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Conserved domains on  [gi|29336622|sp|Q14683|]
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RecName: Full=Structural maintenance of chromosomes protein 1A; Short=SMC protein 1A; Short=SMC-1-alpha; Short=SMC-1A; AltName: Full=Sb1.8

Protein Classification

chromosome segregation protein SMC( domain architecture ID 12035156)

chromosome segregation protein SMC is an ATPase required for chromosome condensation and partitioning

Gene Ontology:  GO:0003682|GO:0005524|GO:0016887|GO:0051301|GO:0007076|GO:0003677

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 3-1210 0e+00

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


:

Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 584.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTS-NLRVKTLRDLIHgaPVGKPAANRAFVS 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     82 MVYSEEGA-------EDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTAL 154
Cdd:pfam02463   79 ITFDNEDHelpidkeEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEA 314
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    315 AKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELE 394
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    395 KFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEIN 474
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    475 KELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGR 554
Cdd:pfam02463  479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    555 DCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEpphikkalqyacgnalvcdnvedarriafgghq 634
Cdd:pfam02463  559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL--------------------------------- 605

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    635 rhktvaldgtlfqksgvisggASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKY 714
Cdd:pfam02463  606 ---------------------AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    715 SQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEE 794
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    795 EKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLK 874
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    875 NQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEE 954
Cdd:pfam02463  825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    955 GSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESV 1034
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1035 RDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYN 1114
Cdd:pfam02463  985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIS 1064

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1115 CVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFY 1194
Cdd:pfam02463 1065 ARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSK-NAQFIVISLREEML 1143

                         1210
                   ....*....|....*.
gi 29336622   1195 TKAESLIGVYPEQGDC 1210
Cdd:pfam02463 1144 EKADKLVGVTMVENGV 1159
 
Name Accession Description Interval E-value
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 3-1210 0e+00

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 584.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTS-NLRVKTLRDLIHgaPVGKPAANRAFVS 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     82 MVYSEEGA-------EDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTAL 154
Cdd:pfam02463   79 ITFDNEDHelpidkeEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEA 314
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    315 AKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELE 394
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    395 KFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEIN 474
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    475 KELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGR 554
Cdd:pfam02463  479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    555 DCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEpphikkalqyacgnalvcdnvedarriafgghq 634
Cdd:pfam02463  559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL--------------------------------- 605

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    635 rhktvaldgtlfqksgvisggASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKY 714
Cdd:pfam02463  606 ---------------------AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    715 SQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEE 794
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    795 EKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLK 874
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    875 NQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEE 954
Cdd:pfam02463  825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    955 GSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESV 1034
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1035 RDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYN 1114
Cdd:pfam02463  985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIS 1064

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1115 CVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFY 1194
Cdd:pfam02463 1065 ARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSK-NAQFIVISLREEML 1143

                         1210
                   ....*....|....*.
gi 29336622   1195 TKAESLIGVYPEQGDC 1210
Cdd:pfam02463 1144 EKADKLVGVTMVENGV 1159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-1203 7.76e-98

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: 338.97  E-value: 7.76e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSN-LRVKTLRDLIHGAPVGKPAaNRAFVS 81
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQSG-NEAYVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     82 MVYSEEGA----EDRTFARVIV---GGSSEYKINNKVVQLHEYSEELEKLGILIKARNFlVFQGAVESIAMKNPKERTAL 154
Cdd:TIGR02169   80 VTFKNDDGkfpdELEVVRRLKVtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPVERRKI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:TIGR02169  159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMR--------EQQQIEKEIKEKDSELNQKRPQyIKAKEnts 306
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKIGELEAEIASLERS-IAEKE--- 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    307 hkiKKLEAAKKSLQNAQKHYKKRKGDMDELEKEmLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHR-LKEEASKR 385
Cdd:TIGR02169  315 ---RELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKDY 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    386 AATLAQ---ELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:TIGR02169  391 REKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    463 VEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQpTQKKYQIAVTKVLGKNM 542
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS-VGERYATAIEVAAGNRL 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    543 DAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGA-KLVIDVIRYEPpHIKKALQYACGNALVCDN 621
Cdd:TIGR02169  550 NNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGViGFAVDLVEFDP-KYEPAFKYVFGDTLVVED 628

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    622 VEDARRIAfgghQRHKTVALDGTLFQKSGVISGGAsdlkaKARRWDEKAVDKLKEKKERLTEELKEqmkAKRKEAELRQV 701
Cdd:TIGR02169  629 IEAARRLM----GKYRMVTLEGELFEKSGAMTGGS-----RAPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSE 696

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    702 QSQAHGLQMRLKYSQSDLEQtKTRHLALNLQEkskLESELANFGPRINDIKRIIQSREREMKDLKEKMnqvedevfeefc 781
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASR-KIGEIEKEIEQ---LEQEEEKLKERLEELEEDLSSLEQEIENVKSEL------------ 760

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    782 reigvrniREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHM-WEQTVKKDENEIEKLKKEEQRHM 860
Cdd:TIGR02169  761 --------KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEKEYLE 832

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    861 KIIDETMAQLQDLKNQhlakkseVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKl 940
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQ-------IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK- 904

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    941 plskgtmddisQEEGSSQGEDSvsgSQRISSiyaREALIEIDYGDLCEDLKDAQAEEEIKQE---MNTLQQKLNEQQSVL 1017
Cdd:TIGR02169  905 -----------IEELEAQIEKK---RKRLSE---LKAKLEALEEELSEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEI 967

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1018 QRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSrNSSAQAF 1097
Cdd:TIGR02169  968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELI 1046

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1098 LgpENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQ 1177
Cdd:TIGR02169 1047 L--ENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREK 1124

                         1210      1220
                   ....*....|....*....|....*.
gi 29336622   1178 STcNFQAIVISLKEEFYTKAESLIGV 1203
Cdd:TIGR02169 1125 AG-EAQFIVVSLRSPMIEYADRAIGV 1149
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 4-148 9.44e-85

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: 275.99  E-value: 9.44e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMV 83
Cdd:cd03275    1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622   84 YSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNP 148
Cdd:cd03275   81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-771 4.89e-59

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 221.35  E-value: 4.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    3 FLKLIEIENFKSYKGRQIIgPFQR-FTAIIGPNGSGKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFV 80
Cdd:COG1196    2 RLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   81 SMVYS-EEGAEDRTFARVIV------GGSSEYKINNKVVQLHEYSEELEKLGIliKARNF-LVFQGAVESIAMKNPKERT 152
Cdd:COG1196   81 SLTFDnSDGTLPIDYDEVTItrrlyrSGESEYYINGKPCRLKDIQDLFLDTGL--GPESYsIIGQGMIDRIIEAKPEERR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  153 ALFEE---ISRsgelaqeYDKRKKEmvkAE---EDTQFNYHRKKNIAAE----RKEAKQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:COG1196  159 AIIEEaagISK-------YKERKEE---AErklEATEENLERLEDILGElerqLEPLERQAEKAERYRELKEELKELEAE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAK 302
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  303 ENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEA 382
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  383 SKRAATLAQELEKFNRDQKADQDRLDLEERkkveteakikqKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLER-----------LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  463 VEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVY-----------GRLIDLCQPTQKKYQ 531
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaalllaglrglAGAVAVLIGVEAAYE 537

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  532 IAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRE----LKGAKLVIDVIRYEPPHIKK 607
Cdd:COG1196  538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgaiGAAVDLVASDLREADARYYV 617

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  608 ALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKE 687
Cdd:COG1196  618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL---EAEAELEELAERLAEEELE 694

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  688 QMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKE 767
Cdd:COG1196  695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774


                 ....
gi 29336622  768 KMNQ 771
Cdd:COG1196  775 EIEA 778
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 513-628 3.40e-32

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 121.57  E-value: 3.40e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     513 GSVYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVK-PTDEKLRELK-- 589
Cdd:smart00968    1 PGVLGRVADLISV-DPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRsPAGSKLREALlp 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 29336622     590 ---GAKLVIDVIRYePPHIKKALQYACGNALVCDNVEDARRI 628
Cdd:smart00968   80 epgFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
PTZ00121 PTZ00121
MAEBL; Provisional
 156-509 1.58e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.40  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   156 EEISRSGELAQ-EYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:PTZ00121 1339 EEAKKAAEAAKaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE---------NT 305
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkaeeakKK 1498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   306 SHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKR 385
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   386 AATLAQELEKFNRDQKADQDRLDLEERK------KVETEAKIK-QKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 458
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeeaKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 29336622   459 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
28-49 7.74e-03

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 39.14  E-value: 7.74e-03
                          10        20
                  ....*....|....*....|..
gi 29336622    28 TAIIGPNGSGKSNLMDAISFVL 49
Cdd:NF040873   21 TAVVGPNGSGKSTLLKVLAGVL 42
 
Name Accession Description Interval E-value
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 3-1210 0e+00

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 584.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTS-NLRVKTLRDLIHgaPVGKPAANRAFVS 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     82 MVYSEEGA-------EDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTAL 154
Cdd:pfam02463   79 ITFDNEDHelpidkeEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEA 314
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    315 AKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELE 394
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    395 KFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEIN 474
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    475 KELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGR 554
Cdd:pfam02463  479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    555 DCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEpphikkalqyacgnalvcdnvedarriafgghq 634
Cdd:pfam02463  559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL--------------------------------- 605

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    635 rhktvaldgtlfqksgvisggASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKY 714
Cdd:pfam02463  606 ---------------------AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    715 SQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEE 794
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    795 EKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLK 874
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    875 NQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEE 954
Cdd:pfam02463  825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    955 GSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESV 1034
Cdd:pfam02463  905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1035 RDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYN 1114
Cdd:pfam02463  985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIS 1064

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1115 CVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFY 1194
Cdd:pfam02463 1065 ARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSK-NAQFIVISLREEML 1143

                         1210
                   ....*....|....*.
gi 29336622   1195 TKAESLIGVYPEQGDC 1210
Cdd:pfam02463 1144 EKADKLVGVTMVENGV 1159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-1203 7.76e-98

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: 338.97  E-value: 7.76e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSN-LRVKTLRDLIHGAPVGKPAaNRAFVS 81
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQSG-NEAYVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     82 MVYSEEGA----EDRTFARVIV---GGSSEYKINNKVVQLHEYSEELEKLGILIKARNFlVFQGAVESIAMKNPKERTAL 154
Cdd:TIGR02169   80 VTFKNDDGkfpdELEVVRRLKVtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPVERRKI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:TIGR02169  159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMR--------EQQQIEKEIKEKDSELNQKRPQyIKAKEnts 306
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKIGELEAEIASLERS-IAEKE--- 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    307 hkiKKLEAAKKSLQNAQKHYKKRKGDMDELEKEmLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHR-LKEEASKR 385
Cdd:TIGR02169  315 ---RELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKDY 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    386 AATLAQ---ELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:TIGR02169  391 REKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    463 VEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQpTQKKYQIAVTKVLGKNM 542
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS-VGERYATAIEVAAGNRL 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    543 DAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGA-KLVIDVIRYEPpHIKKALQYACGNALVCDN 621
Cdd:TIGR02169  550 NNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGViGFAVDLVEFDP-KYEPAFKYVFGDTLVVED 628

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    622 VEDARRIAfgghQRHKTVALDGTLFQKSGVISGGAsdlkaKARRWDEKAVDKLKEKKERLTEELKEqmkAKRKEAELRQV 701
Cdd:TIGR02169  629 IEAARRLM----GKYRMVTLEGELFEKSGAMTGGS-----RAPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSE 696

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    702 QSQAHGLQMRLKYSQSDLEQtKTRHLALNLQEkskLESELANFGPRINDIKRIIQSREREMKDLKEKMnqvedevfeefc 781
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASR-KIGEIEKEIEQ---LEQEEEKLKERLEELEEDLSSLEQEIENVKSEL------------ 760

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    782 reigvrniREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHM-WEQTVKKDENEIEKLKKEEQRHM 860
Cdd:TIGR02169  761 --------KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEKEYLE 832

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    861 KIIDETMAQLQDLKNQhlakkseVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKl 940
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQ-------IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK- 904

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    941 plskgtmddisQEEGSSQGEDSvsgSQRISSiyaREALIEIDYGDLCEDLKDAQAEEEIKQE---MNTLQQKLNEQQSVL 1017
Cdd:TIGR02169  905 -----------IEELEAQIEKK---RKRLSE---LKAKLEALEEELSEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEI 967

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1018 QRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSrNSSAQAF 1097
Cdd:TIGR02169  968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS-GGTGELI 1046

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1098 LgpENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQ 1177
Cdd:TIGR02169 1047 L--ENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREK 1124

                         1210      1220
                   ....*....|....*....|....*.
gi 29336622   1178 STcNFQAIVISLKEEFYTKAESLIGV 1203
Cdd:TIGR02169 1125 AG-EAQFIVVSLRSPMIEYADRAIGV 1149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-1220 1.59e-92

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: 323.93  E-value: 1.59e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFVS 81
Cdd:TIGR02168    1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEqSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     82 MVYSEEgaeDRTFA-----------RVIVGGSSEYKINNKVVQLHEYSEELekLGILIKARNF-LVFQGAVESIAMKNPK 149
Cdd:TIGR02168   81 LVFDNS---DGLLPgadyseisitrRLYRDGESEYFINGQPCRLKDIQDLF--LDTGLGKRSYsIIEQGKISEIIEAKPE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    150 ERTALFEE---ISRsgelaqeYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEA----KQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:TIGR02168  156 ERRAIFEEaagISK-------YKERRKETERKLERTRENLDRLEDILNELERQlkslERQAEKAERYKELKAELRELELA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAK 302
Cdd:TIGR02168  229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    303 ENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKarqefeermeeesqsqgrDLTLEENQVKKYHRLKEEA 382
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE------------------ELESLEAELEELEAELEEL 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    383 SKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSK-----QSLEEQKKLEG 457
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELE 450

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    458 ELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQES--------SRQQRKAEIMESIK-----RLYPGSVYGRLIDLCQ 524
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLqarldsleRLQENLEGFSEGVKallknQSGLSGILGVLSELIS 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    525 pTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLE----VKPTDEKLRELKGAKLVIDVIRY 600
Cdd:TIGR02168  531 -VDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgteiQGNDREILKNIEGFLGVAKDLVK 609

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    601 EPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAK--ARRwdeKAVDKLKEKK 678
Cdd:TIGR02168  610 FDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSilERR---REIEELEEKI 686

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    679 ERLTEELKE-QMKAKRKEAELRQVQSQAHGLQMRLKYSQsdleqtktrhlalnlQEKSKLESELANFGPRINDIKRIIQS 757
Cdd:TIGR02168  687 EELEEKIAElEKALAELRKELEELEEELEQLRKELEELS---------------RQISALRKDLARLEAEVEQLEERIAQ 751

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    758 REREMKDLKEKMNQVEDEVFEEFcreigvRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQldfeKNQLKEDQDKVHM 837
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAE------EELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAAN 821

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    838 WEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKnqhlakkSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIET 917
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRS 894

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    918 KLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQgedsvsgsQRISSIyaREALIEiDYGDLCEDLkdAQAEE 997
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE--------VRIDNL--QERLSE-EYSLTLEEA--EALEN 961

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    998 EIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESV 1077
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQV 1041

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   1078 ATNIDEIYKALSRNSSAQ-AFLGPENPEEPyldGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLD 1156
Cdd:TIGR02168 1042 NENFQRVFPKLFGGGEAElRLTDPEDLLEA---GIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILD 1118

                         1210      1220      1230      1240      1250      1260
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622   1157 EIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTKAESLIGV-YPEQGdcvISKVLTFDL 1220
Cdd:TIGR02168 1119 EVDAPLDDANVERFANLLKEFSK-NTQFIVITHNKGTMEVADQLYGVtMQEKG---VSKIVSVDL 1179
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 4-148 9.44e-85

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: 275.99  E-value: 9.44e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMV 83
Cdd:cd03275    1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622   84 YSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNP 148
Cdd:cd03275   81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 1117-1220 8.90e-66

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: 222.83  E-value: 8.90e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1117 APGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTK 1196
Cdd:cd03275  145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFSK 224

                         90       100
                 ....*....|....*....|....
gi 29336622 1197 AESLIGVYPEQgDCVISKVLTFDL 1220
Cdd:cd03275  225 ADALVGVYRDQ-ECNSSKVLTLDL 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-771 4.89e-59

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 221.35  E-value: 4.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    3 FLKLIEIENFKSYKGRQIIgPFQR-FTAIIGPNGSGKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFV 80
Cdd:COG1196    2 RLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   81 SMVYS-EEGAEDRTFARVIV------GGSSEYKINNKVVQLHEYSEELEKLGIliKARNF-LVFQGAVESIAMKNPKERT 152
Cdd:COG1196   81 SLTFDnSDGTLPIDYDEVTItrrlyrSGESEYYINGKPCRLKDIQDLFLDTGL--GPESYsIIGQGMIDRIIEAKPEERR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  153 ALFEE---ISRsgelaqeYDKRKKEmvkAE---EDTQFNYHRKKNIAAE----RKEAKQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:COG1196  159 AIIEEaagISK-------YKERKEE---AErklEATEENLERLEDILGElerqLEPLERQAEKAERYRELKEELKELEAE 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAK 302
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  303 ENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEA 382
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  383 SKRAATLAQELEKFNRDQKADQDRLDLEERkkveteakikqKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLER-----------LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  463 VEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVY-----------GRLIDLCQPTQKKYQ 531
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaalllaglrglAGAVAVLIGVEAAYE 537

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  532 IAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRE----LKGAKLVIDVIRYEPPHIKK 607
Cdd:COG1196  538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgaiGAAVDLVASDLREADARYYV 617

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  608 ALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKE 687
Cdd:COG1196  618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL---EAEAELEELAERLAEEELE 694

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  688 QMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKE 767
Cdd:COG1196  695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774


                 ....
gi 29336622  768 KMNQ 771
Cdd:COG1196  775 EIEA 778
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 513-628 3.40e-32

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 121.57  E-value: 3.40e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     513 GSVYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVK-PTDEKLRELK-- 589
Cdd:smart00968    1 PGVLGRVADLISV-DPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRsPAGSKLREALlp 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 29336622     590 ---GAKLVIDVIRYePPHIKKALQYACGNALVCDNVEDARRI 628
Cdd:smart00968   80 epgFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 1117-1203 1.43e-29

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: 116.80  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1117 APGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTK 1196
Cdd:cd03278  103 APGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSK-ETQFIVITHRKGTMEA 181


                 ....*..
gi 29336622 1197 AESLIGV 1203
Cdd:cd03278  182 ADRLYGV 188
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 1118-1204 4.87e-29

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: 115.86  E-value: 4.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1118 PGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQsTCNFQAIVISLKEEFYTKA 1197
Cdd:cd03274  118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKER-TKNAQFIVISLRNNMFELA 196


                 ....*..
gi 29336622 1198 ESLIGVY 1204
Cdd:cd03274  197 DRLVGIY 203
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
 515-629 8.99e-28

SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 461926 [Multi-domain]  Cd Length: 116  Bit Score: 108.89  E-value: 8.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    515 VYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLV 594
Cdd:pfam06470    4 VLGRLADLIEV-DEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGAGPL 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 29336622    595 IDVIRYEPPhIKKALQYACGNALVCDNVEDARRIA 629
Cdd:pfam06470   83 LDLVEYDDE-YRKALRYLLGNTLVVDDLDEALELA 116
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 1128-1208 1.71e-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: 104.70  E-value: 1.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1128 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQ 1207
Cdd:cd03239   95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVLFVH 174


                 .
gi 29336622 1208 G 1208
Cdd:cd03239  175 G 175
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 3-145 4.33e-25

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: 104.69  E-value: 4.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    3 FLKLIEIENFKSYKGRQIIGPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPvGKPAANRAFVS 81
Cdd:cd03274    2 IITKLVLENFKSYAGEQVIGPFhKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSA-GHPNLDSCSVE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29336622   82 MvyseegaedrTFARVIVggsseykinnkvvqlheySEELEKLGILIKARNFLVFQGAVESIAM 145
Cdd:cd03274   81 V----------HFQEIID------------------KPLLKSKGIDLDHNRFLILQGEVEQIAQ 116
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 4-100 4.32e-24

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: 101.00  E-value: 4.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    4 LKLIEIENFKSYKGRQIIgPFQR-FTAIIGPNGSGKSNLMDAISFVLGEKTS-NLRVKTLRDLIHGAPVGKPAANRAFVS 81
Cdd:cd03278    1 LKKLELKGFKSFADKTTI-PFPPgLTAIVGPNGSGKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSETRKPANFAEVT 79

                         90
                 ....*....|....*....
gi 29336622   82 MVYSEegaEDRTFArvIVG 100
Cdd:cd03278   80 LTFDN---SDGRYS--IIS 93
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 3-140 1.96e-23

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: 100.84  E-value: 1.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    3 FLKLIEIENFKSYKGRQIIGPFQR-FTAIIGPNGSGKSNLMDAISFVLG-EKTSNLRVKTLRDLIHGApvGKPAANRAFV 80
Cdd:cd03273    2 HIKEIILDGFKSYATRTVISGFDPqFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYKR--GQAGITKASV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29336622   81 SMVY-------SEEGAEDR---TFAR-VIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAV 140
Cdd:cd03273   80 TIVFdnsdksqSPIGFENYpeiTVTRqIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 4-84 4.21e-23

The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.


Pssm-ID: 213206 [Multi-domain]  Cd Length: 178  Bit Score: 97.76  E-value: 4.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGApvGKPAANRAFVSMV 83
Cdd:cd03239    1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGG--VKAGINSASVEIT 78


                 .
gi 29336622   84 Y 84
Cdd:cd03239   79 F 79
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 1128-1208 1.06e-19

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: 87.42  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1128 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQ 1207
Cdd:cd03227   78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKVI 157


                 .
gi 29336622 1208 G 1208
Cdd:cd03227  158 T 158
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 4-145 5.02e-16

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 79.23  E-value: 5.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    4 LKLIEIENFKSYKGRQIIGPFQ-RFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIH-GApvgKPAANRAFVS 81
Cdd:cd03272    1 IKQVIIQGFKSYKDQTVIEPFSpKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHeGS---GPSVMSAYVE 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   82 MVY--SEE----GAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAM 145
Cdd:cd03272   78 IIFdnSDNrfpiDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTN 147
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 1128-1213 6.41e-16

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 78.88  E-value: 6.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1128 LSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALD--NT-NIGKVanyIKEQSTcNFQAIVISLKEEFYTKAESLIGVY 1204
Cdd:cd03273  167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDlsHTqNIGRM---IKTHFK-GSQFIVVSLKEGMFNNANVLFRTR 242


                 ....*....
gi 29336622 1205 PEQGDCVIS 1213
Cdd:cd03273  243 FVDGTSTVT 251
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 1125-1203 2.50e-15

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: 76.92  E-value: 2.50e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29336622 1125 MDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTcNFQAIVISLKEEFYTKAESLIGV 1203
Cdd:cd03272  156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSD-GAQFITTTFRPELLEVADKFYGV 233
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 7-84 8.39e-13

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: 67.38  E-value: 8.39e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29336622    7 IEIENFKSYKGRQIIGPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTlrdlihgapVGKPAANRAFVSMVY 84
Cdd:cd03227    2 IVLGRFPSYFVPNDVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS---------GVKAGCIVAAVSAEL 71
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
4-127 6.12e-12

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 66.19  E-value: 6.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNlRVKTLRDLIHgapvgkPAANRAFVSMV 83
Cdd:COG0419    2 LLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLIN------VGSEEASVELE 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 29336622   84 YSEEGAEDR------TFARVIVGGSSE-YKINNKVVQLHEYSEELEKLGIL 127
Cdd:COG0419   75 FEHGGKRYRierrqgEFAEFLEAKPSErKEALKRLLGLEIYEELKERLKEL 125
PTZ00121 PTZ00121
MAEBL; Provisional
 156-509 1.58e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.40  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   156 EEISRSGELAQ-EYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:PTZ00121 1339 EEAKKAAEAAKaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE---------NT 305
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkaeeakKK 1498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   306 SHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKR 385
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   386 AATLAQELEKFNRDQKADQDRLDLEERK------KVETEAKIK-QKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 458
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeeaKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 29336622   459 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
PTZ00121 PTZ00121
MAEBL; Provisional
 156-509 1.75e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.01  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   156 EEISRSGELAQEYDKRK-KEMVKAEEDTQFNYHRKKniAAERKEAKQEKEEADRYQRLKDEVVR-AQVQLQLFKLYHNEV 233
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKaDEAKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKkAEEAKKAAEAAKAEA 1352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   234 EIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE--NTSHKIKK 311
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEakKKAEEKKK 1432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   312 LEAAKKSLQNAQK--HYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYH---RLKEEASKRA 386
Cdd:PTZ00121 1433 ADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeaKKAAEAKKKA 1512

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   387 ATL--------AQELEKFNRDQKADQDR-----------LDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY------ 441
Cdd:PTZ00121 1513 DEAkkaeeakkADEAKKAEEAKKADEAKkaeekkkadelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeea 1592

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29336622   442 -ITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK--ELNQVMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1593 rIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKaeEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
PTZ00121 PTZ00121
MAEBL; Provisional
 144-508 4.35e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.86  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   144 AMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNiAAERKEAKQEKEEADRYQRLKDEVVRAQvql 223
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKAD--- 1434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   224 QLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE 303
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   304 -------NTSHKIKKLEAAKKSlQNAQKHYKKRKGD----MDELEK--EMLSVEKARQEFEERMEEESQSQGRDlTLEEN 370
Cdd:PTZ00121 1515 akkaeeaKKADEAKKAEEAKKA-DEAKKAEEKKKADelkkAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAK-KAEEA 1592

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   371 QVKKYHRLKEEASKRAATLAQELEKfnRDQKADQDRLDLEERKKVE----TEAKIKQKLREI----EENQKRIEKLEEYI 442
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEqlkkKEAEEKKKAEELkkaeEENKIKAAEEAKKA 1670

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29336622   443 TTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKelnqvMEQLGDARIDRQESSRQQRKAEIMESIK 508
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIK 1731
PTZ00121 PTZ00121
MAEBL; Provisional
 144-505 5.33e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 5.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   144 AMKNPKERTALFEEISRSGELAQEYDKRKKemvKAEEDTQFNYHRKKNIAAER-KEAKQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKK---KAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAKKA 1472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKE---KDSELNQKRPQYI 299
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKADELK 1552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   300 KAKE-NTSHKIKKLEAAKKSLQNAQKHYKK----RKGDMDELEKEM--LSVEKARQEFEERMEEESQSQGRDLTLEENQV 372
Cdd:PTZ00121 1553 KAEElKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   373 KKYHRLK--EEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE 450
Cdd:PTZ00121 1633 KKVEQLKkkEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 29336622   451 EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIME 505
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
COG4637 COG4637
Predicted ATPase [General function prediction only];
4-48 1.02e-10

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 64.95  E-value: 1.02e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 29336622    4 LKLIEIENFKSYkgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFV 48
Cdd:COG4637    2 ITRIRIKNFKSL--RDLELPLGPLTVLIGANGSGKSNLLDALRFL 44
PTZ00121 PTZ00121
MAEBL; Provisional
 156-775 1.64e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.93  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   156 EEISRSGELAQEYDKRKKEMV-------KAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEvvRAQVQLQLFKL 228
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAArkaeeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN--EEIRKFEEARM 1262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   229 YHNEVEIEKLNKELASKNKEIEK--DKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQyikAKENTS 306
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA---AKKKAE 1339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   307 HKIKKLEAAKKSLQNAQKHYK--KRKGDMDELEKEmlsvekarqefeermeeESQSQGRDLTLEENQVKKYHRLKEEASK 384
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKE-----------------EAKKKADAAKKKAEEKKKADEAKKKAEE 1402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   385 RAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE-----------EQK 453
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEakkadeakkkaEEA 1482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   454 KLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIA 533
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   534 VTKVLGKNMDAiiVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYAC 613
Cdd:PTZ00121 1563 KKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   614 GNALVCDNVEDARRIAFGGHQRHKTVAldgtlfQKSGVISGGASDLKaKARRWDEKAVDKLKEKKE--RLTEELKEQMKA 691
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEA------KKAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEeaKKAEELKKKEAE 1713

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   692 KRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQ 771
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793


                  ....
gi 29336622   772 VEDE 775
Cdd:PTZ00121 1794 MEVD 1797
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-854 9.09e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 9.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELnqkrPQYIKAKENTSHKIKKLEAA 315
Cdd:PRK03918  161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL----PELREELEKLEKEVKELEEL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKaRQEFEERMEEESQSQGRDLTLEENQVKKYHRLKE---EASKRAATLAQE 392
Cdd:PRK03918  237 KEEIEELEKELESLEGSKRKLEEKIRELEE-RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKR 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   393 LEKFNRDQKADQDRLDLEERKKVETEaKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELT-EEVEMAKRRID 471
Cdd:PRK03918  316 LSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELE 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   472 EINKELNQVMEQLGD--ARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIdlcqptqkkyqiavtkvlgknmdaiivDS 549
Cdd:PRK03918  395 ELEKAKEEIEEEISKitARIGELKKEIKELKKAIEELKKAKGKCPVCGREL---------------------------TE 447

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   550 EKTGRDCIQYIKEQRGEPEtflpldylEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYA-----CGNALVCDNVED 624
Cdd:PRK03918  448 EHRKELLEEYTAELKRIEK--------ELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkeLEEKLKKYNLEE 519

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   625 ARRIAfgghqrHKTVALDGTLFQKSGVISGGASDLKA-----KARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELR 699
Cdd:PRK03918  520 LEKKA------EEYEKLKEKLIKLKGEIKSLKKELEKleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   700 -QVQSQAHGLQMRLKYSQSDLEQTktrhlalnLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQvedevfE 778
Cdd:PRK03918  594 lKELEPFYNEYLELKDAEKELERE--------EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE------E 659

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29336622   779 EFcreigvrniREFEEEKVKRQNEIAKKRLEFEnqktrlgiQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKK 854
Cdd:PRK03918  660 EY---------EELREEYLELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
AAA_23 pfam13476
AAA domain;
7-183 3.63e-09

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 57.89  E-value: 3.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      7 IEIENFKSYKGrQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAP-VGKPAANRAFVSMVYS 85
Cdd:pfam13476    1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIrIGLEGKGKAYVEITFE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     86 EEGAE-----DRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVF---QGAVESIAMKNPKER-TALFE 156
Cdd:pfam13476   80 NNDGRytyaiERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVflgQEREEEFERKEKKERlEELEK 159

                          170       180
                   ....*....|....*....|....*..
gi 29336622    157 EISRSGELAQEYDKRKKEMVKAEEDTQ 183
Cdd:pfam13476  160 ALEEKEDEKKLLEKLLQLKEKKKELEE 186
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 7-880 3.97e-09

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: 61.14  E-value: 3.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      7 IEIENFKSYKGRQII--GPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLR--VKTLRDLIHGAPVGKPA-------- 74
Cdd:TIGR00618    6 LTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSevIRSLNSLYAAPSEAAFAelefslgt 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     75 -ANRAFVSMVYSEEGAEDRTFARVIVG--GSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKER 151
Cdd:TIGR00618   86 kIYRVHRTLRCTRSHRKTEQPEQLYLEqkKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    152 TALFE----------------EISRSGELAQEYDKRKKEMVK--AEEDTQFNYHRKKNIAAERK---EAKQEKEEADRYQ 210
Cdd:TIGR00618  166 KELLMnlfpldqytqlalmefAKKKSLHGKAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKhlrEALQQTQQSHAYL 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    211 RLKDEVVRAQVQLQ--LFKLYHNEVEIEKLNKELASKNKEIEKDKKrmdkvEDELKEKKKELGKMMREQQQIEKEIKEKD 288
Cdd:TIGR00618  246 TQKREAQEEQLKKQqlLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQSKM 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    289 SELNQKRPQYIKAKENTShKIKKLEAAKKSLQNAQKHYK----KRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRD 364
Cdd:TIGR00618  321 RSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLHSQEIHIRdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    365 LTLEENQVKKYHRLKEEASKRAatLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITT 444
Cdd:TIGR00618  400 KELDILQREQATIDTRTSAFRD--LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    445 SKQSLE---EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSR-QQRKAEIMESIKRLYpgsvygrli 520
Cdd:TIGR00618  478 KEQIHLqetRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSEEDVY--------- 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    521 DLCQPTQKKYQIAvtkvlgKNMDAIIVDSEKTGRDCIQYIKEQRgePETFLPLDylEVKPTDEKLRELKGAKLVIDVIRY 600
Cdd:TIGR00618  549 HQLTSERKQRASL------KEQMQEIQQSFSILTQCDNRSKEDI--PNLQNITV--RLQDLTEKLSEAEDMLACEQHALL 618

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    601 EPPHIKKALQYACGNALVCDNVEDARRIAFGG------HQRHKTVALDGTLFQKSgviSGGASDLKAKARRWDEKAVDKL 674
Cdd:TIGR00618  619 RKLQPEQDLQDVRLHLQQCSQELALKLTALHAlqltltQERVREHALSIRVLPKE---LLASRQLALQKMQSEKEQLTYW 695

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    675 KEKKERLTEELKEQMKAKRKEAELRQVQSQA-HGLQMRLKYSQSDLEQ----------TKTRHLALNLQEKSKLESELAN 743
Cdd:TIGR00618  696 KEMLAQCQTLLRELETHIEEYDREFNEIENAsSSLGSDLAAREDALNQslkelmhqarTVLKARTEAHFNNNEEVTAALQ 775

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    744 FGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEfcreigvrnIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDF 823
Cdd:TIGR00618  776 TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE---------IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGE 846

                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29336622    824 EKNQLKEDQDKVHMWEQTVKKDENEIEKLKK-----------EEQRHMKIIDETMAQ-LQDLKNQHLAK 880
Cdd:TIGR00618  847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKlnginqikiqfDGDALIKFLHEITLYaNVRLANQSEGR 915
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
3-113 5.07e-09

Recombinational DNA repair ATPase RecF [Replication, recombination and repair];


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 59.40  E-value: 5.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGekTSNLRVKTLRDLI-HGAPvgkpaanRAFVS 81
Cdd:COG1195    1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYLLAT--GRSFRTARDAELIrFGAD-------GFRVR 70

                         90       100       110
                 ....*....|....*....|....*....|..
gi 29336622   82 MVYSEEGAEDRTFARVIVGGSSEYKINNKVVQ 113
Cdd:COG1195   71 AEVERDGREVRLGLGLSRGGKKRVRINGKPVR 102
PTZ00121 PTZ00121
MAEBL; Provisional
 145-509 7.17e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 7.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   145 MKNPKERTALFEEISRSGELAQEYD--KRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQrlKDEVVRAQVQ 222
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADE 1526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   223 LQLFKLYHNEVEIEKLN-KELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKrpQYIKA 301
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEE 1604

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   302 KENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERmeeesqsqgrdltlEENQVKKYH-RLKE 380
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE--------------EENKIKAAEeAKKA 1670

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   381 EASKRAATLAQELEKFNRdQKADQDRLDLEERKKVEteakikQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELT 460
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEK-KAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 29336622   461 EEVEMAKRRIDEINKelnqvMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
309-869 1.16e-08

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.54  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  309 IKKLEAAKKSLQNAQKHYKKRKGDMDELE-----KEMLSVEKARQEFeermeeesQSQGRDLTLEENQVKKYHRLKEEAS 383
Cdd:COG4913  244 LEDAREQIELLEPIRELAERYAAARERLAeleylRAALRLWFAQRRL--------ELLEAELEELRAELARLEAELERLE 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  384 KRAATLAQELEKFNRD-QKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLegeltee 462
Cdd:COG4913  316 ARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE------- 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  463 vemAKRRIDEINKELNQVMEQLGDARIDRQESSRQQR--KAEI--MESIKRLYPGSVY--------------------GR 518
Cdd:COG4913  389 ---AAALLEALEEELEALEEALAEAEAALRDLRRELRelEAEIasLERRKSNIPARLLalrdalaealgldeaelpfvGE 465

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  519 LIDLcQPTQKKYQIAVTKVLGKNMDAIIVDsEKTGRDCIQYIKEQRGEPEtflpLDYLEVKPTDEKLRELKG------AK 592
Cdd:COG4913  466 LIEV-RPEEERWRGAIERVLGGFALTLLVP-PEHYAAALRWVNRLHLRGR----LVYERVRTGLPDPERPRLdpdslaGK 539

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  593 LVIDVIRYEP---PHIKKALQYACgnalvCDNVEDARRiafggHQRHKTVA----LDGTLFQKsgvisggasDLKAKARR 665
Cdd:COG4913  540 LDFKPHPFRAwleAELGRRFDYVC-----VDSPEELRR-----HPRAITRAgqvkGNGTRHEK---------DDRRRIRS 600

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  666 -----WD-EKAVDKLKEKKERLTEELKE-QMKAKRKEAELRQVQSQAHGLQMRLKYS--QSDLEQTKTRHLALNlQEKSK 736
Cdd:COG4913  601 ryvlgFDnRAKLAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELE-AELER 679

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  737 LE---SELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEvfeefcreigvrnIREFEEEKvkrqnEIAKKRLEFENQ 813
Cdd:COG4913  680 LDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-------------LEQAEEEL-----DELQDRLEAAED 741

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 29336622  814 KTRLGIQLDFEKNQLKEDQDKVhmwEQTVKKD-ENEIEKLKKEEQRHMKIIDETMAQ 869
Cdd:COG4913  742 LARLELRALLEERFAAALGDAV---ERELRENlEERIDALRARLNRAEEELERAMRA 795
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 195-508 2.45e-08

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: 58.60  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    195 ERKEAKQEKEEADRYQRLKDEVVRAqvqlqlfklyhnevEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMM 274
Cdd:pfam17380  279 QHQKAVSERQQQEKFEKMEQERLRQ--------------EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    275 REQQQIEK-EIKEKDSELNQKRPQYIKAKENTSHKIKKL--EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFE 351
Cdd:pfam17380  345 ERERELERiRQEERKRELERIRQEEIAMEISRMRELERLqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    352 ERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLaQELEKFNRDQKADQDRLDLEERKKVETEAK----IKQKLRE 427
Cdd:pfam17380  425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEE 503

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    428 -----IEENQKR--IEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRideinkelnQVMEQLGDARIDRQESSRQQRK 500
Cdd:pfam17380  504 rkqamIEEERKRklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR---------RIQEQMRKATEERSRLEAMERE 574


                   ....*...
gi 29336622    501 AEIMESIK 508
Cdd:pfam17380  575 REMMRQIV 582
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 659-1035 2.83e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  659 LKAKARRwdEKAVDKLKEKKERLT------EELKEQMKAKRKEAElrqVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQ 732
Cdd:COG1196  168 SKYKERK--EEAERKLEATEENLErledilGELERQLEPLERQAE---KAERYRELKEELKELEAELLLLKLRELEAELE 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  733 EKSKLESELANfgpRINDIKRIIQSREREMKDLKEKMNQVEDEVfeefcreigvrnirefeEEKVKRQNEIAKKRLEFEN 812
Cdd:COG1196  243 ELEAELEELEA---ELEELEAELAELEAELEELRLELEELELEL-----------------EEAQAEEYELLAELARLEQ 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  813 QKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEME 892
Cdd:COG1196  303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  893 EIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQgedsvsgsQRISSI 972
Cdd:COG1196  383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA--------EEEAEL 454

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29336622  973 YAREALIEIdygdlcEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVR 1035
Cdd:COG1196  455 EEEEEALLE------LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
156-508 4.45e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.77  E-value: 4.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE- 234
Cdd:PRK03918  384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKr 463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEkkkelgkmMREQQQIEKEIKEKDSELNQKRPQYIKAK----ENTSHKIK 310
Cdd:PRK03918  464 IEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKELEEKLKKYNLEELEKKaeeyEKLKEKLI 535

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   311 KLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLkeeaskraatlA 390
Cdd:PRK03918  536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE-----------Y 604

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   391 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKL------EEYITTSKQSLEEQKKLEGeLTEEVE 464
Cdd:PRK03918  605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseEEYEELREEYLELSRELAG-LRAELE 683

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 29336622   465 MAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIK 508
Cdd:PRK03918  684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELR 727
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 3-55 5.98e-08

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: 56.16  E-value: 5.98e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 29336622    3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSN 55
Cdd:COG3593    2 KLEKIKIKNFRSIK-DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
PTZ00121 PTZ00121
MAEBL; Provisional
 287-923 6.26e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 6.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   287 KDSELNQKRPQyiKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEkEMLSVEKARQEFEERMEEESQSQGRDLT 366
Cdd:PTZ00121 1077 KDFDFDAKEDN--RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARKAEDARKAEEARKAEDAKR 1153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   367 LEENQVKKYHRLKEEASKraatlAQELEKFNRDQKADQDRlDLEERKKVETEAKIKQKLREieENQKRIEKLEEYitTSK 446
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARK-----AEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKA--EEERKAEEARKA--EDA 1223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   447 QSLEEQKKLEgELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRlypgSVYGRLIDLCQPT 526
Cdd:PTZ00121 1224 KKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK----AEEKKKADEAKKA 1298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   527 QKKYQIAVTKVLGKNMDAiIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIK 606
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   607 KALQYACGNALVCDNVEDARRIAFGGHQRHKTValdgtlfQKSGVISGGASDLKAKARrwDEKAVDKLKEKKE--RLTEE 684
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADEL-------KKAAAAKKKADEAKKKAE--EKKKADEAKKKAEeaKKADE 1448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   685 LKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSRE-REMK 763
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKaDEAK 1528

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   764 DLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQL-DFEKNQLKE-----DQDKVHM 837
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEvmklyEEEKKMK 1608

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   838 WEQTVKKDENEI--EKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDK------NHEMEEIRKKLGGANKEMTHLQ 909
Cdd:PTZ00121 1609 AEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKAEEDEK 1688

                         650
                  ....*....|....
gi 29336622   910 KEVTAIETKLEQKR 923
Cdd:PTZ00121 1689 KAAEALKKEAEEAK 1702
PTZ00121 PTZ00121
MAEBL; Provisional
 188-1041 1.07e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   188 RKKNIAAER-KEAKQEKEEADRYQRLKDEVVRaqvqlqlfklyhnEVEIEKLNKELASKNKEIEK--DKKRMDKVEDELK 264
Cdd:PTZ00121 1084 KEDNRADEAtEEAFGKAEEAKKTETGKAEEAR-------------KAEEAKKKAEDARKAEEARKaeDARKAEEARKAED 1150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   265 EKKKELGKMMREQQQIEKEIKEKDS---ELNQKRPQYIKAKE-NTSHKIKKLEAAKKSlQNAQKHYKKRKGDMDELEKEM 340
Cdd:PTZ00121 1151 AKRVEIARKAEDARKAEEARKAEDAkkaEAARKAEEVRKAEElRKAEDARKAEAARKA-EEERKAEEARKAEDAKKAEAV 1229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   341 LSVEKARQEFEERMEEESQSQGRDL-TLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRlDLEERKKVETEA 419
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIrKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK-KAEEKKKADEAK 1308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   420 KIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKlegelteEVEMAKRRIDEINKELNQVMEQlgdARIDRQESSRQQR 499
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK-------AAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKK 1378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   500 KAEIMEsikrlypgsvygrlidlcqptQKKYQIAVTKVLGKNmdaiiVDSEKTGRDCIQYIKEQRGEPEtflpldylEVK 579
Cdd:PTZ00121 1379 KADAAK---------------------KKAEEKKKADEAKKK-----AEEDKKKADELKKAAAAKKKAD--------EAK 1424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   580 PTDEKLRELKGAKLVIDVIRYEPPHIKKAlqyacgnalvcdnvEDARRIAFGGHQRHKTVALDGTlfQKSGVISGGASDL 659
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKA--------------EEAKKAEEAKKKAEEAKKADEA--KKKAEEAKKADEA 1488

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   660 KAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLES 739
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   740 ELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEvfeefcREIGVRNIREFEEEKVK----RQNEIAKKRLEFENQKT 815
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE------KKMKAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKE 1642

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   816 RLGIQlDFEKNQLKEDQDKVHMWEQTVKKDEN--EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNhEMEE 893
Cdd:PTZ00121 1643 AEEKK-KAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEE 1720

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   894 IRKKLGGANKEMTHLQKEVTAIETKLEQKRSD---RHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQR-I 969
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKkI 1800

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29336622   970 SSIYAREALIEI--DYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQET 1041
Cdd:PTZ00121 1801 KDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
7-49 1.85e-07

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 54.66  E-value: 1.85e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 29336622    7 IEIENFKSYKGRQII------GPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:COG1106    5 FSIENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFLR 53
PTZ00121 PTZ00121
MAEBL; Provisional
 156-477 1.86e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQlfklyhnevEI 235
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK---------KA 1589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKEntSHKIKKLEAA 315
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEA 1667

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARqefeermeeesqsqgrdltlEENQVKKYHRLKEEASKRAATLAQELEK 395
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE--------------------EAKKAEELKKKEAEEKKKAEELKKAEEE 1727

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   396 fnRDQKADQDRLDLEERKKVETEAKIKqklrEIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK 475
Cdd:PTZ00121 1728 --NKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801


                  ..
gi 29336622   476 EL 477
Cdd:PTZ00121 1802 DI 1803
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 4-65 1.98e-07

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 52.99  E-value: 1.98e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29336622    4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVL-GEKTSNLR-VKTLRDLI 65
Cdd:cd03240    1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKgGAHDPKLI 64
recF PRK00064
recombination protein F; Reviewed
 3-137 2.02e-07

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 54.78  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFvLGeKTSNLRVKTLRDLI-HGAPvgkpaanRAFVS 81
Cdd:PRK00064    2 YLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-PGRSHRTARDKELIrFGAE-------AAVIH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29336622    82 MVYSEEGAEDRTFARVIVGGSSEYKIN-NKVVQLHEYSEEL-------EKLGILIKA----RNFL---VFQ 137
Cdd:PRK00064   72 GRVEKGGRELPLGLEIDKKGGRKVRINgEPQRKLAELAGLLnvvlftpEDLRLVKGGpserRRFLdrlLFQ 142
PRK01156 PRK01156
chromosome segregation protein; Provisional
 4-505 2.19e-07

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 55.29  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     4 LKLIEIENFKSYKGRQIIGPfQRFTAIIGPNGSGKSNLMDAISFVLgekTSNLRVKTLRDLIhgapvgKPAANRAFVSMV 83
Cdd:PRK01156    3 IKRIRLKNFLSHDDSEIEFD-TGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMI------KKGKNNLEVELE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    84 YSEEGAEDRTFARVIVGG-----SSEYKINNKVVQ--LHEYSEELEKLGILIKARNFL----VFQGAVESIAMKNPKERT 152
Cdd:PRK01156   73 FRIGGHVYQIRRSIERRGkgsrrEAYIKKDGSIIAegFDDTTKYIEKNILGISKDVFLnsifVGQGEMDSLISGDPAQRK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   153 ALFEEISRSGELAQEYDKRKKEMvkaeedtqfnyhrkKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLfKLYHNE 232
Cdd:PRK01156  153 KILDEILEINSLERNYDKLKDVI--------------DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEK-SHSITL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   233 VEIEKLNKELASKNKEIEKDKKRMDkvedelkekkkELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKL 312
Cdd:PRK01156  218 KEIERLSIEYNNAMDDYNNLKSALN-----------ELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKII 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   313 EAAKKSLQNAQKHYKKRKGDMDELeKEMLSVEKArqefeermeeesqsqgrdltleenQVKKYHRLKEEASKRAATLAQE 392
Cdd:PRK01156  287 NDPVYKNRNYINDYFKYKNDIENK-KQILSNIDA------------------------EINKYHAIIKKLSVLQKDYNDY 341

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   393 LEKFNRDQKADQDRLDLEerkkvETEAKIKQKLREIEENQKRIEKLEeyittskqslEEQKKLEGELTEEVEMAKRRIDE 472
Cdd:PRK01156  342 IKKKSRYDDLNNQILELE-----GYEMDYNSYLKSIESLKKKIEEYS----------KNIERMSAFISEILKIQEIDPDA 406

                         490       500       510
                  ....*....|....*....|....*....|...
gi 29336622   473 INKELNQVMEQLGDarIDRQESSRQQRKAEIME 505
Cdd:PRK01156  407 IKKELNEINVKLQD--ISSKVSSLNQRIRALRE 437
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
4-510 2.43e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     4 LKLIEIENFKSYKGRQIigpfqRFTA----IIGPNGSGKSNLMDAISFVL-GEKTSNLRVKTLRDLIhgapvgKPAANRA 78
Cdd:PRK03918    3 IEELKIKNFRSHKSSVV-----EFDDginlIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFT------RIGGSGT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    79 FVSMVYSEEGaEDRTFARVIVGGSSEYKINNKVVQLHEYSEEL-EKLGILIKARNFL----VFQGAVESIaMKNPKERTA 153
Cdd:PRK03918   72 EIELKFEKNG-RKYRIVRSFNRGESYLKYLDGSEVLEEGDSSVrEWVERLIPYHVFLnaiyIRQGEIDAI-LESDESREK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   154 LFEEISRSGELAQEYD---KRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRaQVQLQLFKLYH 230
Cdd:PRK03918  150 VVRQILGLDDYENAYKnlgEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP-ELREELEKLEK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   231 NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELkekkkelgkmmreqQQIEKEIKEKDSELNqkrpqyikakentshKIK 310
Cdd:PRK03918  229 EVKELEELKEEIEELEKELESLEGSKRKLEEKI--------------RELEERIEELKKEIE---------------ELE 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   311 KLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKaRQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLA 390
Cdd:PRK03918  280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK-RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   391 QELEKFNrDQKADQDRLD-LEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRR 469
Cdd:PRK03918  359 ERHELYE-EAKAKKEELErLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 29336622   470 IDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:PRK03918  438 CPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 1-99 2.58e-07

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: 52.66  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    1 MGFLKLiEIENFKSYKGRQII----GPFQRFTAIIGPNGSGKSNLMDAISFVL-GEKTSNLRVKTLRDLIHgapvgkPAA 75
Cdd:cd03279    1 MKPLKL-ELKNFGPFREEQVIdftgLDNNGLFLICGPTGAGKSTILDAITYALyGKTPRYGRQENLRSVFA------PGE 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 29336622   76 NRAFVSMVYS----------EEGAEDRTFARVIV 99
Cdd:cd03279   74 DTAEVSFTFQlggkkyrverSRGLDYDQFTRIVL 107
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
333-768 2.99e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.77  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  333 MDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRL---KEEASKRAATLAQELEKFNRD----QKADQD 405
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREEleklEKLLQL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  406 RLDLEERKKVETE--------AKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEG--------ELTEEVEMAKRR 469
Cdd:COG4717  128 LPLYQELEALEAElaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQR 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  470 IDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGknMDAIIVds 549
Cdd:COG4717  208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG--VLFLVL-- 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  550 ektGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYAcgnalvcDNVEDARRIA 629
Cdd:COG4717  284 ---GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL-------DRIEELQELL 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  630 FGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAvDKLKEKKERLtEELKEQMKAKRKEAELRQVQSQAHGLQ 709
Cdd:COG4717  354 REAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEEL-EELEEQLEELLGELEELLEALDEEELE 431

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29336622  710 MRLKYSQSDLEQTKTRHLALnLQEKSKLESELANFGP--RINDIKRIIQSREREMKDLKEK 768
Cdd:COG4717  432 EELEELEEELEELEEELEEL-REELAELEAELEQLEEdgELAELLQELEELKAELRELAEE 491
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
3-65 6.53e-07

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 52.31  E-value: 6.53e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29336622    3 FLKLIEIENFKSYKGRQI-IGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLI 65
Cdd:COG3950    2 RIKSLTIENFRGFEDLEIdFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 1122-1203 6.56e-07

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 51.45  E-value: 6.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1122 FRPMDNLSGGEKTVAALALLFAIHSYKPA--PFFVLDEIDAALDNTNI-GKVANYIKEQ-STCNFQAIVISLKEEFYTKA 1197
Cdd:cd03240  110 LDMRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERkSQKNFQLIVITHDEELVDAA 189


                 ....*.
gi 29336622 1198 ESLIGV 1203
Cdd:cd03240  190 DHIYRV 195
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-510 6.78e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  149 KERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNiaaERKEAKQEKEEA-DRYQRLKDEVVRAQVQLQLFK 227
Cdd:COG4717   53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE---ELEELEEELEELeAELEELREELEKLEKLLQLLP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  228 LYHnevEIEKLNKELASKNKEIEKDKKRMDKVEDelkekkkelgkMMREQQQIEKEIKEKDSELNQ--------KRPQYI 299
Cdd:COG4717  130 LYQ---ELEALEAELAELPERLEELEERLEELRE-----------LEEELEELEAELAELQEELEElleqlslaTEEELQ 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  300 KAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQS------------------- 360
Cdd:COG4717  196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllslilti 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  361 -----------------QGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRL-----DLEERKKVETE 418
Cdd:COG4717  276 agvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldRIEELQELLRE 355

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  419 AKIKQKLREIEENQKRIEKL-EEYITTSKQSLE---EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQES 494
Cdd:COG4717  356 AEELEEELQLEELEQEIAALlAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE 435

                        410
                 ....*....|....*.
gi 29336622  495 SRQQRKAEIMESIKRL 510
Cdd:COG4717  436 ELEEELEELEEELEEL 451
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 281-503 7.70e-07

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 53.90  E-value: 7.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    281 EKEIKEKDSELNQKRPQYIKAKENT--SHKIKKLEAAKKSLQNAQKhykkrkgdMDELEKEMLSVEKARQEFEERMEEES 358
Cdd:TIGR00606  844 KIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQ--------LVELSTEVQSLIREIKDAKEQDSPLE 915

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    359 QSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRL-DLEERKKVETEAKIKQKLREIEENQKRIEK 437
Cdd:TIGR00606  916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIqDGKDDYLKQKETELNTVNAQLEECEKHQEK 995

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29336622    438 LEEYITTSKQSLEEQKKLEGELTEEVEMAKRR--IDEINKELNQVMEQLGDARIDRQESSRQQRKAEI 503
Cdd:TIGR00606  996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENI 1063
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 163-439 8.07e-07

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: 53.59  E-value: 8.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    163 ELAQEYDKRKKeMVKAEEDTQFNYHRKKNIAAERKEAKQEKE-EADRYQRLKDEVVRAQVQLQLFKLYHNEV-EIEKLNK 240
Cdd:pfam17380  307 EKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERErELERIRQEERKRELERIRQEEIAMEISRMrELERLQM 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    241 ELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEiKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKK--S 318
Cdd:pfam17380  386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE-QEEARQREVRRLEEERAREMERVRLEEQERQQQveR 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    319 LQNAQKHYKKRKGDMDELEKEMLSVEKAR-----QEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQ-- 391
Cdd:pfam17380  465 LRQQEEERKRKKLELEKEKRDRKRAEEQRrkileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERrk 544

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 29336622    392 ELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLE 439
Cdd:pfam17380  545 QQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 1119-1188 1.10e-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: 50.67  E-value: 1.10e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29336622 1119 GKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNiGKVA--NYIKE-QSTCNFQAIVIS 1188
Cdd:cd03276  101 KAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN-RKIStdLLVKEaKKQPGRQFIFIT 172
PTZ00121 PTZ00121
MAEBL; Provisional
 156-476 1.42e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQ-EKEEADRYQRLKDEVVRAQVQlQLFKLYHNEVE 234
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIK 1621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQyiKAKENTSHKIKKLEA 314
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEALKKEAE 1699

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   315 AKKSLQNAQKHYKKRKGDMDELEKEMlSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELE 394
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   395 KFNRD--QKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDE 472
Cdd:PTZ00121 1779 AVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNN 1858


                  ....
gi 29336622   473 INKE 476
Cdd:PTZ00121 1859 ENGE 1862
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 1128-1188 1.67e-06

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 49.17  E-value: 1.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29336622 1128 LSGGEKTVAALALLFAihsYKPaPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVIS 1188
Cdd:cd00267   81 LSGGQRQRVALARALL---LNP-DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVT 137
AAA_29 pfam13555
P-loop containing region of AAA domain;
4-49 1.71e-06

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 46.44  E-value: 1.71e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 29336622      4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:pfam13555    1 LTRLQLINWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 27-253 2.24e-06

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: 50.85  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     27 FTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPV--GKPAANRAFVSMVYSEEGAEDRtfarvivGGSSE 104
Cdd:pfam13304    1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGipSLLNGIDPKEPIEFEISEFLED-------GVRYR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    105 YKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAmKNPKERTALFEEISRSGELAqEYDKRKKEMVKAEEDTQF 184
Cdd:pfam13304   74 YGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPP-EAEELRLGLDVEERIELSLS-ELSDLISGLLLLSIISPL 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29336622    185 NYHRKKNIAAeRKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDK 253
Cdd:pfam13304  152 SFLLLLDEGL-LLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRER 219
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 863-1058 2.43e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  863 IDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDiklpl 942
Cdd:COG3883   25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG----- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  943 skGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAE-EEIKQEMNTLQQKLNEQQSVLQRIA 1021
Cdd:COG3883  100 --GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAElEAKLAELEALKAELEAAKAELEAQQ 177

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 29336622 1022 APNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQA 1058
Cdd:COG3883  178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 8-65 5.51e-06

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 47.62  E-value: 5.51e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622    8 EIENF-KSYKGRQIIGPFQ------RFTAIIGPNGSGKSNLMDAISFVL----------GEKTSNLRVKTLRDLI 65
Cdd:cd00267    1 EIENLsFRYGGRTALDNVSltlkagEIVALVGPNGSGKSTLLRAIAGLLkptsgeilidGKDIAKLPLEELRRRI 75
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
156-510 6.90e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 6.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   156 EEISRSGELAQEYDKRKKEMVKAEEdtqfnyhRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEI 235
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEE-------RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   236 EKLNKELAS---KNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKenTSHKIKKL 312
Cdd:PRK03918  387 EKLEKELEElekAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEE--YTAELKRI 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   313 EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEA---SKRAATL 389
Cdd:PRK03918  465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklKGEIKSL 544

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   390 AQELEKFNrDQKADQDRLDLEERKKVETEAKIKQKLRE-----IEENQKRIEKLEEY------ITTSKQSLEEQKKLEGE 458
Cdd:PRK03918  545 KKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKELEPFyneyleLKDAEKELEREEKELKK 623

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 29336622   459 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:PRK03918  624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 275-501 8.24e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.76  E-value: 8.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  275 REQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEK---ARQEFE 351
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQKEEL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  352 ERMEEESQSQGRDLTLEenqvkkyHRLKEEASKRAATLAQELEKFNRDQKADQDRLdleerkkVETEAKIKQKLREIEEN 431
Cdd:COG4942  107 AELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAE 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29336622  432 QKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKA 501
Cdd:COG4942  173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAERTP 244
PTZ00121 PTZ00121
MAEBL; Provisional
 141-926 1.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   141 ESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKdevvraq 220
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIAR------- 1158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   221 vqlqlfklyhnevEIEKLNKELASKNKEiekDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIK 300
Cdd:PTZ00121 1159 -------------KAEDARKAEEARKAE---DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED 1222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   301 AKEntSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSqgrDLTLEENQVKKYHRLKE 380
Cdd:PTZ00121 1223 AKK--AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DELKKAEEKKKADEAKK 1297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   381 EASKRAATLAQEleKFNRDQKADQDRLDLEERKKVETEAKIKQ---------KLREIEENQKRIEKLEEYITTSKQSLEE 451
Cdd:PTZ00121 1298 AEEKKKADEAKK--KAEEAKKADEAKKKAEEAKKKADAAKKKAeeakkaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   452 QKKLEGELTEEVEmAKRRIDEINK---ELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDlcqPTQK 528
Cdd:PTZ00121 1376 AKKKADAAKKKAE-EKKKADEAKKkaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD---EAKK 1451

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   529 KyqiavtkvlgknmdaiiVDSEKTGRDCIQYIKEQRGEPEtfLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKA 608
Cdd:PTZ00121 1452 K-----------------AEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   609 lqyacgnalvcDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKEQ 688
Cdd:PTZ00121 1513 -----------DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK---KAEEKKKAEEAKKAEEDKNM 1578

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   689 mkAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHlalnlQEKSKLESELANfgpRINDIKRIIQSREREMKDLKEK 768
Cdd:PTZ00121 1579 --ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKK 1648

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   769 MNQVEDEvfEEFCREIGVRNIREFEEEkvKRQNEIAKKRLEFENQKtrlgiqldfeKNQLKEDQDKVHMWEQTVKKDENE 848
Cdd:PTZ00121 1649 AEELKKA--EEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKA----------AEALKKEAEEAKKAEELKKKEAEE 1714

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   849 I---EKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKN---HEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQK 922
Cdd:PTZ00121 1715 KkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794


                  ....
gi 29336622   923 RSDR 926
Cdd:PTZ00121 1795 EVDK 1798
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
5-479 1.60e-05

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 49.35  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    5 KLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRdlIHGAPVGKPAA----NRAFV 80
Cdd:COG4694    4 KIKKLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFE--IEAGGSAPNPSvrvfNRDFV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   81 SM-VYSEEGAEDrtfaRVIVGGSS---EYKINNKVVQLHEYSEELEKLGILIKARNflvfqGAVESIAMKNPKERTALFE 156
Cdd:COG4694   82 EEnLRSGEEIKG----IFTLGEENielEEEIEELEKEIEDLKKELDKLEKELKEAK-----KALEKLLEDLAKSIKDDLK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  157 EISRSGElaQEYDKRK-KEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADrYQRLKDEVVRAQVQLQlfklyhnEVEI 235
Cdd:COG4694  153 KLFASSG--RNYRKANlEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITP-LPDLKALLSEAETLLE-------KSAV 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  236 EKLNKELASKNKEIEKD------KKRMDKVEdelkekkkelgkmmRE-----QQQIEKEIKEK-DSELNQkrpQYIKAKE 303
Cdd:COG4694  223 SSAIEELAALIQNPGNSdwveqgLAYHKEEE--------------DDtcpfcQQELAAERIEAlEAYFDD---EYEKLLA 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  304 NTSHKIKKLEAAKKSL-----QNAQKHYKKRKGDMDELEKEMLS-VEKARQEFEERMEEESQSQGRDLTLEENQVKKyhr 377
Cdd:COG4694  286 ALKDLLEELESAINALsalllEILRTLLPSAKEDLKAALEALNAlLETLLAALEEKIANPSTSIDLDDQELLDELND--- 362

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  378 LKEEASKRAATLAQELEKFnrDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEG 457
Cdd:COG4694  363 LIAALNALIEEHNAKIANL--KAEKEEARKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEA 440

                        490       500
                 ....*....|....*....|..
gi 29336622  458 ELTEEVEMAkrriDEINKELNQ 479
Cdd:COG4694  441 ELSSVDEAA----DEINEELKA 458
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
 24-124 2.00e-05

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 47.97  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   24 FQR-FTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKT--LRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVI-V 99
Cdd:cd03241   19 FEEgLTVLTGETGAGKSILLDALSLLLGGRASADLIRSgaEKAVVEGVFDISDEEEAKALLLELGIEDDDDLIIRREIsR 98

                         90       100
                 ....*....|....*....|....*
gi 29336622  100 GGSSEYKINNKVVQLHEYSEELEKL 124
Cdd:cd03241   99 KGRSRYFINGQSVTLKLLRELGSLL 123
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 231-469 2.28e-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: 48.22  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  231 NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRpqyikakentshkiK 310
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------------K 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  311 KLEAAKKSLQNAQKHYKK------RKGDMDELeKEMLSVEKARQEFEERMEEESQSQGRdltleENQVKKYHRLKEEASK 384
Cdd:COG4942   91 EIAELRAELEAQKEELAEllralyRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPAR-----REQAEELRADLAELAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  385 RAATLAQE---LEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTE 461
Cdd:COG4942  165 LRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244


                 ....*...
gi 29336622  462 EVEMAKRR 469
Cdd:COG4942  245 AAGFAALK 252
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 676-1095 2.51e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.56  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    676 EKKERLTEELKEQMKAKRKEAELRQVQSQAHglQMRLKYSQSDLEQTKTRhlALNLQEKSKLESElanfgprinDIKRII 755
Cdd:pfam05483  222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEK--ENKMKDLTFLLEESRDK--ANQLEEKTKLQDE---------NLKELI 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    756 QSRE---REMKDLKEKMNQ-VEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKR-------LEFENQKTRLGIQLDFE 824
Cdd:pfam05483  289 EKKDhltKELEDIKMSLQRsMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTE 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    825 KNQLKEDQDKVHMWEQTVKKDENEIEKLkkeeqrhMKIIDETMAQLQDLKNQhLAKKSEVNDKNHEMEEIRKKLGGANKE 904
Cdd:pfam05483  369 QQRLEKNEDQLKIITMELQKKSSELEEM-------TKFKNNKEVELEELKKI-LAEDEKLLDEKKQFEKIAEELKGKEQE 440

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    905 MTHL----QKEVTAIETKLEQKRSDRHNLLQacKMQDIKLPLSKGTMDDISQEEGSsqgeDSVSGSQRISSIYAREALIE 980
Cdd:pfam05483  441 LIFLlqarEKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNIELTAHC----DKLLLENKELTQEASDMTLE 514

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    981 IDYGDlcEDLKDAQAEEE-IKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAF 1059
Cdd:pfam05483  515 LKKHQ--EDIINCKKQEErMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 29336622   1060 EQikkeRFDRFNACFESVATNIDEIY---KALSRNSSAQ 1095
Cdd:pfam05483  593 EN----KCNNLKKQIENKNKNIEELHqenKALKKKGSAE 627
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 7-46 2.69e-05

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 47.00  E-value: 2.69e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 29336622    7 IEIEN-FKSYKGRQIIG------PFQRFTAIIGPNGSGKSNLMDAIS 46
Cdd:COG4604    2 IEIKNvSKRYGGKVVLDdvsltiPKGGITALIGPNGAGKSTLLSMIS 48
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 7-65 2.98e-05

ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213243 [Multi-domain]  Cd Length: 198  Bit Score: 46.44  E-value: 2.98e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29336622    7 IEIENFKSYKGRQI-IGPfqRFTAIIGPNGSGKSNLMDAISFVLGEKTSNL-RVKTLRDLI 65
Cdd:cd03276    4 ITLKNFMCHRHLQIeFGP--RVNFIVGNNGSGKSAILTALTIGLGGKASDTnRGSSLKDLI 62
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 281-502 4.52e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 4.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  281 EKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEK---ARQEFEERMEEE 357
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  358 SQSQGRDLTLEENQVkkyhrlkeeASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEK 437
Cdd:COG3883   95 LYRSGGSVSYLDVLL---------GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622  438 LEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAE 502
Cdd:COG3883  166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 276-511 4.88e-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: 47.81  E-value: 4.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    276 EQQQIEKEIKEKDSELNQKRPqyIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERME 355
Cdd:pfam17380  297 EQERLRQEKEEKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEI 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    356 EESQSQGRdLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRI 435
Cdd:pfam17380  375 SRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRL 453

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29336622    436 EKLE--EYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDrQESSRQQRKAEIMESIKRLY 511
Cdd:pfam17380  454 EEQErqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIY 530
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 660-928 5.01e-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: 47.81  E-value: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    660 KAKARRWDEKAVDKLKEKKERL-TEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLE 738
Cdd:pfam17380  282 KAVSERQQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    739 SElanfgprindikriiQSREREMKDLKEKMNQVEDEVFEefcreigvrniREFEEEKVKRQNEIAKKRLEFENQKTRLG 818
Cdd:pfam17380  362 LE---------------RIRQEEIAMEISRMRELERLQME-----------RQQKNERVRQELEAARKVKILEEERQRKI 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    819 IQLDFEKNQLKEDQDKVHMWEQTVKKDEN--EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRK 896
Cdd:pfam17380  416 QQQKVEMEQIRAEQEEARQREVRRLEEERarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 29336622    897 KLggaNKEMTHLQKEVTAIETK---LEQKRSDRHN 928
Cdd:pfam17380  496 IL---EKELEERKQAMIEEERKrklLEKEMEERQK 527
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 2-67 5.07e-05

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 45.66  E-value: 5.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29336622    2 GFLKLIEIENFKSYkGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNL-RVKTLRDLI-HG 67
Cdd:cd03277    1 GSIVRIKLENFVTY-DETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLgRAKKVGEFVkRG 67
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 113-510 5.26e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.81  E-value: 5.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    113 QLHEYSEELEKLGILIKARNFLVfQGAVES--IAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKk 190
Cdd:pfam15921  420 ELDDRNMEVQRLEALLKAMKSEC-QGQMERqmAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT- 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    191 niAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYH----------NEVEIEKLNKELASKNKEIEKDKKRMDKVE 260
Cdd:pfam15921  498 --VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknegdhlrnVQTECEALKLQMAEKDKVIEILRQQIENMT 575

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    261 DELKEKKKELGKMMREQQQIEKEIKEKDSELNqkrpQYIKAKENTSHKIKKLEA-------AKKSLQNAQKHYKKRKGDM 333
Cdd:pfam15921  576 QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ----EFKILKDKKDAKIRELEArvsdlelEKVKLVNAGSERLRAVKDI 651

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    334 DELEKEMLSVEKarqefeermeeESQSQGRDLTLEENQVKKYHRLK-EEASKRAATLAQELEKFNRDQKADQDRLDLEE- 411
Cdd:pfam15921  652 KQERDQLLNEVK-----------TSRNELNSLSEDYEVLKRNFRNKsEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEg 720

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    412 ------RKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQS----LEEQKKLEGEL----TEEVEMA----------- 466
Cdd:pfam15921  721 sdghamKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhflKEEKNKLSQELstvaTEKNKMAgelevlrsqer 800

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 29336622    467 --KRRIDEINKELNQVMEQLGDAR--IDRQESSRQQRKAEIMESIKRL 510
Cdd:pfam15921  801 rlKEKVANMEVALDKASLQFAECQdiIQRQEQESVRLKLQHTLDVKEL 848
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4-510 6.29e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    4 LKLIEIENFKSYKGRQIIGPfQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKtlrdlihgapVGKPAANRAFVSMV 83
Cdd:COG4717    3 IKELEIYGFGKFRDRTIEFS-PGLNVIYGPNEAGKSTLLAFIRAMLLERLEKEADE----------LFKPQGRKPELNLK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   84 YSEEGAEDRTFARvivggSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGE 163
Cdd:COG4717   72 ELKELEEELKEAE-----EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  164 LAQEYDKRKKEMVKAEEDtqfnyhrkknIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELA 243
Cdd:COG4717  147 RLEELEERLEELRELEEE----------LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  244 SKNKEIEKDKKRMDKVEDElkekkkelgkmmREQQQIEKEIKEKDSELN--------QKRPQYIKAKENTSHKIKKLEAA 315
Cdd:COG4717  217 EAQEELEELEEELEQLENE------------LEAAALEERLKEARLLLLiaaallalLGLGGSLLSLILTIAGVLFLVLG 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEE-----NQVKKYHRLKEEASKRAATLa 390
Cdd:COG4717  285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllellDRIEELQELLREAEELEEEL- 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  391 qELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEEnqkRIEKLEEYITTSKQSLEEQKKL--EGELTEEVEMAKR 468
Cdd:COG4717  364 -QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE---ELEELEEQLEELLGELEELLEAldEEELEEELEELEE 439

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 29336622  469 RIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:COG4717  440 ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 413-519 6.60e-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: 46.68  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  413 KKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVmeqlgDARIDRQ 492
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----EKEIAEL 95

                         90       100
                 ....*....|....*....|....*..
gi 29336622  493 ESSRQQRKAEIMESIKRLYPGSVYGRL 519
Cdd:COG4942   96 RAELEAQKEELAELLRALYRLGRQPPL 122
PRK12704 PRK12704
phosphodiesterase; Provisional
 273-395 6.62e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   273 MMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEE 352
Cdd:PRK12704   66 IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 29336622   353 RMEEESQSQGRDLTLEEnqvkkyhrLKEEASKRAATLAQELEK 395
Cdd:PRK12704  146 RISGLTAEEAKEILLEK--------VEEEARHEAAVLIKEIEE 180
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 371-511 7.04e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  371 QVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQK---------LREIEENQKRIEKLEEY 441
Cdd:COG1579   32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRISDLEDE 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  442 ITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLgDARIDRQESSRQQRKAEIMESIKRLY 511
Cdd:COG1579  112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL-EAELEELEAEREELAAKIPPELLALY 180
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
371-510 1.05e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  371 QVKKYHRLKEEASKRAATLAQELEKFnrdQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE 450
Cdd:COG4913  236 DLERAHEALEDAREQIELLEPIRELA---ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29336622  451 EQKKLEGELTEEVEMAKRRIDEI-NKELNQVMEQLGDARIDRQEssRQQRKAEIMESIKRL 510
Cdd:COG4913  313 RLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEE--RERRRARLEALLAAL 371
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
 3-90 1.05e-04

recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273173 [Multi-domain]  Cd Length: 365  Bit Score: 46.19  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622      3 FLKLIEIENFKSYKgrQIIGPFQ-RFTAIIGPNGSGKSNLMDAIsFVLGEkTSNLRVKTLRDLI-HGAPvgkpaanRAFV 80
Cdd:TIGR00611    2 YLSRLELTDFRNYD--AVDLELSpGVNVIVGPNGQGKTNLLEAI-YYLAL-GRSHRTSRDKPLIrFGAE-------AFVI 70

                           90
                   ....*....|
gi 29336622     81 SMVYSEEGAE 90
Cdd:TIGR00611   71 EGRVSKGDRE 80
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 6-46 1.13e-04

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 45.42  E-value: 1.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 29336622    6 LIEIENFK-SYKGRQIIGP--FQ----RFTAIIGPNGSGKSNLMDAIS 46
Cdd:COG1120    1 MLEAENLSvGYGGRPVLDDvsLSlppgEVTALLGPNGSGKSTLLRALA 48
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 1121-1174 1.22e-04

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 44.89  E-value: 1.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29336622 1121 RFRPMDNL--------SGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYI 1174
Cdd:cd03277  112 KFREGEQLqeldphhqSGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDML 173
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 1110-1208 1.30e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 44.24  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1110 GINYncVAPGkrfRPMDNLSGGEKTVAALALLFAIHSykPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISL 1189
Cdd:cd03238   75 GLGY--LTLG---QKLSTLSGGELQRVKLASELFSEP--PGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147

                         90
                 ....*....|....*....
gi 29336622 1190 KEEFYTKAESLIGVYPEQG 1208
Cdd:cd03238  148 NLDVLSSADWIIDFGPGSG 166
PRK12704 PRK12704
phosphodiesterase; Provisional
 377-509 1.57e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   377 RLKEEASKRAATLAQELEkfnRDQKadqdrlDLEERKKVETEAKIKQKLREIEENQKRIEKLEE-------YITTSKQSL 449
Cdd:PRK12704   42 RILEEAKKEAEAIKKEAL---LEAK------EEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrkleLLEKREEEL 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622   450 EEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLG-----DARIDRQESSRQQRKAEIMESIKR 509
Cdd:PRK12704  113 EKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeEAKEILLEKVEEEARHEAAVLIKE 177
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 150-500 1.75e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 46.19  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   150 ERTALFEEISRSGELaQEYDKRKKEMVKaeEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLY 229
Cdd:PTZ00108 1012 SNKVRFIKHVINGEL-VITNAKKKDLVK--ELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSY 1088

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   230 H----------NEVEIEKLNKELASKNKEIEKDKKRmdkvedelkekkkELGKM-MREQQQIEKEIKEKDSELNQKRPQY 298
Cdd:PTZ00108 1089 DyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNT-------------TPKDMwLEDLDKFEEALEEQEEVEEKEIAKE 1155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   299 IKAKENTSHKIKKLeaAKKSLQNAQKhyKKRKGDMDELEKEMLSVEKARQEFEERMEEESQ-------SQGRDLTLEENQ 371
Cdd:PTZ00108 1156 QRLKSKTKGKASKL--RKPKLKKKEK--KKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKpdnkksnSSGSDQEDDEEQ 1231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   372 VKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEE 451
Cdd:PTZ00108 1232 KTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVK 1311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 29336622   452 QKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRK 500
Cdd:PTZ00108 1312 KRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKK 1360
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 690-921 1.96e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  690 KAKRKEAELRQVQSQahglqmrLKYSQSDLEQTKtrhlalnlQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKM 769
Cdd:COG4942   21 AAAEAEAELEQLQQE-------IAELEKELAALK--------KEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  770 NQVEDEvfeefcreigvrnIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEI 849
Cdd:COG4942   86 AELEKE-------------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29336622  850 EKLKKE-------EQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQ 921
Cdd:COG4942  153 EELRADlaelaalRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
336-485 2.04e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.62  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  336 LEKEMlsvEKARQEFEERMEEESQSQGRDLTLEENQVKKY----HRLKEEASKRAATLAqELEKFNRDQKADQDRLDLEE 411
Cdd:COG2433  382 LEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLeeqvERLEAEVEELEAELE-EKDERIERLERELSEARSEE 457

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622  412 RKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKE-LNQVMEQLG 485
Cdd:COG2433  458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEaIRRLEEEYG 532
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 840-1072 2.08e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  840 QTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKL 919
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  920 EQKRSDRHNLLQACKMQdiklplskGTMDDISQEEGSSQGEDSVSGSQRISSIY-AREALIEiDYGDLCEDLKDAQAE-E 997
Cdd:COG4942  100 EAQKEELAELLRALYRL--------GRQPPLALLLSPEDFLDAVRRLQYLKYLApARREQAE-ELRADLAELAALRAElE 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622  998 EIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNA 1072
Cdd:COG4942  171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 8-46 2.60e-04

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 43.19  E-value: 2.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 29336622    8 EIEN-FKSYKGRQIIGPFQ------RFTAIIGPNGSGKSNLMDAIS 46
Cdd:cd03214    1 EVENlSVGYGGRTVLDDLSlsieagEIVGILGPNGAGKSTLLKTLA 46
COG4938 COG4938
Predicted ATPase [General function prediction only];
7-49 2.65e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443965 [Multi-domain]  Cd Length: 277  Bit Score: 44.19  E-value: 2.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 29336622    7 IEIENFKSYKGRQIigPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:COG4938    4 ISIKNFGPFKEAEL--ELKPLTLLIGPNGSGKSTLIQALLLLL 44
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 378-508 3.68e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   378 LKEEASKRA-ATLAQELEKFNR-DQKADQDRLDLEERKKvETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEqkkl 455
Cdd:PRK00409  499 LPENIIEEAkKLIGEDKEKLNElIASLEELERELEQKAE-EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK---- 573

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 29336622   456 egELTEEVEMAKRRIDEINKELNQvMEQLGDARIDRQESSRQQRK----AEIMESIK 508
Cdd:PRK00409  574 --EAQQAIKEAKKEADEIIKELRQ-LQKGGYASVKAHELIEARKRlnkaNEKKEKKK 627
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
 4-75 3.75e-04

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: 43.83  E-value: 3.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29336622    4 LKLIEIENFKSYKGRQIigPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTsnLRVKTLRDLIHgapVGKPAA 75
Cdd:cd03242    1 LKSLELRNFRNYAELEL--EFePGVTVLVGENAQGKTNLLEAISLLATGKS--HRTSRDKELIR---WGAEEA 66
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 166-475 4.51e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.71  E-value: 4.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    166 QEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQrlkdEVVRAQVQLQLFKLYHNEVEIEKLNKELASK 245
Cdd:pfam05483  387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA----EELKGKEQELIFLLQAREKEIHDLEIQLTAI 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    246 NKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKH 325
Cdd:pfam05483  463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    326 YKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQD 405
Cdd:pfam05483  543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    406 RLDLEERKKVETEAKIKQKLREIEENQkriEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK 475
Cdd:pfam05483  623 KGSAENKQLNAYEIKVNKLELELASAK---QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
PRK01156 PRK01156
chromosome segregation protein; Provisional
 647-1213 4.93e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.51  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   647 QKSGVISGGASDLKAKARRWDE--KAVDKLKEKKERLTEELK--EQMKAKRKEAELRQVQSQAHgLQMRLKYSQSDLEQT 722
Cdd:PRK01156  329 KKLSVLQKDYNDYIKKKSRYDDlnNQILELEGYEMDYNSYLKsiESLKKKIEEYSKNIERMSAF-ISEILKIQEIDPDAI 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   723 KTRHLALNlQEKSKLESELANFGPRINDIkriiqsREREMkDLKEKMNQVEDEVFEEFCR----EIGVRNIRE------- 791
Cdd:PRK01156  408 KKELNEIN-VKLQDISSKVSSLNQRIRAL------RENLD-ELSRNMEMLNGQSVCPVCGttlgEEKSNHIINhynekks 479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   792 -FEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMA-Q 869
Cdd:PRK01156  480 rLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlK 559

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   870 LQDL--KNQHLAKKSEVNDkNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRS-----------------DRHNLL 930
Cdd:PRK01156  560 LEDLdsKRTSWLNALAVIS-LIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidksireieneannlnNKYNEI 638

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   931 QACKMQDIKLplsKGTMDDISQEegsSQGEDSVSGSQriSSIYAREALIEIDYGDLCEDLKDAQAE--------EEIKQE 1002
Cdd:PRK01156  639 QENKILIEKL---RGKIDNYKKQ---IAEIDSIIPDL--KEITSRINDIEDNLKKSRKALDDAKANrarlestiEILRTR 710

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  1003 MNTLQQKLNEQQSVLQRiaapnMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVatNID 1082
Cdd:PRK01156  711 INELSDRINDINETLES-----MKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKYLFEFNLDFDDI--DVD 783

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  1083 EIYK-ALSRNSSAQAflgpenpeepyldginyncvapgkrfrpMDNLSGGEKTVAALALLFAIHSY--KPAPFFVLDEID 1159
Cdd:PRK01156  784 QDFNiTVSRGGMVEG----------------------------IDSLSGGEKTAVAFALRVAVAQFlnNDKSLLIMDEPT 835

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 29336622  1160 AALDN---TNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVIS 1213
Cdd:PRK01156  836 AFLDEdrrTNLKDIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSKVI 892
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-80 5.25e-04

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 43.15  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    1 MGFLKLIEIEN--FkSYKGRQII---------GpfqRFTAIIGPNGSGKSNLMDAIsfvLGE-KTSNLRVKtlrdlIHGA 68
Cdd:COG1121    1 MMMMPAIELENltV-SYGGRPVLedvsltippG---EFVAIVGPNGAGKSTLLKAI---LGLlPPTSGTVR-----LFGK 68

                         90
                 ....*....|..
gi 29336622   69 PVGKPAANRAFV 80
Cdd:COG1121   69 PPRRARRRIGYV 80
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 235-502 5.27e-04

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: 44.44  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQiekeikEKDsELNQKRPQYIKAKENtshKIKKLEA 314
Cdd:pfam12128  620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS------EKD-KKNKALAERKDSANE---RLNSLEA 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    315 AKKSLQNAQKHYKKR-KGDMDELEKEMLSVEKArqefeermeeesqsqgrdltLEENQVKKYHRLKEEASKRAATLAQEL 393
Cdd:pfam12128  690 QLKQLDKKHQAWLEEqKEQKREARTEKQAYWQV--------------------VEGALDAQLALLKAAIAARRSGAKAEL 749

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    394 EKFNRDQKADQDRLDLEErkkvETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE-LTEEVEMAKRRIDE 472
Cdd:pfam12128  750 KALETWYKRDLASLGVDP----DVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPrLATQLSNIERAISE 825

                          250       260       270
                   ....*....|....*....|....*....|
gi 29336622    473 INKELNQVMEqlgDARIDRQESSRQQRKAE 502
Cdd:pfam12128  826 LQQQLARLIA---DTKLRRAKLEMERKASE 852
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
279-510 6.29e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   279 QIE-KEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQ---KHYKKRKGDMDELEKEMLSV-EKARQEFEER 353
Cdd:PRK02224  195 QIEeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLrETIAETERER 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   354 MEEESQSQGRDLTLEEnqvkkyhrLKEEASKRAATLAQElekfNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQK 433
Cdd:PRK02224  275 EELAEEVRDLRERLEE--------LEEERDDLLAEAGLD----DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   434 RIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKR-------RIDEINKELNQVMEQLGDARIDRQES-----SRQQRKA 501
Cdd:PRK02224  343 EAESLREDADDLEERAEELREEAAELESELEEAREavedrreEIEELEEEIEELRERFGDAPVDLGNAedfleELREERD 422


                  ....*....
gi 29336622   502 EIMESIKRL 510
Cdd:PRK02224  423 ELREREAEL 431
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 7-46 6.73e-04

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 41.28  E-value: 6.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 29336622    7 IEIENF-KSYKGRQIIGPFqRFT-------AIIGPNGSGKSNLMDAIS 46
Cdd:cd03221    1 IELENLsKTYGGKLLLKDI-SLTinpgdriGLVGRNGAGKSTLLKLIA 47
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
657-878 7.48e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 7.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  657 SDLKAKARRWDEKAVDKlkekkeRLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNlQEKSK 736
Cdd:COG4913  255 EPIRELAERYAAARERL------AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR-EELDE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  737 LESELANF-GPRINDIKRIIQSREREMKDLKEKMNQvedevFEEFCREIGVrnirefeeekvkrqnEIAKKRLEFENQKT 815
Cdd:COG4913  328 LEAQIRGNgGDRLEQLEREIERLERELEERERRRAR-----LEALLAALGL---------------PLPASAEEFAALRA 387

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29336622  816 RLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKE----EQRHMKiIDETMAQLQDLKNQHL 878
Cdd:COG4913  388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslERRKSN-IPARLLALRDALAEAL 453
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 391-510 7.95e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 7.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  391 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE---------LTE 461
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQK 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 29336622  462 EVEMAKRRIDEINKELNQVMEQLGDAR--IDRQESSRQQRKAEIMESIKRL 510
Cdd:COG1579   97 EIESLKRRISDLEDEILELMERIEELEeeLAELEAELAELEAELEEKKAEL 147
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 118-462 8.21e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 43.69  E-value: 8.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   118 SEELEKLGILiKARNFLVFQGA--VESIAMKNPKERTALFeeiSRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAE 195
Cdd:PLN03229  390 TEELLKHRML-KFRKIGGFQEGvpVDPERKVNMKKREAVK---TPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIE 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   196 R--KEAKQEKEEA-------DRYQRLKDEVVRAQVQLQLFklyhNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEK 266
Cdd:PLN03229  466 KlkKEIDLEYTEAviamglqERLENLREEFSKANSQDQLM----HPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLN 541

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   267 KKELGKMMREQQQIEKEIKekdSELNQKRPQYIKAKEntshkIK-KLEAAKKSLQNaQKHYKKrkGDMDELEKEmlSVEK 345
Cdd:PLN03229  542 EFSRAKALSEKKSKAEKLK---AEINKKFKEVMDRPE-----IKeKMEALKAEVAS-SGASSG--DELDDDLKE--KVEK 608

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   346 ARQEFEERMEEESQSQGRDL-------------TLEENQVKKYHRLKEEASK------RAATLAQELEKFNRDQKADQDR 406
Cdd:PLN03229  609 MKKEIELELAGVLKSMGLEVigvtkknkdtaeqTPPPNLQEKIESLNEEINKkierviRSSDLKSKIELLKLEVAKASKT 688

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 29336622   407 LDLEERKKVET-EAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:PLN03229  689 PDVTEKEKIEAlEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKND 745
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 193-434 8.62e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 8.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  193 AAERKEAKQEKEEadryqrlkdevVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGK 272
Cdd:COG4942   19 ADAAAEAEAELEQ-----------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  273 MMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKI----KKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQ 348
Cdd:COG4942   88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  349 EFEERMEEESQsqgrdltLEENQVKKYHRLKEEASKRAATLAQelekFNRDQKADQDRLDLEERKKVETEAKIKQKLREI 428
Cdd:COG4942  168 ELEAERAELEA-------LLAELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEA 236


                 ....*.
gi 29336622  429 EENQKR 434
Cdd:COG4942  237 AAAAER 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
672-931 1.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   672 DKLKEKKERLTEELKEqmkAKRKEAELRQVQSQAHGLQMRLKysqsDLEQTKTRhlalnlqekskleselanfgprINDI 751
Cdd:PRK03918  193 ELIKEKEKELEEVLRE---INEISSELPELREELEKLEKEVK----ELEELKEE----------------------IEEL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   752 KRIIQSREREMKDLKEKMNQVEDEVFEEfcreigVRNIREFeEEKVKRQNEIAKKRLEFENQKtRLGIQLDFEKNQLKED 831
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIRELEERIEEL------KKEIEEL-EEKVKELKELKEKAEEYIKLS-EFYEEYLDELREIEKR 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   832 QDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKsEVNDKNHEMEEIRKKLGGANKEmtHLQKE 911
Cdd:PRK03918  316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKE 392

                         250       260
                  ....*....|....*....|
gi 29336622   912 VTAIETKLEQKRSDRHNLLQ 931
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITA 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
793-1022 1.64e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  793 EEEKVKRQNEIAKKRLEFENQKTRLGIqLDFEKNQLK--EDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQL 870
Cdd:COG4913  247 AREQIELLEPIRELAERYAAARERLAE-LEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  871 QDLKNQHLAkksevndknhemeeirkkLGGANKEmtHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDI 950
Cdd:COG4913  326 DELEAQIRG------------------NGGDRLE--QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29336622  951 SQEegssqgedsvsGSQRISSIYAREALIEIDYGDLCEDLKDAQAE-EEIKQEMNTLQQ-KLN---EQQSVLQRIAA 1022
Cdd:COG4913  386 RAE-----------AAALLEALEEELEALEEALAEAEAALRDLRRElRELEAEIASLERrKSNipaRLLALRDALAE 451
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 3-54 1.83e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 42.20  E-value: 1.83e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 29336622      3 FLKLIEIENFKSYKGRQIigPFQ-RFTAIIGPNGSGKSNLMDAISFVLGEKTS 54
Cdd:pfam13175    2 KIKSIIIKNFRCLKDTEI--DLDeDLTVLIGKNNSGKSSILEALDIFLNNKEK 52
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
679-876 1.94e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  679 ERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSR 758
Cdd:COG4717   49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  759 E--REMKDLKEKMNQVEDEVfEEFCREIgvRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQldfEKNQLKEDQDKVH 836
Cdd:COG4717  129 PlyQELEALEAELAELPERL-EELEERL--EELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELE 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 29336622  837 MWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQ 876
Cdd:COG4717  203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 27-45 1.95e-03

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 40.98  E-value: 1.95e-03
                         10
                 ....*....|....*....
gi 29336622   27 FTAIIGPNGSGKSNLMDAI 45
Cdd:cd03235   27 FLAIVGPNGAGKSTLLKAI 45
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 195-477 2.20e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    195 ERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMM 274
Cdd:TIGR04523  402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    275 REQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERM 354
Cdd:TIGR04523  482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    355 EEESQSQgrdltlEENQVKKYHRLKEEASKRAATLAQELEKfnrdqkaDQDRLDLEERKKVETEAKIKQKLREIEENQKR 434
Cdd:TIGR04523  562 EIDEKNK------EIEELKQTQKSLKKKQEEKQELIDQKEK-------EKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 29336622    435 IEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKEL 477
Cdd:TIGR04523  629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
26-46 2.25e-03

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 41.25  E-value: 2.25e-03
                         10        20
                 ....*....|....*....|.
gi 29336622   26 RFTAIIGPNGSGKSNLMDAIS 46
Cdd:COG4559   28 ELTAIIGPNGAGKSTLLKLLT 48
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 379-510 2.88e-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: 41.67  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  379 KEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 458
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622  459 LT---------------------EEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKAEIMESIKRL 510
Cdd:COG4942  109 LLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRAdlAELAALRAELEAERAELEALLAEL 183
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 27-46 2.94e-03

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 40.88  E-value: 2.94e-03
                         10        20
                 ....*....|....*....|
gi 29336622   27 FTAIIGPNGSGKSNLMDAIS 46
Cdd:cd03219   28 IHGLIGPNGAGKTTLFNLIS 47
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 708-921 3.12e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    708 LQMRLKYSQsdleqtKTRHLALNLQEKSKLESELANfgpriNDIKRIIQSREREMKDLKEKMNQVEDEVfeefcreigvR 787
Cdd:pfam07888   32 LQNRLEECL------QERAELLQAQEAANRQREKEK-----ERYKRDREQWERQRRELESRVAELKEEL----------R 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    788 NIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETM 867
Cdd:pfam07888   91 QSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 29336622    868 AQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQ 921
Cdd:pfam07888  171 AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 8-46 3.29e-03

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 40.23  E-value: 3.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 29336622    8 EIENFKSYKGRQII----GPFQ--RFTAIIGPNGSGKSNLMDAIS 46
Cdd:cd03213   12 TVKSSPSKSGKQLLknvsGKAKpgELTAIMGPSGAGKSTLLNALA 56
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 666-931 3.73e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.63  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    666 WDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAhgLQMRLKYSQSDLEQTKTRHLalnlQEKSKLESELANFG 745
Cdd:pfam05483  422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA--IKTSEEHYLKEVEDLKTELE----KEKLKNIELTAHCD 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    746 PRINDIKRIIQSREREMKDLKekmNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEK 825
Cdd:pfam05483  496 KLLLENKELTQEASDMTLELK---KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE 572

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    826 NQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEM 905
Cdd:pfam05483  573 ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKF 652

                          250       260
                   ....*....|....*....|....*.
gi 29336622    906 THLqkeVTAIETKLEQKRSDRHNLLQ 931
Cdd:pfam05483  653 EEI---IDNYQKEIEDKKISEEKLLE 675
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 16-498 4.09e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 4.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     16 KGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLgekTSNLRVKTLRD-LIHGAPVGKPAANRAFVSMVYSEEGAEDRTF 94
Cdd:TIGR00606   19 KDKQIIDFFSPLTILVGPNGAGKTTIIECLKYIC---TGDFPPGTKGNtFVHDPKVAQETDVRAQIRLQFRDVNGEECAV 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     95 ARVIVGGS----SEYKINNKVVQLHEYSEE--------------LEKLGILIKARNFLVFQGAVESI-AMKNPKERTALF 155
Cdd:TIGR00606   96 VRSMVCTQktkkTEFKTLEGVITRYKHGEKvslsskcaeidremISHLGVSKAVLNNVIFCHQEDSNwPLSEGKALKQKF 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    156 EEISRSGELAQEYDKRKK------EMVKAEEDTQFNYHRKKNIAAERKE---AKQEKEEADRYQRLKDEVVRAQVQLQLF 226
Cdd:TIGR00606  176 DEIFSATRYIKALETLRQvrqtqgQKVQEHQMELKYLKQYKEKACEIRDqitSKEAQLESSREIVKSYENELDPLKNRLK 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    227 KLYHNEVEIEKLNKELA---SKNKEIEKDKKRMDkvedelkekkkelGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE 303
Cdd:TIGR00606  256 EIEHNLSKIMKLDNEIKalkSRKKQMEKDNSELE-------------LKMEKVFQGTDEQLNDLYHNHQRTVREKERELV 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    304 NTSHKIKKLEAAKKSLQNAQKHYKKRKGDM----DELEKEMLSVEKARQEFEERMEEESQSQGRDLtleENQVKKYHRLK 379
Cdd:TIGR00606  323 DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFS---ERQIKNFHTLV 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    380 EEA-SKRAATLAQELEKFNRDQKADQDRLDLEE-----------------RKKVETEAKIKQKLREIEENQKRIEKLEEY 441
Cdd:TIGR00606  400 IERqEDEAKTAAQLCADLQSKERLKQEQADEIRdekkglgrtielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQE 479

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29336622    442 ITTSKQSL---EEQKKLEGELTEEVEMAKRRIDEINK--ELNQVMEQLgdariDRQESSRQQ 498
Cdd:TIGR00606  480 LRKAERELskaEKNSLTETLKKEVKSLQNEKADLDRKlrKLDQEMEQL-----NHHTTTRTQ 536
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 187-319 4.22e-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: 40.29  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  187 HRKKNIAAERKEAKQEKEEA-DRYQRLKDEVVRAQVQLQLFKLYHNEVE--IEKL---------NKELASKNKEIEKDKK 254
Cdd:COG1579   24 HRLKELPAELAELEDELAALeARLEAAKTELEDLEKEIKRLELEIEEVEarIKKYeeqlgnvrnNKEYEALQKEIESLKR 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29336622  255 RMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSL 319
Cdd:COG1579  104 RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 362-502 4.77e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.14  E-value: 4.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    362 GRDLTLEENQVKKYHRLKEEASKRAATLAQELEKfnrdqkaDQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY 441
Cdd:pfam05262  191 EKGVNFRRDMTDLKERESQEDAKRAQQLKEELDK-------KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKP 263

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29336622    442 ITTskQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKAE 502
Cdd:pfam05262  264 ADT--SSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKEL 324
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
679-1178 4.82e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  679 ERLTEELKEqmkAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLAL--------NLQEKSKLESELANFGPRIND 750
Cdd:COG4717   74 KELEEELKE---AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllqllpLYQELEALEAELAELPERLEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  751 IKRIIQSREREMKDLKEKMNQVED--EVFEEFCREIGVRNIREFEEeKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQL 828
Cdd:COG4717  151 LEERLEELRELEEELEELEAELAElqEELEELLEQLSLATEEELQD-LAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  829 KEDQDKVHMWEQTVKKDENEI----------------------------------------EKLKKEEQRHMKIIDETma 868
Cdd:COG4717  230 EQLENELEAAALEERLKEARLllliaaallallglggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEEL-- 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  869 qlqdlknQHLAKKSEVNDKnhEMEEIRKKLG----GANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSK 944
Cdd:COG4717  308 -------QALPALEELEEE--ELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  945 GTMDDISQ-EEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAP 1023
Cdd:COG4717  379 AGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEL 458

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1024 N------------MKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNAcfesvatNIDEIYKALSRN 1091
Cdd:COG4717  459 EaeleqleedgelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLE-------RASEYFSRLTDG 531

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622 1092 SSAQAFLgpenPEEPYLDGINYNCvapgkRFRPMDNLSGGEKTVAALALLFA-IHSYKPAPF-FVLDEIDAALDNTNIGK 1169
Cdd:COG4717  532 RYRLIRI----DEDLSLKVDTEDG-----RTRPVEELSRGTREQLYLALRLAlAELLAGEPLpLILDDAFVNFDDERLRA 602


                 ....*....
gi 29336622 1170 VANYIKEQS 1178
Cdd:COG4717  603 ALELLAELA 611
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 313-510 5.03e-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: 41.26  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    313 EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRdLTLEENQ----VKKYHRLKEEASKRAAT 388
Cdd:pfam17380  291 EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERelerIRQEERKRELERIRQEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    389 LAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREiEENQKRIekleeyittsKQSLEEQKKLEGELTEEVEMAKR 468
Cdd:pfam17380  370 IAMEISRMRELERLQMERQQKNERVRQELEAARKVKILE-EERQRKI----------QQQKVEMEQIRAEQEEARQREVR 438

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 29336622    469 RIDEinkELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:pfam17380  439 RLEE---ERAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 28-501 5.86e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.98  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     28 TAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAF---------VSMVYSEEGAEDRTFARVI 98
Cdd:pfam12128   20 TNICGTNAAGKTTLLRLLPLFYGEYPSRIVPGTDRDSFEDYYLPRDSSYIVYeyqrpdgqlCMAVLHSNGDGKGVQYRFI 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622     99 VGGSSE---YKINNKVVQLHEYSE---ELEKLGIlikARNFLVFQGAVESIAMKnpkERTALFEEISRSGELAQEYDKRK 172
Cdd:pfam12128  100 AGGYRLddfIKANNDFVKCETVAElgrFMKNAGI---QRTNLLNTREYRSIIQN---DRTLLGRERVELRSLARQFALCD 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    173 KE--------MVKAEEDTQFNYHRKKNIAAER--------KEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE-I 235
Cdd:pfam12128  174 SEsplrhidkIAKAMHSKEGKFRDVKSMIVAIleddgvvpPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNtL 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMReqqQIEKEIKEKDSELNQkrpqyikakentshkikKLEAA 315
Cdd:pfam12128  254 ESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLR---TLDDQWKEKRDELNG-----------------ELSAA 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLT-LEENQVK---KYHRLKEEASKRAATLAQ 391
Cdd:pfam12128  314 DAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKaLTGKHQDvtaKYNRRRSKIKEQNNRDIA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    392 ELEKFNRDQKADQDRLDLEERKKVEteaKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRID 471
Cdd:pfam12128  394 GIKDKLAKIREARDRQLAVAEDDLQ---ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFD 470

                          490       500       510
                   ....*....|....*....|....*....|
gi 29336622    472 EinkELNQVMEQLGDARIDRQESSRQQRKA 501
Cdd:pfam12128  471 E---RIERAREEQEAANAEVERLQSELRQA 497
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 227-509 6.21e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    227 KLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTS 306
Cdd:TIGR04523   90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    307 HKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKE------ 380
Cdd:TIGR04523  170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktteis 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    381 EASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKriEKLEEYITTSKQSLEEQKKLEGELT 460
Cdd:TIGR04523  250 NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQ 327

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 29336622    461 EEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQ-QRKAEIMESIKR 509
Cdd:TIGR04523  328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRElEEKQNEIEKLKK 377
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
668-923 6.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 6.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   668 EKAVDKLKEKKERLTE----ELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQS------DLEQTKTRHLALN------L 731
Cdd:PRK03918  227 EKEVKELEELKEEIEElekeLESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSefyeeyL 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   732 QEKSKLESELANFGPRINDIKRIIQ---SREREMKDLKEKMNQVEDEVfeefcreigvrnirEFEEEKVKRQNEIAKKRL 808
Cdd:PRK03918  307 DELREIEKRLSRLEEEINGIEERIKeleEKEERLEELKKKLKELEKRL--------------EELEERHELYEEAKAKKE 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622   809 EFENQKTRLGiqlDFEKNQLKEDQDKVhmwEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLA--------- 879
Cdd:PRK03918  373 ELERLKKRLT---GLTPEKLEKELEEL---EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelt 446

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 29336622   880 ---KKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKR 923
Cdd:PRK03918  447 eehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 380-487 6.54e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.05  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622  380 EEASKRAATLAQELEKFNRDQKADQDRLDLEERK---KVETEAKIKQKlREIEENQKRIEKL-EEYITTSKQSLEEQKKL 455
Cdd:cd22656  131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKAlkdLLTDEGGAIAR-KEIKDLQKELEKLnEEYAAKLKAKIDELKAL 209

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 29336622  456 EGELTEEVEMAKR---RIDEINKELNQVMEQLGDA 487
Cdd:cd22656  210 IADDEAKLAAALRliaDLTAADTDLDNLLALIGPA 244
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 28-46 7.55e-03

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 39.75  E-value: 7.55e-03
                          10
                  ....*....|....*....
gi 29336622    28 TAIIGPNGSGKSNLMDAIS 46
Cdd:PRK13548   31 VAILGPNGAGKSTLLRALS 49
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
28-49 7.74e-03

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 39.14  E-value: 7.74e-03
                          10        20
                  ....*....|....*....|..
gi 29336622    28 TAIIGPNGSGKSNLMDAISFVL 49
Cdd:NF040873   21 TAVVGPNGSGKSTLLKVLAGVL 42
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 277-947 7.87e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    277 QQQIEKEIKEKDSELNQKRPQYIKAKENTSHK---------IKKLEAAKKSLQNAQKHYKKRkgdMDELEKEMLSVEKAR 347
Cdd:pfam15921  110 QSVIDLQTKLQEMQMERDAMADIRRRESQSQEdlrnqlqntVHELEAAKCLKEDMLEDSNTQ---IEQLRKMMLSHEGVL 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    348 QEFEERMEEESQSQGRDLTLEENQVKKYHR-LKEEASKRAATLAQELEKFNRDQKADQDRLdleERKKVETEAKIKQKLr 426
Cdd:pfam15921  187 QEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKILRELDTEISYLKGRIFPVEDQL---EALKSESQNKIELLL- 262

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    427 eiEENQKRIEKLEEyittskqslEEQKKLEGeLTEEVEMAKRRIDEINKELNQVMEQLGDA------RIDRQESSRQQRK 500
Cdd:pfam15921  263 --QQHQDRIEQLIS---------EHEVEITG-LTEKASSARSQANSIQSQLEIIQEQARNQnsmymrQLSDLESTVSQLR 330

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    501 AEIMESiKRLYPGSVY---GRLI----DLCQPTQKKYQIAV-TKVLGKNMDAIIVDSEKTGRDcIQYIKEQRgepETFLP 572
Cdd:pfam15921  331 SELREA-KRMYEDKIEeleKQLVlansELTEARTERDQFSQeSGNLDDQLQKLLADLHKREKE-LSLEKEQN---KRLWD 405

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    573 LDYLEVKPTDEKLRELKGAKLviDVIRYEPphIKKALQYACGN------ALVCDNVEDARRIAFGGHQRHKT-------- 638
Cdd:pfam15921  406 RDTGNSITIDHLRRELDDRNM--EVQRLEA--LLKAMKSECQGqmerqmAAIQGKNESLEKVSSLTAQLESTkemlrkvv 481

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    639 ---VALDGTLFQKSGVISGGASDLKAKARRWdEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYS 715
Cdd:pfam15921  482 eelTAKKMTLESSERTVSDLTASLQEKERAI-EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEK 560

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    716 QSDLEQTKT-------------RHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEF-C 781
Cdd:pfam15921  561 DKVIEILRQqienmtqlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVnA 640

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    782 REIGVRNIREFEEEKVKRQNEIAKKRLE--------------FENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDEN 847
Cdd:pfam15921  641 GSERLRAVKDIKQERDQLLNEVKTSRNElnslsedyevlkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG 720

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29336622    848 EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRH 927
Cdd:pfam15921  721 SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800

                          730       740
                   ....*....|....*....|
gi 29336622    928 NLLQacKMQDIKLPLSKGTM 947
Cdd:pfam15921  801 RLKE--KVANMEVALDKASL 818
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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