMEMADQLmgVTMHE 1142
Cdd:COG1122 180 LNKEgKTVIIVTHDlDLVAELADRV--IVLDD 209
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
15-319 |
4.72e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 15 VDPTTVNFPSNMAAVVGPNGCGKSNIIDAVRWVMGEssaknlRGESmtDVIFNGSSgrkpvsQASIELVFDNSETTLVGE 94
Cdd:COG0497 13 IDELELEFGPGLTVLTGETGAGKSILLDALGLLLGG------RADA--SLVRHGAD------KAEVEAVFDLSDDPPLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 95 YAAYAEIS-------IRRKVTRDGQNSYYLNGTKCRRRDITDIFlgtglgprsysiieqgmiSKLIE----------AKP 157
Cdd:COG0497 79 WLEENGLDlddgeliLRREISADGRSRAFINGRPVTLSQLRELG------------------ELLVDihgqhehqslLDP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 158 EELRNFIEEAAGISKYKERRRETENRIRRTQENLARLTDLREELERQLERLHRQAQAAEkyreykaqerqlKARLSALRW 237
Cdd:COG0497 141 DAQRELLDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELE------------AAALQPGEE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 238 RDLDEQvRQR----ESVIGDQGVSHEALVAEQRNADASIERLR---------DGH-HELSERFNQVQGRFYSVAGDIARV 303
Cdd:COG0497 209 EELEEE-RRRlsnaEKLREALQEALEALSGGEGGALDLLGQALralerlaeyDPSlAELAERLESALIELEEAASELRRY 287
|
330
....*....|....*.
gi 24985991 304 EQSIQHGQQRLRQLQD 319
Cdd:COG0497 288 LDSLEFDPERLEEVEE 303
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
20-88 |
5.92e-03 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 39.50 E-value: 5.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24985991 20 VNFPSNMAAVVGPNGCGKSNIIDAVRWVMGESSAKNLRGESMTDVIFNGSsgrkpvSQASIELVFDNSE 88
Cdd:cd03276 17 IEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGE------SSAKITVTLKNQG 79
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1056-1136 |
5.94e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.12 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1056 KKNSTIHLLSGGEKALTALALVFAifkLNPApFCMLDEVDAPLDDANVGRYARLVKEMSES--VQFIYITHNKI-AMEmA 1132
Cdd:PRK13648 135 RADYEPNALSGGQKQRVAIAGVLA---LNPS-VIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSeAME-A 209
|
....
gi 24985991 1133 DQLM 1136
Cdd:PRK13648 210 DHVI 213
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
662-840 |
6.66e-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: 39.52 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 662 EQLEQEAALEQLDQQLQALREQQ-------LDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRRLQEELS 734
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLkelpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 735 ELEEQR---ALEHEqlgearlllQEALELMAQDTEQRE-QLMARRDTLRESLDRVRQEARQHKDHahqlavrlgsLRAQH 810
Cdd:COG1579 84 NVRNNKeyeALQKE---------IESLKRRISDLEDEIlELMERIEELEEELAELEAELAELEAE----------LEEKK 144
|
170 180 190
....*....|....*....|....*....|
gi 24985991 811 DSTRQALERLEQQAARLTERQEQLSLNLEE 840
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
650-905 |
6.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 650 LARGQEIERLGQEQleqEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENrlhgELKASLSASRARAEQVELRRRRl 729
Cdd:PRK03918 185 IKRTENIEELIKEK---EKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRK- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 730 qeelsELEEQRALEhEQLGEARLLLQEaLELMAQDTEQREQLMARRDTLRESLDRVRQEARqhkdhahQLAVRLGSLRAQ 809
Cdd:PRK03918 257 -----LEEKIRELE-ERIEELKKEIEE-LEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-------EIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 810 HDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQEELRLKLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQ 889
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250
....*....|....*.
gi 24985991 890 AEQQAQLLRGQLEQLR 905
Cdd:PRK03918 403 IEEEISKITARIGELK 418
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
687-905 |
7.93e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 40.69 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 687 LEEQREQLRRR-TQDENR---LHGELKASLSASRARAEQveLRRRRLQEELSELEEQRALEHEQLGEARLLLQEAlelma 762
Cdd:PLN03188 1045 PEKKLEQERLRwTEAESKwisLAEELRTELDASRALAEK--QKHELDTEKRCAEELKEAMQMAMEGHARMLEQYA----- 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 763 qDTEQRE-QLMARRDTLRESLDRVRQEARQ------HKDHAHQLAVRLGSLRAQHDSTRQALeRLEQQAArlterQEQLS 835
Cdd:PLN03188 1118 -DLEEKHiQLLARHRRIQEGIDDVKKAAARagvrgaESKFINALAAEISALKVEREKERRYL-RDENKSL-----QAQLR 1190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 836 lnlEEGEAPQEELRLkleellerrmsvdeemrLARLhmDEADRELRDAEKRRTQAEQQAQLLRGQLEQLR 905
Cdd:PLN03188 1191 ---DTAEAVQAAGEL-----------------LVRL--KEAEEALTVAQKRAMDAEQEAAEAYKQIDKLK 1238
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
713-896 |
8.29e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.32 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 713 SASRARAEQVELRRRRLQEELSELEEQRALEHEQLGEARLLlQEALELMAQdtEQREQLMARRDTLREslDRVRQEARQH 792
Cdd:pfam15709 334 SRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKM-REELELEQQ--RRFEEIRLRKQRLEE--ERQRQEEEER 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 793 KDHAHQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQlslnlEEGEAPQEELRLKLEELLERRMSVDEEMRLARLH 872
Cdd:pfam15709 409 KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEA-----EKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQK 483
|
170 180
....*....|....*....|....
gi 24985991 873 MDEADRELRDAEKRRTQAEQQAQL 896
Cdd:pfam15709 484 QEAEEKARLEAEERRQKEEEAARL 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
767-978 |
8.53e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 767 QREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQHD--STRQALERLEQQAARLTERQEQLSLNLEEGEAP 844
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 845 QEELRLKLEELLERRMSVDEEMRLARLHMDEADRELRDAEKRRTQAEQ--QAQLLRGQLEQLRlecqgldvrrKTLQEQL 922
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpDVIALRAQIAALR----------AQLQQEA 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24985991 923 LADGYDLQGVLATLEAEasEQGTEQELEQLEARIQRLGAInLAAIEEYEQQSERKR 978
Cdd:COG3206 312 QRILASLEAELEALQAR--EASLQAQLAQLEARLAELPEL-EAELRRLEREVEVAR 364
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
775-1000 |
8.64e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 775 RDTLRESLDRVRQEARQHKDHahQLAVRLGSLRAQHDSTRQALERLEQQAARLTERQEQLSLNLEEGEAPQEELRLKLEE 854
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 855 LLERRMSVDEEMR--------------------------LARLHMDEADREL----------RDAEKRRT--QAEQQAQL 896
Cdd:PRK02224 260 IEDLRETIAETERereelaeevrdlrerleeleeerddlLAEAGLDDADAEAvearreeledRDEELRDRleECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 897 LRGQLEQLRLECQGLDVRRKTLQEQLLADGYDLQGVLATLEAEASEQGT-EQELEQLEARIQRLGAINLAAIEEYEQQSE 975
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEElEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260
....*....|....*....|....*
gi 24985991 976 RKRYLDAQDADLVEALETLENVIRK 1000
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEE 444
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1041-1124 |
8.79e-03 |
|
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: 39.49 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 1041 DLLDTG---VTIMARP-PGKK-NSTIHLLSGGEKALTALALVFAIFKLNPAPFCMLDEVDAPLDDANVGRYARLVKEMSE 1115
Cdd:cd03241 143 DLLDGGlddVEFLFSTnPGEPlKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSR 222
|
....*....
gi 24985991 1116 SVQFIYITH 1124
Cdd:cd03241 223 SHQVLCITH 231
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
658-826 |
8.98e-03 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 40.35 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 658 RLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQL-------RRRTQDENRLHGELKASLSASRARAEQVELRRRRlq 730
Cdd:pfam04632 170 RLAAAALAGAPGAEAFEAARLRLAADILALEALRSHAafesprgRARARALRRLLARMLALLPRLRSLARLLARLRTE-- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24985991 731 eelseleeqralEHEQLGEARLLLQEALELmaQDTEQREQLMARRDTLRESLDRVRQEARQHKDHAHQLAVRLGSLRAQH 810
Cdd:pfam04632 248 ------------GAGTVPELAALLDELAAW--EAALAAEALQAALAALRARLRALRPALPLDFDTAAELLARLADLLAEL 313
|
170
....*....|....*.
gi 24985991 811 DSTRQALERLEQQAAR 826
Cdd:pfam04632 314 AEALASCRALRHPIAQ 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
651-728 |
9.77e-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: 9.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24985991 651 ARGQEIERLGQEQLEQEAALEQLDQQLQALREQQLDLEEQREQLRRRTQDENRLHGELKASLSASRARAEQVELRRRR 728
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| |
