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Conserved domains on  [gi|613410199|ref|NP_683515|]
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structural maintenance of chromosomes protein 1B isoform 1 [Homo sapiens]

Protein Classification

chromosome segregation SMC family protein( domain architecture ID 11439815)

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

Gene Ontology:  GO:0003682|GO:0005524|GO:0016887|GO:0051301|GO:0007076|GO:0003677
PubMed:  14660695

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 3-1206 1.04e-106

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


The actual alignment was detected with superfamily member pfam02463:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1161  Bit Score: 363.91  E-value: 1.04e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199     3 HLELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIA-NLRVKNIQELIHgaHIGKPISSSASVK 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    82 IIYVEESGEEKT-------FARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKPKERTQF 154
Cdd:pfam02463   79 ITFDNEDHELPIdkeevsiRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   155 FEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQLFQLYHNEKK 234
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   235 IHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDV 314
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   315 AKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLE 394
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   395 KLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVN 474
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   475 EELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVFGRLFDLCHPIHKKYQLAVTKVFGRFITAIVVASEKVAK 554
Cdd:pfam02463  479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   555 DCIRFLKEERAEPETFLALDYLDIKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCETMEEARHIALSGpE 634
Cdd:pfam02463  559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK-L 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   635 RQKTVALDGTLFLKSGVISGGSSDLKYKARcwdekelknlrdrrsqkiqelkglMKTLRKETDLKQIQTLIQGTQTRLKY 714
Cdd:pfam02463  638 KESAKAKESGLRKGVSLEEGLAEKSEVKAS------------------------LSELTKELLEIQELQEKAESELAKEE 693

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   715 SQNELEMIKKKhlvafyqEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQhfCEEIGVENIREFEN 794
Cdd:pfam02463  694 ILRRQLEIKKK-------EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE--EEEKSRLKKEEKEE 764

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   795 KHVKRQQEIDQKRLEFEKQKTRLNVQLEYsrshlKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLK 874
Cdd:pfam02463  765 EKSELSLKEKELAEEREKTEKLKVEEEKE-----EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   875 dirvtQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNLLLDCKVQDIEIILLSGSLDDIIEVE 954
Cdd:pfam02463  840 -----LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   955 MGTEAESTQATIDIYekeeafEIDYSSLKEDLKALQSDQEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKF 1034
Cdd:pfam02463  915 KENEIEERIKEEAEI------LLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEE 988

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1035 QESTDAFEASRKEARLCRQEFEQVKKRRYDLFTQCFEHVSISIDQIYKKLCRNNSAQAFLSPENPEEPYLEGISYNCVAP 1114
Cdd:pfam02463  989 RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPP 1068

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1115 GKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTqDQFQMIVISLKEEFYSRAD 1194
Cdd:pfam02463 1069 GKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS-KNAQFIVISLREEMLEKAD 1147

                         1210
                   ....*....|..
gi 613410199  1195 ALIGIYPEYDDC 1206
Cdd:pfam02463 1148 KLVGVTMVENGV 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 ...
 3-1206 1.04e-106

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 363.91  E-value: 1.04e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199     3 HLELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIA-NLRVKNIQELIHgaHIGKPISSSASVK 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    82 IIYVEESGEEKT-------FARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKPKERTQF 154
Cdd:pfam02463   79 ITFDNEDHELPIdkeevsiRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   155 FEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQLFQLYHNEKK 234
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   235 IHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDV 314
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   315 AKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLE 394
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   395 KLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVN 474
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   475 EELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVFGRLFDLCHPIHKKYQLAVTKVFGRFITAIVVASEKVAK 554
Cdd:pfam02463  479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   555 DCIRFLKEERAEPETFLALDYLDIKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCETMEEARHIALSGpE 634
Cdd:pfam02463  559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK-L 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   635 RQKTVALDGTLFLKSGVISGGSSDLKYKARcwdekelknlrdrrsqkiqelkglMKTLRKETDLKQIQTLIQGTQTRLKY 714
Cdd:pfam02463  638 KESAKAKESGLRKGVSLEEGLAEKSEVKAS------------------------LSELTKELLEIQELQEKAESELAKEE 693

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   715 SQNELEMIKKKhlvafyqEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQhfCEEIGVENIREFEN 794
Cdd:pfam02463  694 ILRRQLEIKKK-------EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE--EEEKSRLKKEEKEE 764

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   795 KHVKRQQEIDQKRLEFEKQKTRLNVQLEYsrshlKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLK 874
Cdd:pfam02463  765 EKSELSLKEKELAEEREKTEKLKVEEEKE-----EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   875 dirvtQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNLLLDCKVQDIEIILLSGSLDDIIEVE 954
Cdd:pfam02463  840 -----LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   955 MGTEAESTQATIDIYekeeafEIDYSSLKEDLKALQSDQEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKF 1034
Cdd:pfam02463  915 KENEIEERIKEEAEI------LLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEE 988

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1035 QESTDAFEASRKEARLCRQEFEQVKKRRYDLFTQCFEHVSISIDQIYKKLCRNNSAQAFLSPENPEEPYLEGISYNCVAP 1114
Cdd:pfam02463  989 RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPP 1068

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1115 GKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTqDQFQMIVISLKEEFYSRAD 1194
Cdd:pfam02463 1069 GKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS-KNAQFIVISLREEMLEKAD 1147

                         1210
                   ....*....|..
gi 613410199  1195 ALIGIYPEYDDC 1206
Cdd:pfam02463 1148 KLVGVTMVENGV 1159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-1199 4.27e-90

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: 316.62  E-value: 4.27e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199     3 HLELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEK-IANLRVKNIQELIHGAHIGKPiSSSASVK 81
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSsSKAMRAERLSDLISNGKNGQS-GNEAYVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    82 IIYVEESGEEKTFARIIR-------GGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNcLVFQGTVESISVKKPKERTQF 154
Cdd:TIGR02169   80 VTFKNDDGKFPDELEVVRrlkvtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYN-VVLQGDVTDFISMSPVERRKI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   155 FEEISTsgelIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQA----KLEKEEAERYQSLLEELkmnkiqlQLFQLYH 230
Cdd:TIGR02169  159 IDEIAG----VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERYQALLKEK-------REYEGYE 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   231 NEKKIHLLNTKLEHVNRDLSVKRESLSHhenivkarkkehgmLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLK 310
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEK--------------LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   311 KldvakkSIKDSEKQCSKQEDDIKALETELADLDAAwrsfEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMT 390
Cdd:TIGR02169  294 E------KIGELEAEIASLERSIAEKERELEDAEER----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   391 QQLEKLQ------------WEQKTDEERLAFE--KRRHGEVQGNLK--------------QIKEQIEDHKKRIEKLEEYT 442
Cdd:TIGR02169  364 EELEDLRaeleevdkefaeTRDELKDYREKLEklKREINELKRELDrlqeelqrlseelaDLNAAIAGIEAKINELEEEK 443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   443 KTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAG--IDTHEGKRQQKRAEVL-----EHLKRLYPDSV 515
Cdd:TIGR02169  444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQreLAEAEAQARASEERVRggravEEVLKASIQGV 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   516 FGRLFDLCHpIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLRELKGC-KMV 594
Cdd:TIGR02169  524 HGTVAQLGS-VGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGViGFA 602

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   595 IDVIKTQfPQLKKVIQFVCGNGLVCETMEEARhiALSGPERqkTVALDGTLFLKSGVISGGSsdLKYKARCWDEKELKNL 674
Cdd:TIGR02169  603 VDLVEFD-PKYEPAFKYVFGDTLVVEDIEAAR--RLMGKYR--MVTLEGELFEKSGAMTGGS--RAPRGGILFSRSEPAE 675

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   675 RDRRSQKIQELKGLMKTLRKETD-----LKQIQTLIQGTQTRLKYSQNELEMIKKKH------LVAFYQEQSQLQSELLN 743
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRrienrLDELSQELSDASRKIGEIEKEIEQLEQEEeklkerLEELEEDLSSLEQEIEN 755

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   744 IESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHFCEEIGVEnIREFENKHvkrqQEIDQKRLEFEKQKTRLNVQLEY 823
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE-LSKLEEEV----SRIEARLREIEQKLNRLTLEKEY 830

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   824 SRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLkdirvtqnssaEKVQTQIEEERKKflaVDR 903
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL-----------ESRLGDLKKERDE---LEA 896

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   904 EVGKLQKEVVSIQTSLEQKRLekhnLLLDCKVQdieiillsgslddiievemgteAESTQATIDIYEKEEAFEIDYSSLK 983
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRK----RLSELKAK----------------------LEALEEELSEIEDPKGEDEEIPEEE 950

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   984 EDLKALQSD-QEIEAHLRLLlqqvasqEDIllktaapNLRALENLKTV---RDKFQESTDAFEASRKEARLCRQEFEQVK 1059
Cdd:TIGR02169  951 LSLEDVQAElQRVEEEIRAL-------EPV-------NMLAIQEYEEVlkrLDELKEKRAKLEEERKAILERIEEYEKKK 1016

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1060 KrryDLFTQCFEHVSISIDQIYKKLcrnNSAQAFLSPENPEEPYLEGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFA 1139
Cdd:TIGR02169 1017 R---EVFMEAFEAINENFNEIFAEL---SGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFA 1090

                         1210      1220      1230      1240      1250      1260
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1140 VHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQfQMIVISLKEEFYSRADALIGI 1199
Cdd:TIGR02169 1091 IQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEA-QFIVVSLRSPMIEYADRAIGV 1149
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 4-148 7.99e-80

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: 262.12  E-value: 7.99e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAHIGKPISSSASVKII 83
Cdd:cd03275     1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199   84 YVEESGEEKTFARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKP 148
Cdd:cd03275    81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-771 8.76e-46

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 179.75  E-value: 8.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    3 HLELLLVENFKSWRGRQVIgPFRR-FTCIIGPNGSGKSNVMDALSFVMGE-KIANLRVKNIQELIH-GAHIGKPiSSSAS 79
Cdd:COG1196     2 RLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFaGSSSRKP-LGRAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   80 VKIIYVEESG------EEKTFARII-RGGCSEFRFNDNLVSRSVyIAEL-EKIGIIVKAQNcLVFQGTVESISVKKPKER 151
Cdd:COG1196    80 VSLTFDNSDGtlpidyDEVTITRRLyRSGESEYYINGKPCRLKD-IQDLfLDTGLGPESYS-IIGQGMIDRIIEAKPEER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  152 TQFFEEIStsGelIGEYEEKK----RKLQKAEEdaqfNFNKKKNIAAE--RRQAKLEK--EEAERYQSLLEELKMNKIQL 223
Cdd:COG1196   158 RAIIEEAA--G--ISKYKERKeeaeRKLEATEE----NLERLEDILGEleRQLEPLERqaEKAERYRELKEELKELEAEL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  224 QLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKE 303
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  304 NTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVR 383
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  384 KKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEI 463
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  464 EKTKSRMSEVNEELNLI-----RSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVFGRLFDLchpihKKYQLAVTKVF 538
Cdd:COG1196   470 EEAALLEAALAELLEELaeaaaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE-----AAYEAALEAAL 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  539 GRFITAIVVASEKVAKDCIRFLKEERAEPETFLALD----YLDIKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCG 614
Cdd:COG1196   545 AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  615 NGLVCETMEEARHIALSGPERQKTVALDGTLFLKSGVISGGSSDLKYKARcwdEKELKNLRDRRSQKIQELKGLMKTLRK 694
Cdd:COG1196   625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL---LEAEAELEELAERLAEEELELEEALLA 701

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199  695 ETDLKQIQTLIQGTQTRLKYSQNELEMIKKKHLVAFYQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDK 771
Cdd:COG1196   702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 513-628 8.61e-27

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: 106.16  E-value: 8.61e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    513 DSVFGRLFDLCHpIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPI-NERLRELK-- 589
Cdd:smart00968    1 PGVLGRVADLIS-VDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPaGSKLREALlp 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 613410199    590 ---GCKMVIDVIKTQfPQLKKVIQFVCGNGLVCETMEEARHI 628
Cdd:smart00968   80 epgFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
PTZ00121 PTZ00121
MAEBL; Provisional
 145-509 2.20e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.55  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  145 VKKPKERTQFFEEISTSGELIGEYEEKKRKL----QKAEEDAQFNFNKKKniAAERRQA---KLEKEEAERYQSLLEELK 217
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakKKAEEKKKADEAKKK--AEEAKKAdeaKKKAEEAKKAEEAKKKAE 1467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  218 MNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEK-----ELKSVETLln 292
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakkadEAKKAEEK-- 1545

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  293 QKRPQYIKAKE-NTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSfEKQIEEEILHKKRDIELEASQ 371
Cdd:PTZ00121 1546 KKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEE 1624

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  372 LDRYKELK---EQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDC 448
Cdd:PTZ00121 1625 LKKAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199  449 LKEKKQQEEtlvdeiEKTKSRMSEVNEELNLIRSElqNAGIDTHEGKRQQKRAEVLEHLKR 509
Cdd:PTZ00121 1705 EELKKKEAE------EKKKAEELKKAEEENKIKAE--EAKKEAEEDKKKAEEAKKDEEEKK 1757
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 153-405 1.09e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  153 QFFEEISTSGELIGEYE------EKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAeryqslleELKMNKIQLQLF 226
Cdd:NF033838  129 QFKKDTLEPGKKVAEATkkveeaEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--------ELELVKEEAKEP 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  227 QlyhNEKKIHLLNTKLEHvnrdlsvKRESLSHHENIVKARKKEHGMLTRQLQQTEKEL--KSVETLLNQKRPQYIK---- 300
Cdd:NF033838  201 R---DEEKIKQAKAKVES-------KKAEATRLEKIKTDREKAEEEAKRRADAKLKEAveKNVATSEQDKPKRRAKrgvl 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  301 -------AKENTSHHL-----------------KKLDVAKKSIKDSEKQCSKQEDD---------IKALETELADLDAAW 347
Cdd:NF033838  271 gepatpdKKENDAKSSdssvgeetlpspslkpeKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntYKTLELEIAESDVKV 350

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199  348 RSFEKQIEEEILHKKRDIEleasqldRYKELKEQVRKKVATMTqQLEKLQWEQKTDEE 405
Cdd:NF033838  351 KEAELELVKEEAKEPRNEE-------KIKQAKAKVESKKAEAT-RLEKIKTDRKKAEE 400
 
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 ...
 3-1206 1.04e-106

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 363.91  E-value: 1.04e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199     3 HLELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIA-NLRVKNIQELIHgaHIGKPISSSASVK 81
Cdd:pfam02463    1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    82 IIYVEESGEEKT-------FARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKPKERTQF 154
Cdd:pfam02463   79 ITFDNEDHELPIdkeevsiRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   155 FEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQLFQLYHNEKK 234
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   235 IHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDV 314
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   315 AKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLE 394
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   395 KLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVN 474
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   475 EELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVFGRLFDLCHPIHKKYQLAVTKVFGRFITAIVVASEKVAK 554
Cdd:pfam02463  479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   555 DCIRFLKEERAEPETFLALDYLDIKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCETMEEARHIALSGpE 634
Cdd:pfam02463  559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK-L 637

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   635 RQKTVALDGTLFLKSGVISGGSSDLKYKARcwdekelknlrdrrsqkiqelkglMKTLRKETDLKQIQTLIQGTQTRLKY 714
Cdd:pfam02463  638 KESAKAKESGLRKGVSLEEGLAEKSEVKAS------------------------LSELTKELLEIQELQEKAESELAKEE 693

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   715 SQNELEMIKKKhlvafyqEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQhfCEEIGVENIREFEN 794
Cdd:pfam02463  694 ILRRQLEIKKK-------EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE--EEEKSRLKKEEKEE 764

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   795 KHVKRQQEIDQKRLEFEKQKTRLNVQLEYsrshlKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLK 874
Cdd:pfam02463  765 EKSELSLKEKELAEEREKTEKLKVEEEKE-----EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   875 dirvtQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNLLLDCKVQDIEIILLSGSLDDIIEVE 954
Cdd:pfam02463  840 -----LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   955 MGTEAESTQATIDIYekeeafEIDYSSLKEDLKALQSDQEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKF 1034
Cdd:pfam02463  915 KENEIEERIKEEAEI------LLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEE 988

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1035 QESTDAFEASRKEARLCRQEFEQVKKRRYDLFTQCFEHVSISIDQIYKKLCRNNSAQAFLSPENPEEPYLEGISYNCVAP 1114
Cdd:pfam02463  989 RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPP 1068

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1115 GKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTqDQFQMIVISLKEEFYSRAD 1194
Cdd:pfam02463 1069 GKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS-KNAQFIVISLREEMLEKAD 1147

                         1210
                   ....*....|..
gi 613410199  1195 ALIGIYPEYDDC 1206
Cdd:pfam02463 1148 KLVGVTMVENGV 1159
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-1199 4.27e-90

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: 316.62  E-value: 4.27e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199     3 HLELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEK-IANLRVKNIQELIHGAHIGKPiSSSASVK 81
Cdd:TIGR02169    1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSsSKAMRAERLSDLISNGKNGQS-GNEAYVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    82 IIYVEESGEEKTFARIIR-------GGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNcLVFQGTVESISVKKPKERTQF 154
Cdd:TIGR02169   80 VTFKNDDGKFPDELEVVRrlkvtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYN-VVLQGDVTDFISMSPVERRKI 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   155 FEEISTsgelIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQA----KLEKEEAERYQSLLEELkmnkiqlQLFQLYH 230
Cdd:TIGR02169  159 IDEIAG----VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERYQALLKEK-------REYEGYE 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   231 NEKKIHLLNTKLEHVNRDLSVKRESLSHhenivkarkkehgmLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLK 310
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEK--------------LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   311 KldvakkSIKDSEKQCSKQEDDIKALETELADLDAAwrsfEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMT 390
Cdd:TIGR02169  294 E------KIGELEAEIASLERSIAEKERELEDAEER----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   391 QQLEKLQ------------WEQKTDEERLAFE--KRRHGEVQGNLK--------------QIKEQIEDHKKRIEKLEEYT 442
Cdd:TIGR02169  364 EELEDLRaeleevdkefaeTRDELKDYREKLEklKREINELKRELDrlqeelqrlseelaDLNAAIAGIEAKINELEEEK 443

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   443 KTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAG--IDTHEGKRQQKRAEVL-----EHLKRLYPDSV 515
Cdd:TIGR02169  444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQreLAEAEAQARASEERVRggravEEVLKASIQGV 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   516 FGRLFDLCHpIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLRELKGC-KMV 594
Cdd:TIGR02169  524 HGTVAQLGS-VGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGViGFA 602

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   595 IDVIKTQfPQLKKVIQFVCGNGLVCETMEEARhiALSGPERqkTVALDGTLFLKSGVISGGSsdLKYKARCWDEKELKNL 674
Cdd:TIGR02169  603 VDLVEFD-PKYEPAFKYVFGDTLVVEDIEAAR--RLMGKYR--MVTLEGELFEKSGAMTGGS--RAPRGGILFSRSEPAE 675

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   675 RDRRSQKIQELKGLMKTLRKETD-----LKQIQTLIQGTQTRLKYSQNELEMIKKKH------LVAFYQEQSQLQSELLN 743
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRrienrLDELSQELSDASRKIGEIEKEIEQLEQEEeklkerLEELEEDLSSLEQEIEN 755

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   744 IESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHFCEEIGVEnIREFENKHvkrqQEIDQKRLEFEKQKTRLNVQLEY 823
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE-LSKLEEEV----SRIEARLREIEQKLNRLTLEKEY 830

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   824 SRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLkdirvtqnssaEKVQTQIEEERKKflaVDR 903
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL-----------ESRLGDLKKERDE---LEA 896

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   904 EVGKLQKEVVSIQTSLEQKRLekhnLLLDCKVQdieiillsgslddiievemgteAESTQATIDIYEKEEAFEIDYSSLK 983
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRK----RLSELKAK----------------------LEALEEELSEIEDPKGEDEEIPEEE 950

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   984 EDLKALQSD-QEIEAHLRLLlqqvasqEDIllktaapNLRALENLKTV---RDKFQESTDAFEASRKEARLCRQEFEQVK 1059
Cdd:TIGR02169  951 LSLEDVQAElQRVEEEIRAL-------EPV-------NMLAIQEYEEVlkrLDELKEKRAKLEEERKAILERIEEYEKKK 1016

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1060 KrryDLFTQCFEHVSISIDQIYKKLcrnNSAQAFLSPENPEEPYLEGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFA 1139
Cdd:TIGR02169 1017 R---EVFMEAFEAINENFNEIFAEL---SGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFA 1090

                         1210      1220      1230      1240      1250      1260
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1140 VHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQfQMIVISLKEEFYSRADALIGI 1199
Cdd:TIGR02169 1091 IQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEA-QFIVVSLRSPMIEYADRAIGV 1149
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 4-148 7.99e-80

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: 262.12  E-value: 7.99e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAHIGKPISSSASVKII 83
Cdd:cd03275     1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199   84 YVEESGEEKTFARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKP 148
Cdd:cd03275    81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-1199 5.40e-78

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: 281.17  E-value: 5.40e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    12 FKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGE-KIANLRVKNIQELIHGAHIGKPISSSASVKIIYVEESGE 90
Cdd:TIGR02168   10 FKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEqSAKALRGGKMEDVIFNGSETRKPLSLAEVELVFDNSDGL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    91 EKTFA--------RIIRGGCSEFRFNDNLVsRSVYIAEL--------EKIGIIVkaqnclvfQGTVESISVKKPKERTQF 154
Cdd:TIGR02168   90 LPGADyseisitrRLYRDGESEYFINGQPC-RLKDIQDLfldtglgkRSYSIIE--------QGKISEIIEAKPEERRAI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   155 FEEisTSGelIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAE--RRQAKLEK--EEAERYQSLLEELKMNKIQLQLFQLYH 230
Cdd:TIGR02168  161 FEE--AAG--ISKYKERRKETERKLERTRENLDRLEDILNEleRQLKSLERqaEKAERYKELKAELRELELALLVLRLEE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   231 NEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLK 310
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   311 KLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeilhKKRDIELEASQLDRYKELKEQVRKKVATMT 390
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE----LEAELEELESRLEELEEQLETLRSKVAQLE 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   391 QQLEKLQWEQKTDEERLAFEKRRHG----EVQGNLKQIKE-QIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEK 465
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRErlqqEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEE 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   466 TKSRMSEVNEELNLIRSELQN-AGIDTHEGKRQQKRAEVLEHLKRLypDSVFGRLFDLCHpIHKKYQLAVTKVFGRFITA 544
Cdd:TIGR02168  473 AEQALDAAERELAQLQARLDSlERLQENLEGFSEGVKALLKNQSGL--SGILGVLSELIS-VDEGYEAAIEAALGGRLQA 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   545 IVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPIN----ERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCE 620
Cdd:TIGR02168  550 VVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQgndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   621 TMEEARHIALSGPERQKTVALDGTLFLKSGVISGGSSdlkykarcwdekELKNLRDRRSQKIQELKGLMKTLrkETDLKQ 700
Cdd:TIGR02168  630 DLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSA------------KTNSSILERRREIEELEEKIEEL--EEKIAE 695

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   701 IQTLIQGTQTRLKYSQNELEMIKKKhLVAFYQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHF 780
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   781 ceeigvENIREFENKHVKRQQEIDQKRLEFEKQKTRLnvqleysrshlKKKLNKINTLKETIQKGSEDIDHLKKAEENCL 860
Cdd:TIGR02168  775 ------EELAEAEAEIEELEAQIEQLKEELKALREAL-----------DELRAELTLLNEEAANLRERLESLERRIAATE 837

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   861 QTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNLLLDCKVQDIEI 940
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   941 ILLSGSLDDIIEVEMGTEAEstqatidIYEKEEAFEIDYSSLKEDLKALQSD-----QEIEAHLRLLLQQVASQEDIllk 1015
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVR-------IDNLQERLSEEYSLTLEEAEALENKieddeEEARRRLKRLENKIKELGPV--- 987

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1016 taapNLRALENLKTVRDKF----QESTDAFEASRKEARLCRQEFEQVKKRrydlFTQCFEHVSISIDQIYKKLCRNNSAQ 1091
Cdd:TIGR02168  988 ----NLAAIEEYEELKERYdfltAQKEDLTEAKETLEEAIEEIDREARER----FKDTFDQVNENFQRVFPKLFGGGEAE 1059

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  1092 -AFLSPENPEEpylEGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYI 1170
Cdd:TIGR02168 1060 lRLTDPEDLLE---AGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLL 1136

                         1210      1220
                   ....*....|....*....|....*....
gi 613410199  1171 KEQTqDQFQMIVISLKEEFYSRADALIGI 1199
Cdd:TIGR02168 1137 KEFS-KNTQFIVITHNKGTMEVADQLYGV 1164
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
 1113-1216 6.25e-65

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: 220.14  E-value: 6.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1113 APGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSR 1192
Cdd:cd03275   145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFSK 224

                          90       100
                  ....*....|....*....|....
gi 613410199 1193 ADALIGIYPEYdDCMFSRVLTLDL 1216
Cdd:cd03275   225 ADALVGVYRDQ-ECNSSKVLTLDL 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-771 8.76e-46

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 179.75  E-value: 8.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    3 HLELLLVENFKSWRGRQVIgPFRR-FTCIIGPNGSGKSNVMDALSFVMGE-KIANLRVKNIQELIH-GAHIGKPiSSSAS 79
Cdd:COG1196     2 RLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFaGSSSRKP-LGRAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   80 VKIIYVEESG------EEKTFARII-RGGCSEFRFNDNLVSRSVyIAEL-EKIGIIVKAQNcLVFQGTVESISVKKPKER 151
Cdd:COG1196    80 VSLTFDNSDGtlpidyDEVTITRRLyRSGESEYYINGKPCRLKD-IQDLfLDTGLGPESYS-IIGQGMIDRIIEAKPEER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  152 TQFFEEIStsGelIGEYEEKK----RKLQKAEEdaqfNFNKKKNIAAE--RRQAKLEK--EEAERYQSLLEELKMNKIQL 223
Cdd:COG1196   158 RAIIEEAA--G--ISKYKERKeeaeRKLEATEE----NLERLEDILGEleRQLEPLERqaEKAERYRELKEELKELEAEL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  224 QLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKE 303
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  304 NTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVR 383
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  384 KKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEI 463
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  464 EKTKSRMSEVNEELNLI-----RSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVFGRLFDLchpihKKYQLAVTKVF 538
Cdd:COG1196   470 EEAALLEAALAELLEELaeaaaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE-----AAYEAALEAAL 544

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  539 GRFITAIVVASEKVAKDCIRFLKEERAEPETFLALD----YLDIKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCG 614
Cdd:COG1196   545 AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  615 NGLVCETMEEARHIALSGPERQKTVALDGTLFLKSGVISGGSSDLKYKARcwdEKELKNLRDRRSQKIQELKGLMKTLRK 694
Cdd:COG1196   625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL---LEAEAELEELAERLAEEELELEEALLA 701

                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199  695 ETDLKQIQTLIQGTQTRLKYSQNELEMIKKKHLVAFYQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDK 771
Cdd:COG1196   702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 1113-1199 2.39e-28

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: 113.33  E-value: 2.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1113 APGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTqDQFQMIVISLKEEFYSR 1192
Cdd:cd03278   103 APGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS-KETQFIVITHRKGTMEA 181


                  ....*..
gi 613410199 1193 ADALIGI 1199
Cdd:cd03278   182 ADRLYGV 188
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 513-628 8.61e-27

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: 106.16  E-value: 8.61e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    513 DSVFGRLFDLCHpIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPI-NERLRELK-- 589
Cdd:smart00968    1 PGVLGRVADLIS-VDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPaGSKLREALlp 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 613410199    590 ---GCKMVIDVIKTQfPQLKKVIQFVCGNGLVCETMEEARHI 628
Cdd:smart00968   80 epgFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 1114-1204 1.03e-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: 106.23  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1114 PGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQfQMIVISLKEEFYSRA 1193
Cdd:cd03274   118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNA-QFIVISLRNNMFELA 196

                          90
                  ....*....|.
gi 613410199 1194 DALIGIYPEYD 1204
Cdd:cd03274   197 DRLVGIYKTNN 207
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 1124-1200 1.53e-23

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


Pssm-ID: 213206 [Multi-domain]  Cd Length: 178  Bit Score: 98.92  E-value: 1.53e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 1124 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGIY 1200
Cdd:cd03239    95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVL 171
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 4-144 3.40e-21

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: 93.13  E-value: 3.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    4 LELLLVENFKSWRGRQVIGPF-RRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAHiGKPISSSASVKI 82
Cdd:cd03274     3 ITKLVLENFKSYAGEQVIGPFhKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSA-GHPNLDSCSVEV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613410199   83 iyveesgeekTFARIIrggcsefrfNDNLvsrsvyiaeLEKIGIIVKAQNCLVFQGTVESIS 144
Cdd:cd03274    82 ----------HFQEII---------DKPL---------LKSKGIDLDHNRFLILQGEVEQIA 115
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
 513-629 1.26e-20

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: 88.47  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   513 DSVFGRLFDLCHpIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLRELKGCK 592
Cdd:pfam06470    2 KGVLGRLADLIE-VDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGAG 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 613410199   593 MVIDVIKTQfPQLKKVIQFVCGNGLVCETMEEARHIA 629
Cdd:pfam06470   81 PLLDLVEYD-DEYRKALRYLLGNTLVVDDLDEALELA 116
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 1124-1202 4.69e-20

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: 88.57  E-value: 4.69e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199 1124 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGIYPE 1202
Cdd:cd03227    78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
 4-95 7.22e-19

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: 85.44  E-value: 7.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAhiGKPISSSASVKII 83
Cdd:cd03239     1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGG--VKAGINSASVEIT 78

                          90       100
                  ....*....|....*....|....*
gi 613410199   84 Y-----------VEE--SGEEKTFA 95
Cdd:cd03239    79 FdksyflvlqgkVEQilSGGEKSLS 103
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 4-83 8.56e-18

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: 82.90  E-value: 8.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    4 LELLLVENFKSWRGRQVIgPF-RRFTCIIGPNGSGKSNVMDALSFVMGEKIA-NLRVKNIQELIHGAHIGKPISSSASVK 81
Cdd:cd03278     1 LKKLELKGFKSFADKTTI-PFpPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSETRKPANFAEVT 79


                  ..
gi 613410199   82 II 83
Cdd:cd03278    80 LT 81
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 3-140 1.25e-17

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: 83.89  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    3 HLELLLVENFKSWRGRQVIGPF-RRFTCIIGPNGSGKSNVMDALSFVMG-EKIANLRVKNIQELIHgaHIGKPISSSASV 80
Cdd:cd03273     2 HIKEIILDGFKSYATRTVISGFdPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIY--KRGQAGITKASV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199   81 KIIYVEES------GEEK----TFARIIRGGCSEFRFNDNLVSRSVYIAEL-EKIGIIVKAQNCLVFQGTV 140
Cdd:cd03273    80 TIVFDNSDksqspiGFENypeiTVTRQIVLGGTNKYLINGHRAQQQRVQDLfQSVQLNVNNPHFLIMQGRI 150
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 1124-1196 7.86e-15

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: 75.80  E-value: 7.86e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 1124 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALD--NT-NIGKVssyIKEQ-TQDQFqmIVISLKEEFYSRADAL 1196
Cdd:cd03273   167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDlsHTqNIGRM---IKTHfKGSQF--IVVSLKEGMFNNANVL 238
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 1121-1199 3.86e-12

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: 67.67  E-value: 3.86e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199 1121 MDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTqDQFQMIVISLKEEFYSRADALIGI 1199
Cdd:cd03272   156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELS-DGAQFITTTFRPELLEVADKFYGV 233
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 7-159 4.70e-12

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: 67.29  E-value: 4.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    7 LLVENFKSWRGRQVIGPFR-RFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIH-GAhigKPISSSASVKII- 83
Cdd:cd03272     4 VIIQGFKSYKDQTVIEPFSpKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHeGS---GPSVMSAYVEIIf 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   84 -----YVEESGEEKTFARIIRGGCSEFRFNDNLVSRSVYIAELEKIGI-------IVKaqnclvfQGTVESISVKKPKEr 151
Cdd:cd03272    81 dnsdnRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFsrsnpyyIVP-------QGKINSLTNMKQDE- 152


                  ....*...
gi 613410199  152 TQFFEEIS 159
Cdd:cd03272   153 QQEMQQLS 160
PTZ00121 PTZ00121
MAEBL; Provisional
 145-509 2.20e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.55  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  145 VKKPKERTQFFEEISTSGELIGEYEEKKRKL----QKAEEDAQFNFNKKKniAAERRQA---KLEKEEAERYQSLLEELK 217
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakKKAEEKKKADEAKKK--AEEAKKAdeaKKKAEEAKKAEEAKKKAE 1467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  218 MNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEK-----ELKSVETLln 292
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakkadEAKKAEEK-- 1545

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  293 QKRPQYIKAKE-NTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSfEKQIEEEILHKKRDIELEASQ 371
Cdd:PTZ00121 1546 KKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEE 1624

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  372 LDRYKELK---EQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDC 448
Cdd:PTZ00121 1625 LKKAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199  449 LKEKKQQEEtlvdeiEKTKSRMSEVNEELNLIRSElqNAGIDTHEGKRQQKRAEVLEHLKR 509
Cdd:PTZ00121 1705 EELKKKEAE------EKKKAEELKKAEEENKIKAE--EAKKEAEEDKKKAEEAKKDEEEKK 1757
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 11-97 1.73e-09

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 58.14  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   11 NFKSWRGRQVIGPFR-RFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNiqelihGAHIGkPISSSASVKIIY--VEE 87
Cdd:cd03227     6 RFPSYFVPNDVTFGEgSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS------GVKAG-CIVAAVSAELIFtrLQL 78

                          90
                  ....*....|
gi 613410199   88 SGEEKTFARI 97
Cdd:cd03227    79 SGGEKELSAL 88
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
244-857 2.38e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.00  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  244 HVNRDLSVKRESLSHHENIvKARKKEHGmltRQLQQTEKELKSvetlLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSE 323
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENI-EELIKEKE---KELEEVLREINE----ISSELPELREELEKLEKEVKELEELKEEIEELE 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  324 KQCSKQEDDIKALETELADLDAAWRSFEKQIE--EEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQK 401
Cdd:PRK03918  245 KELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  402 TDEERLA---FEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEY--TKTCMDCLKEKKQQE--ETLVDEIEKTKSRMSEVN 474
Cdd:PRK03918  325 GIEERIKeleEKEERLEELKKKLKELEKRLEELEERHELYEEAkaKKEELERLKKRLTGLtpEKLEKELEELEKAKEEIE 404

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  475 EELNLIRSELqnAGIDThEGKRQQKRAEVLEHLKRLYPdsVFGRLFDLCH--PIHKKYQLAVTKVFGRFITAivvasekv 552
Cdd:PRK03918  405 EEISKITARI--GELKK-EIKELKKAIEELKKAKGKCP--VCGRELTEEHrkELLEEYTAELKRIEKELKEI-------- 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  553 aKDCIRFLKEERAEPETFLaldyldikpinERLRELKGCKMVIDVIKTQFPQLKKViqfvcgnglVCETMEEARHialsg 632
Cdd:PRK03918  472 -EEKERKLRKELRELEKVL-----------KKESELIKLKELAEQLKELEEKLKKY---------NLEELEKKAE----- 525

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  633 pERQKTVALDGTLflkSGVISGGSSDLKykarcwDEKELKNLRDRRSQKIQELKGLMKTLrketdLKQIQTLIQGTQTRL 712
Cdd:PRK03918  526 -EYEKLKEKLIKL---KGEIKSLKKELE------KLEELKKKLAELEKKLDELEEELAEL-----LKELEELGFESVEEL 590

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  713 KYSQNELEMIKKKHLVAFYQEqSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDdifqhFCEEIGVENIREF 792
Cdd:PRK03918  591 EERLKELEPFYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE-----LEKKYSEEEYEEL 664

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199  793 ENKHVKRQQEIDQKRLEFEkqktrlnvQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEE 857
Cdd:PRK03918  665 REEYLELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
PTZ00121 PTZ00121
MAEBL; Provisional
 145-476 9.17e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 9.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  145 VKKPKERTQFFEEISTSGELIGEYEEKKRK---LQKAEEDAQFNFNKKKniAAERRQAKLEKEEAERYQSLLEELKMNKi 221
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAeeaKKKAEEAKKADEAKKK--AEEAKKADEAKKKAEEAKKKADEAKKAA- 1506

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  222 qlqlfqlyHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEK--ELKSVEtllnQKRpqyi 299
Cdd:PTZ00121 1507 --------EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeEKKKAE----EAK---- 1570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  300 KAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIEL---------EAS 370
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLkkkeaeekkKAE 1650

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  371 QLDRYKEL----KEQVRKKVATMTQQLEKLQWEQKtDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKL---EEYTK 443
Cdd:PTZ00121 1651 ELKKAEEEnkikAAEEAKKAEEDKKKAEEAKKAEE-DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkaEEENK 1729

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 613410199  444 TCMDCLK-----EKKQQEETLVDEIEKTKSRMSEVNEE 476
Cdd:PTZ00121 1730 IKAEEAKkeaeeDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
COG4637 COG4637
Predicted ATPase [General function prediction only];
4-48 1.45e-08

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 58.40  E-value: 1.45e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 613410199    4 LELLLVENFKSWRgrQVIGPFRRFTCIIGPNGSGKSNVMDALSFV 48
Cdd:COG4637     2 ITRIRIKNFKSLR--DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 276-476 1.59e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 58.24  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  276 QLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIE 355
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  356 E---------------------EILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRH 414
Cdd:COG4942   101 AqkeelaellralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613410199  415 GEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEE 476
Cdd:COG4942   181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 330-511 1.67e-08

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: 56.47  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  330 EDDIKALEtELADLDAAWRSFEKQIEE---EILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEER 406
Cdd:COG1579     3 PEDLRALL-DLQELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  407 LafekrrhGEVQGN--LKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSEL 484
Cdd:COG1579    82 L-------GNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154

                         170       180
                  ....*....|....*....|....*..
gi 613410199  485 QNAgIDTHEGKRQQKRAEVLEHLKRLY 511
Cdd:COG1579   155 EAE-LEELEAEREELAAKIPPELLALY 180
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 169-469 3.13e-08

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 58.43  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  169 EEKKRKLQKAEEDAQFNFNKKKNIAAER-RQAKL--EKEEAERYQSLLE-ELKMNKIQLQLFQ--LYHNEKkihllntkL 242
Cdd:COG3096   278 NERRELSERALELRRELFGARRQLAEEQyRLVEMarELEELSARESDLEqDYQAASDHLNLVQtaLRQQEK--------I 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  243 EHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLL---------NQKRP-QY---IKAKENTSHHL 309
Cdd:COG3096   350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqqaldvQQTRAiQYqqaVQALEKARALC 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  310 KKLDVAKKSIKDSEKQCSKQEDDIK----ALETELADLDAAWRSFEKQIEeeiLHKKRDIELEASQ--------LDRYKE 377
Cdd:COG3096   430 GLPDLTPENAEDYLAAFRAKEQQATeevlELEQKLSVADAARRQFEKAYE---LVCKIAGEVERSQawqtarelLRRYRS 506

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  378 LKEQVrKKVATMTQQLEKL--QWEQKTDEERLA--FEKRRHGEVQGNLkQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKK 453
Cdd:COG3096   507 QQALA-QRLQQLRAQLAELeqRLRQQQNAERLLeeFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQRSELR 584

                         330
                  ....*....|....*.
gi 613410199  454 QQEETLVDEIEKTKSR 469
Cdd:COG3096   585 QQLEQLRARIKELAAR 600
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
9-214 3.60e-08

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 55.02  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    9 VENFKSWRGRQVIgPFRR-FTCIIGPNGSGKSNVMDALSFVMGEKiANLRVKNIQELIHGAhigkpiSSSASVKIIYvee 87
Cdd:COG0419     7 LENFRSYRDTETI-DFDDgLNLIVGPNGAGKSTILEAIRYALYGK-ARSRSKLRSDLINVG------SEEASVELEF--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   88 SGEEKTFaRIIRggcsefrfndnlvsrsvyiaelekigiivkaqnclvFQGTVESISVKKPKERTQFFEEIStsgeLIGE 167
Cdd:COG0419    76 EHGGKRY-RIER------------------------------------RQGEFAEFLEAKPSERKEALKRLL----GLEI 114

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 613410199  168 YEEKKRKLQKAEEDAQfnfnkkkniAAERRQAKLEKEEAERYQSLLE 214
Cdd:COG0419   115 YEELKERLKELEEALE---------SALEELAELQKLKQEILAQLSG 152
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
298-929 4.42e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.77  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  298 YIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLdaawrsfEKQIEEeILHKKRDIELEASQLDRYKE 377
Cdd:PRK03918  160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEV-------LREINE-ISSELPELREELEKLEKEVK 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  378 LKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKtcmdcLKEKKQQEE 457
Cdd:PRK03918  232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-----LSEFYEEYL 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  458 TLVDEIEKTKSRMSevnEELNLIRSELQNAGIDTHE-GKRQQKRAEVLEHLKRLYPDSvfgRLFDLCHPIHKKYQLAVTK 536
Cdd:PRK03918  307 DELREIEKRLSRLE---EEINGIEERIKELEEKEERlEELKKKLKELEKRLEELEERH---ELYEEAKAKKEELERLKKR 380

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  537 VFGRFItaivvasEKVAKDcIRFLKEERAEPEtflaldyLDIKPINERLRELKGckmVIDVIKTQFPQLK--KVIQFVCG 614
Cdd:PRK03918  381 LTGLTP-------EKLEKE-LEELEKAKEEIE-------EEISKITARIGELKK---EIKELKKAIEELKkaKGKCPVCG 442

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  615 NglvcETMEEARHIALSgperqktvaldgtlflksgvisggssdlKYKARCWD-EKELKNLRDRRSQKIQELKGLMKTLR 693
Cdd:PRK03918  443 R----ELTEEHRKELLE----------------------------EYTAELKRiEKELKEIEEKERKLRKELRELEKVLK 490

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  694 KETDLKQIQTLIQgtqtRLKYSQNELEMIKKKHLVAFYQEQSQLQSELLNIESQCimlsEGIKERQRRIKEFQEKIDKVE 773
Cdd:PRK03918  491 KESELIKLKELAE----QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI----KSLKKELEKLEELKKKLAELE 562

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  774 DDIfqHFCEEIGVENIREFENKHVKRQQEIDQKRLEFEKQKTRLnVQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLK 853
Cdd:PRK03918  563 KKL--DELEEELAELLKELEELGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELAETE 639

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613410199  854 KAEENCLQTVNELMAKQQQlkdirvtqnSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNL 929
Cdd:PRK03918  640 KRLEELRKELEELEKKYSE---------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 146-499 1.53e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.80  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   146 KKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKN------------IAAERRQAKLEKE--EAERYQS 211
Cdd:TIGR04523  149 KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNkllklelllsnlKKKIQKNKSLESQisELKKQNN 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   212 LLE---ELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKArkkehgmLTRQLQQTEKELksvE 288
Cdd:TIGR04523  229 QLKdniEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE-------LEKQLNQLKSEI---S 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   289 TLLNQKRPQYIKA-KENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeilhKKRDIEL 367
Cdd:TIGR04523  299 DLNNQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEK 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   368 EASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEE------- 440
Cdd:TIGR04523  375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvkel 454

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199   441 YTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQK 499
Cdd:TIGR04523  455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
270-771 1.97e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  270 HGMLTRQLQQTEKELKSVetllnQKRPQYIKAKEntshhLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAwrs 349
Cdd:COG4717    44 RAMLLERLEKEADELFKP-----QGRKPELNLKE-----LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE--- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  350 fekqiEEEILHKKRDIELEASQLDRYKELkEQVRKKVATMTQQLEKLQWEQKTDEERLAfekrrhgevqgNLKQIKEQIE 429
Cdd:COG4717   111 -----LEELREELEKLEKLLQLLPLYQEL-EALEAELAELPERLEELEERLEELRELEE-----------ELEELEAELA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  430 DHKKRIEKLEEYTKTcmdclkEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKR 509
Cdd:COG4717   174 ELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  510 LYPDS-VFGRLFDLCHPIHKKYQLAVTkvFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLREL 588
Cdd:COG4717   248 ARLLLlIAAALLALLGLGGSLLSLILT--IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  589 KGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCETMEEARHIALSGPERQKtvaldgtLFLKSGVISggSSDLKYKARCWDE 668
Cdd:COG4717   326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA-------LLAEAGVED--EEELRAALEQAEE 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  669 -KELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQTLIQGTQTRLKYSQNELEMIKkkhlvafyQEQSQLQSELLNIESQ 747
Cdd:COG4717   397 yQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR--------EELAELEAELEQLEED 468

                         490       500
                  ....*....|....*....|....
gi 613410199  748 cIMLSEGIKERQRRIKEFQEKIDK 771
Cdd:COG4717   469 -GELAELLQELEELKAELRELAEE 491
PTZ00121 PTZ00121
MAEBL; Provisional
 169-505 3.04e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  169 EEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKM----NKIQLQLFQLYHNEKKIHLLNTKLEH 244
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKaaaaKKKADEAKKKAEEKKKADEAKKKAEE 1442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  245 VNR--DLSVKRESLSHHENIVK----ARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKE--NTSHHLKKLDVAK 316
Cdd:PTZ00121 1443 AKKadEAKKKAEEAKKAEEAKKkaeeAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAK 1522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  317 KSIKDSEKQCSKQEDDI-KALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKK----VATMTQ 391
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieeVMKLYE 1602

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  392 QLEKLQWEQ--KTDEERLAFEK-RRHGEVQGNLKQIKEQIEDHKKRIEKL---EEYTKTCMDCLKEKKQQEETLVDEIEK 465
Cdd:PTZ00121 1603 EEKKMKAEEakKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKK 1682

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 613410199  466 TKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLE 505
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
3-114 3.14e-07

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


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 54.01  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    3 HLELLLVENFKSWRgRQVIGPFRRFTCIIGPNGSGKSNVMDALSFV-MGEkiaNLRVKNIQELI-HGAhigkpisSSASV 80
Cdd:COG1195     1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYLLaTGR---SFRTARDAELIrFGA-------DGFRV 69

                          90       100       110
                  ....*....|....*....|....*....|....
gi 613410199   81 KIIYVEESGEEKTFARIIRGGCSEFRFNDNLVSR 114
Cdd:COG1195    70 RAEVERDGREVRLGLGLSRGGKKRVRINGKPVRR 103
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 156-477 4.47e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 54.26  E-value: 4.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   156 EEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAER----RQAKLEKEEAERYQSLLEELKmNKIQLQLFQLYHN 231
Cdd:TIGR04523  117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyNDLKKQKEELENELNLLEKEK-LNIQKNIDKIKNK 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   232 EKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKK 311
Cdd:TIGR04523  196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   312 LDVAKKSIKDSEKQCSKQEDDIKALETE-LADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMT 390
Cdd:TIGR04523  276 LEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   391 QQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRM 470
Cdd:TIGR04523  356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435


                   ....*..
gi 613410199   471 SEVNEEL 477
Cdd:TIGR04523  436 IKNNSEI 442
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
194-431 5.38e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 5.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  194 AERRQAKLE--KEEAERYQSLLEELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHG 271
Cdd:COG4913   247 AREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  272 MLTRQLQQtekelksvetllnqkrpqyikakentsHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSfe 351
Cdd:COG4913   327 ELEAQIRG---------------------------NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA-- 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  352 kqiEEEILHKKRdiELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDH 431
Cdd:COG4913   378 ---SAEEFAALR--AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 1124-1199 6.96e-07

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 50.32  E-value: 6.96e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199 1124 LSGGEKCVAALALLFAvhsfRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRA-DALIGI 1199
Cdd:cd00267    81 LSGGQRQRVALARALL----LNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 18-893 7.52e-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: 7.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    18 RQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNiqELIHGAHIGKPISSSASVKIIYVEESGEEKTFARI 97
Cdd:TIGR00606   21 KQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGN--TFVHDPKVAQETDVRAQIRLQFRDVNGEECAVVRS 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    98 I----RGGCSEFRFNDNLVSR---------SVYIAELEK-----IGIIVKAQNCLVFQGTVESI-SVKKPKERTQFFEEI 158
Cdd:TIGR00606   99 MvctqKTKKTEFKTLEGVITRykhgekvslSSKCAEIDRemishLGVSKAVLNNVIFCHQEDSNwPLSEGKALKQKFDEI 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   159 STSGELIGEYE-------EKKRKLQKAEEDAQFNFNKKKNIAAERRQ--AKLEKEEAERYQSLLEELKMNKIQLQLFQLY 229
Cdd:TIGR00606  179 FSATRYIKALEtlrqvrqTQGQKVQEHQMELKYLKQYKEKACEIRDQitSKEAQLESSREIVKSYENELDPLKNRLKEIE 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   230 HNEKKIHLLNTKL----------EHVNRDLSVKRESL------------SHHENIVKARKKEHGMLTRQLQQTEKELKsv 287
Cdd:TIGR00606  259 HNLSKIMKLDNEIkalksrkkqmEKDNSELELKMEKVfqgtdeqlndlyHNHQRTVREKERELVDCQRELEKLNKERR-- 336

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   288 etLLNQKRPQYIkaKENTSHHLKKLDVAKKSIK-DSEKQCSKQEDDIKALETElADLDAAWRSFEKQIEEEILHKKRDIE 366
Cdd:TIGR00606  337 --LLNQEKTELL--VEQGRLQLQADRHQEHIRArDSLIQSLATRLELDGFERG-PFSERQIKNFHTLVIERQEDEAKTAA 411

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   367 LEASQLDRYKELKEQ------VRKKVATMTQQLEKLQWEQKTDEerLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEE 440
Cdd:TIGR00606  412 QLCADLQSKERLKQEqadeirDEKKGLGRTIELKKEILEKKQEE--LKFVIKELQQLEGSSDRILELDQELRKAERELSK 489

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   441 YTKTCM-DCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDThegKRQQKRAEVLEHLKRLYPDSVFGRL 519
Cdd:TIGR00606  490 AEKNSLtETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLL 566

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   520 FDLchpihkKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLD--IKPINERLRELKGCKMV--- 594
Cdd:TIGR00606  567 GYF------PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEeqLSSYEDKLFDVCGSQDEesd 640

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   595 IDVIKTQFPQLKKVIQFVCGnglvcETMEEARHIALSGPERQKTVALDGTLFLKSGVISGGSSDLKYKARCWD------E 668
Cdd:TIGR00606  641 LERLKEEIEKSSKQRAMLAG-----ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPdklkstE 715

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   669 KELKNLRDRRSQKIQELKGLMKTL-RKETDLKQIQTLIQGTQTRLKYSQNELEmikkkhlvafyQEQSQLQSELLNIESQ 747
Cdd:TIGR00606  716 SELKKKEKRRDEMLGLAPGRQSIIdLKEKEIPELRNKLQKVNRDIQRLKNDIE-----------EQETLLGTIMPEEESA 784

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   748 CIMLSE-GIKERqrrikeFQEKIDKVEDDIFQHFCEEIGVENIREFEnkHVKRQQEIDQKRLEFEKQKTRLNVQLEYSRS 826
Cdd:TIGR00606  785 KVCLTDvTIMER------FQMELKDVERKIAQQAAKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856

                          890       900       910       920       930       940       950
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199   827 ----HLKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEE 893
Cdd:TIGR00606  857 eqiqHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
259-896 9.03e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 9.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  259 HENIVKARKKEHgmLTRQLQQTEKELKSVETLLNQKRpqYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALET 338
Cdd:COG4913   241 HEALEDAREQIE--LLEPIRELAERYAAARERLAELE--YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  339 ELADLDAAWRSFEKQI-----------EEEILHKKRDieleasqldrykelKEQVRKKVATMTQQLEKLQWEQKTDEERL 407
Cdd:COG4913   317 RLDALREELDELEAQIrgnggdrleqlEREIERLERE--------------LEERERRRARLEALLAALGLPLPASAEEF 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  408 AfekrrhgEVQGNLKQIKEQIEDHKKRIEklEEYTKTcMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSEL-QN 486
Cdd:COG4913   383 A-------ALRAEAAALLEALEEELEALE--EALAEA-EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALaEA 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  487 AGIDTHEgkrqqkraevlehLKrlypdsVFGRLFDLcHPIHKKYQLAVTKVFGRFITAIVVaSEKVAKDCIRFLKEERAE 566
Cdd:COG4913   453 LGLDEAE-------------LP------FVGELIEV-RPEEERWRGAIERVLGGFALTLLV-PPEHYAAALRWVNRLHLR 511

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  567 petfLALDYLDIKPINERLRELKG------CKMVIDV------IKTqfpQLKKVIQFVCgnglvCETMEEARH----IAL 630
Cdd:COG4913   512 ----GRLVYERVRTGLPDPERPRLdpdslaGKLDFKPhpfrawLEA---ELGRRFDYVC-----VDSPEELRRhpraITR 579

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  631 SGPERQKTVA--LDGTLFLKSGVISGGSSDLKYKARcwdEKELKNLRDRRSQ---KIQELKGLMKTLRKE-TDLKQIQTL 704
Cdd:COG4913   580 AGQVKGNGTRheKDDRRRIRSRYVLGFDNRAKLAAL---EAELAELEEELAEaeeRLEALEAELDALQERrEALQRLAEY 656

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  705 ------IQGTQTRLKYSQNELEMIKK--KHLVAFYQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEdDI 776
Cdd:COG4913   657 swdeidVASAEREIAELEAELERLDAssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-DR 735

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  777 FQHFCEEIGVENIREFENK--HVKRQQEIDQKRLEFEKQKTRLNVQLEYSRSHLKKKLNKINTL-KETIQKGSEDIDHLK 853
Cdd:COG4913   736 LEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLP 815

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 613410199  854 KAEENCLQTVNE-LMAKQQQLKDiRVTQNSSAEKV--QTQIEEERK 896
Cdd:COG4913   816 EYLALLDRLEEDgLPEYEERFKE-LLNENSIEFVAdlLSKLRRAIR 860
AAA_23 pfam13476
AAA domain;
7-190 1.01e-06

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 50.57  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199     7 LLVENFKSWRGrQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANL-RVKNIQELIHGAHIGKPISSSASVKIIYV 85
Cdd:pfam13476    1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLkRKSGGGFVKGDIRIGLEGKGKAYVEITFE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    86 EESGE-----EKTFARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKPKERTQFFEEISt 160
Cdd:pfam13476   80 NNDGRytyaiERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELE- 158

                          170       180       190
                   ....*....|....*....|....*....|
gi 613410199   161 sgELIGEYEEKKRKLQKAEEDAQFNFNKKK 190
Cdd:pfam13476  159 --KALEEKEDEKKLLEKLLQLKEKKKELEE 186
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 275-487 1.32e-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: 52.07  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  275 RQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQI 354
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  355 EE--------------EILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQweqktdeerlafekrrhgevqgn 420
Cdd:COG4942   107 AEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA----------------------- 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199  421 lkQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNA 487
Cdd:COG4942   164 --ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
PTZ00121 PTZ00121
MAEBL; Provisional
 145-515 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 613410199  145 VKKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQfnfNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQlq 224
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE---EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-- 1375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  225 lfqlyhNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHG-MLTRQLQQTEKELKSVETLlnQKRPQYIKAKE 303
Cdd:PTZ00121 1376 ------AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkKKADEAKKKAEEKKKADEA--KKKAEEAKKAD 1447

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  304 NTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADlDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELK--EQ 381
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkaDE 1526

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  382 VRK-KVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQgNLKQIKEQIEDHKKRIEKLEEYTKTcmdclkEKKQQEETLV 460
Cdd:PTZ00121 1527 AKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK-KAEEAKKAEEDKNMALRKAEEAKKA------EEARIEEVMK 1599

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 613410199  461 DEIEKTKSRMSEVNEElnlirselQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSV 515
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKA--------EEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-440 2.47e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  162 GELIGEY-------EEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKmnkiQLQLFQLYHNEKK 234
Cdd:PRK03918  451 KELLEEYtaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLK----KYNLEELEKKAEE 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  235 IHLLNTKLEHVNRDLSVKRESLSHheniVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKK--- 311
Cdd:PRK03918  527 YEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPfyn 602

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  312 ----LDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeiLHKKRDIELEASQLDRYKELkeqvRKKVA 387
Cdd:PRK03918  603 eyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELREEYLEL----SRELA 676

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 613410199  388 TMTQQLEKLQWEQKTDEERLAFEKRRHGEvqgnLKQIKEQIEDHKKRIEKLEE 440
Cdd:PRK03918  677 GLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEKALERVEE 725
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
4-510 2.56e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    4 LELLLVENFKSWRGRQVigPFRR-FTCIIGPNGSGKSNVMDA----LSFVMGEKIANLRVKNIQElihgahigkpISSSA 78
Cdd:PRK03918    3 IEELKIKNFRSHKSSVV--EFDDgINLIIGQNGSGKSSILEAilvgLYWGHGSKPKGLKKDDFTR----------IGGSG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   79 SVKIIYVEESGEEKTFARIIRGGCSEFRFND---NLVSRSVYIAE-LEKIGIIVKAQNCL-VFQGTVESIsVKKPKERTQ 153
Cdd:PRK03918   71 TEIELKFEKNGRKYRIVRSFNRGESYLKYLDgseVLEEGDSSVREwVERLIPYHVFLNAIyIRQGEIDAI-LESDESREK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  154 FFEEISTsgelIGEYEekkrklqkaeedaqfnfNKKKNIAAERRQAKLEKEEAERYQSLLEELKmNKIQLQLFQLYHNEK 233
Cdd:PRK03918  150 VVRQILG----LDDYE-----------------NAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLR 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  234 KIHLLNTKLehvnRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRpQYIKAKENTSHHLKKLD 313
Cdd:PRK03918  208 EINEISSEL----PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKV 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  314 VAKKSIKDSEKQ-------CSKQEDDIKALETELADLDAAWRSFEKQIEE---------EILHKKRDIELEASQLDRYKE 377
Cdd:PRK03918  283 KELKELKEKAEEyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKEleekeerleELKKKLKELEKRLEELEERHE 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  378 LKEQVRKKVATMTQQLEKLQWEQKTD-EERLAFEKRRHGEVQGNLKQIKEQI-------EDHKKRIEKLEEYTKTCMDCL 449
Cdd:PRK03918  363 LYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIgelkkeiKELKKAIEELKKAKGKCPVCG 442

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613410199  450 KE-----KKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRL 510
Cdd:PRK03918  443 RElteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEL 508
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 4-96 3.40e-06

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: 49.14  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVM-GEKIANLRvkniqeliHGAHIGKPI---SSSAS 79
Cdd:cd03240     1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSK--------GGAHDPKLIregEVRAQ 72

                          90
                  ....*....|....*..
gi 613410199   80 VKIIYVEESGEEKTFAR 96
Cdd:cd03240    73 VKLAFENANGKKYTITR 89
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
9-48 4.33e-06

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


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 50.43  E-value: 4.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 613410199    9 VENFKSWRGRQVI------GPFRRFTCIIGPNGSGKSNVMDALSFV 48
Cdd:COG1106     7 IENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFL 52
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 755-1050 4.37e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  755 IKERQRRIKEFQEKIDKVEDDIfqhfcEEIGvENIrefenKHVKRQQEIDQKRLEFEKQKTRLNVQLeysrshlkkKLNK 834
Cdd:COG1196   174 KEEAERKLEATEENLERLEDIL-----GELE-RQL-----EPLERQAEKAERYRELKEELKELEAEL---------LLLK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  835 INTLKETIQKGSEDIDHLKKAEEnclqtvnELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVS 914
Cdd:COG1196   234 LRELEAELEELEAELEELEAELE-------ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  915 IQTSLEQKRLEKHNLLLDCKVQDIEIILLSGSLDDIIEVEMGTEAESTQATIDIYEKEEAFEIDYSSLKEDLKALQSDQE 994
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 613410199  995 IEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKFQESTDAFEASRKEARL 1050
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 7-1008 1.12e-05

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: 49.97  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199     7 LLVENFKSWRGRQVI--GPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIAnlRVKNIQELIHGAHIGKPISSSASVKIIY 84
Cdd:TIGR00618    6 LTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALYGKLP--RRSEVIRSLNSLYAAPSEAAFAELEFSL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    85 veesgeektfariirgGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNclvFQGTVESISVKKPKERtqffeeISTSGEL 164
Cdd:TIGR00618   84 ----------------GTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKK---GRGRILAAKKSETEEV------IHDLLKL 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   165 IGEYEEKKRKLQKAEEDAQFNFNKKkniaaERRQAKLEKEEAERYQSLLEELKMNKIQLqlfqlyhnEKKIHLLNTKLEH 244
Cdd:TIGR00618  139 DYKTFTRVVLLPQGEFAQFLKAKSK-----EKKELLMNLFPLDQYTQLALMEFAKKKSL--------HGKAELLTLRSQL 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   245 VNRDLSVKRESLshhenivkarkkehgmlTRQLQQTEKELKSVETLLNQKRpqyikakeNTSHHLKKLDVAKKSIKDSEK 324
Cdd:TIGR00618  206 LTLCTPCMPDTY-----------------HERKQVLEKELKHLREALQQTQ--------QSHAYLTQKREAQEEQLKKQQ 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   325 QCSKQEDDIKALETELADLDAAW--RSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKT 402
Cdd:TIGR00618  261 LLKQLRARIEELRAQEAVLEETQerINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI 340

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   403 DEERLAFEK--------RRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVN 474
Cdd:TIGR00618  341 EEQRRLLQTlhsqeihiRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFR 420

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   475 -EELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVfgRLFDLCHpiHKKYQLAVTKVfgrfitaIVVASEKVA 553
Cdd:TIGR00618  421 dLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ--ESAQSLK--EREQQLQTKEQ-------IHLQETRKK 489

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   554 KDCIRFLKEERAEPetflaldyldiKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGlvcETMEEARHIALSGP 633
Cdd:TIGR00618  490 AVVLARLLELQEEP-----------CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE---TSEEDVYHQLTSER 555

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   634 ERQKTvaldgtlflksgvisggssdLKYKARCWDEKELKnlrdrRSQKIQELKGLMKTLRKETDLKQIQTLIQGTQTRLK 713
Cdd:TIGR00618  556 KQRAS--------------------LKEQMQEIQQSFSI-----LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   714 YSQNELEMIKKKHLVAFYQ--------EQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQE--------KIDKVEDDIF 777
Cdd:TIGR00618  611 ACEQHALLRKLQPEQDLQDvrlhlqqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKellasrqlALQKMQSEKE 690

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   778 QHFCEEIGVENIREFENKHVKRQQEIDQKRLEFEKQKTRLNVQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLKK--- 854
Cdd:TIGR00618  691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNeev 770

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   855 -AEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKF-LAVDREVGKLQKEVVSIQTSLEQKRLEKHNL--- 929
Cdd:TIGR00618  771 tAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDeDILNLQCETLVQEEEQFLSRLEEKSATLGEIthq 850

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   930 ---LLDCKVQDIEIILLSGSLDDIIEVEMGTEAESTQATIDIYEKEEAfEIDYSSLKEdlkaLQSDQEIEAHLRLLLQQV 1006
Cdd:TIGR00618  851 llkYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLH-EITLYANVR----LANQSEGRFHGRYADSHV 925


                   ..
gi 613410199  1007 AS 1008
Cdd:TIGR00618  926 NA 927
PTZ00121 PTZ00121
MAEBL; Provisional
 156-469 1.20e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  156 EEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERyqslLEELKMNKIQLQLFQLYHNE--K 233
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK----ADELKKAEEKKKADEAKKAEekK 1302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  234 KIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKK-EHGMLTRQLQQTEKELKSVETLLNQKRPQyiKAKENTSHHLKKL 312
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKaEEAKKAAEAAKAEAEAAADEAEAAEEKAE--AAEKKKEEAKKKA 1380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  313 DVAKKSIKDSEK---------QCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDielEASQLDRYKELKEQVR 383
Cdd:PTZ00121 1381 DAAKKKAEEKKKadeakkkaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---EAKKADEAKKKAEEAK 1457

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  384 KkvatmTQQLEKlqweqKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEI 463
Cdd:PTZ00121 1458 K-----AEEAKK-----KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527


                  ....*.
gi 613410199  464 EKTKSR 469
Cdd:PTZ00121 1528 KKAEEA 1533
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-441 1.42e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  260 ENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRpQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQED------DI 333
Cdd:COG4717    56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLQllplyqEL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  334 KALETELADLDAAWRSFEKQIEE--EILHKKRDIELEASQLDR-----YKELKEQVRKKVATMTQQLEKLQWEQKTDEER 406
Cdd:COG4717   135 EALEAELAELPERLEELEERLEElrELEEELEELEAELAELQEeleelLEQLSLATEEELQDLAEELEELQQRLAELEEE 214

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 613410199  407 LAFEKRRHGEVQGNLKQIKEQIEDHKKRiEKLEEY 441
Cdd:COG4717   215 LEEAQEELEELEEELEQLENELEAAALE-ERLKEA 248
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
 3-52 1.64e-05

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 48.46  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 613410199    3 HLELLLVENFKSWRgRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEK 52
Cdd:COG3593     2 KLEKIKIKNFRSIK-DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 168-505 1.87e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 49.05  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   168 YEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEElKMNKIQLQLF----QLYHNEKKIHLLNTKLE 243
Cdd:pfam10174  354 LEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQK-KIENLQEQLRdkdkQLAGLKERVKSLQTDSS 432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   244 HVNRDLSVKRESLSHHENIVKARKKEHGMLTRQ----LQQTEKELKSVETLLNQKRPQ-------YIKAKENTSHHLKKL 312
Cdd:pfam10174  433 NTDTALTTLEEALSEKERIIERLKEQREREDRErleeLESLKKENKDLKEKVSALQPEltekessLIDLKEHASSLASSG 512

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   313 DVAKKSIKDSEKQCSKQEDDIKALETELadLDAAWRSFEKQIEEEILHKKRDIELEASqldRYKELKEQVRKKVATMTQQ 392
Cdd:pfam10174  513 LKKDSKLKSLEIAVEQKKEECSKLENQL--KKAHNAEEAVRTNPEINDRIRLLEQEVA---RYKEESGKAQAEVERLLGI 587

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   393 LEKLQWEQKTDEERLA-FEK---RRHGEVQGNLKQIKE-QIEDHKKRIEKLEEYTKTCMDCL-KEKKQQEETLVDEIEKT 466
Cdd:pfam10174  588 LREVENEKNDKDKKIAeLESltlRQMKEQNKKVANIKHgQQEMKKKGAQLLEEARRREDNLAdNSQQLQLEELMGALEKT 667

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 613410199   467 KSRMSEVNEELNLIRSELQNAgiDTHEGKRQQKRAEVLE 505
Cdd:pfam10174  668 RQELDATKARLSSTQQSLAEK--DGHLTNLRAERRKQLE 704
PTZ00121 PTZ00121
MAEBL; Provisional
 146-486 2.65e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  146 KKPKERTQFFEEISTSGELIGEYEEKKRK---LQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSL--LEELKMNK 220
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKadeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkkAEEKKKAD 1549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  221 IQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLShhENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIK 300
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA--KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  301 AKENTSHHLKKLDVAKKSIKDSEkQCSKQEDDIKALETELADLDAAwrsfEKQIEEEILHKKRDIELEASQLDRYKELK- 379
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIKAAEEAKKAEE----DKKKAEEAKKAEEDEKKAAEALKKEAEEAk 1702

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  380 --EQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEE 457
Cdd:PTZ00121 1703 kaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782

                         330       340
                  ....*....|....*....|....*....
gi 613410199  458 TLVDeiEKTKSRMSEVNEELNLIRSELQN 486
Cdd:PTZ00121 1783 EELD--EEDEKRRMEVDKKIKDIFDNFAN 1809
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 1120-1197 3.54e-05

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 46.06  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1120 PMDNLSGGEKCVAALALLFAVHSFRPA--PFFVLDEVDAALDNTNI-GKVSSYIKEQ-TQDQFQMIVISLKEEFYSRADA 1195
Cdd:cd03240   112 MRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERkSQKNFQLIVITHDEELVDAADH 191


                  ..
gi 613410199 1196 LI 1197
Cdd:cd03240   192 IY 193
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 751-1050 4.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  751 LSEGIKERQ-----RRIKEFQEKIDKVEDDIfqhfceEIGVENIREFENKHVKRQQEIDQKRLEFEKQKTRLNVQLEysr 825
Cdd:COG1196   218 LKEELKELEaelllLKLRELEAELEELEAEL------EELEAELEELEAELAELEAELEELRLELEELELELEEAQA--- 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  826 shlkkklnKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREV 905
Cdd:COG1196   289 --------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  906 GKLQKEVVSIQTSLEQKRLEKHNL---LLDCKVQDIEIILLSGSLDDIIEVEMGTEAESTQATIDIYEKEEAFEIDYSSL 982
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199  983 KEDLKA-------LQSDQEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKFQESTDAFEASRKEARL 1050
Cdd:COG1196   441 EEALEEaaeeeaeLEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
PRK01156 PRK01156
chromosome segregation protein; Provisional
 774-1199 7.02e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.20  E-value: 7.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  774 DDIFQHFCEEIG--VENIREFENKhvkrQQEIDQKRLEFEKQKTRLNV-----------QLEYSRSHLKKKLNKINTLKE 840
Cdd:PRK01156  468 NHIINHYNEKKSrlEEKIREIEIE----VKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKD 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  841 TIQKGSEDIDHLKKAEENCLQTVNElmakqQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLE 920
Cdd:PRK01156  544 KHDKYEEIKNRYKSLKLEDLDSKRT-----SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  921 Q--KRLEKHNLLLDCKVQDIE-----IILLSGSLDDIIEVEMGT-EAESTQATIDIyeKEEAFEIDYSSLKEDLKALQSD 992
Cdd:PRK01156  619 KsiREIENEANNLNNKYNEIQenkilIEKLRGKIDNYKKQIAEIdSIIPDLKEITS--RINDIEDNLKKSRKALDDAKAN 696

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  993 Q-EIEAHLRLLLQQVASQEDIL------LKTAAPNLRALENLKTVRDKFqeSTDAFEAS-RKEArlcrQEFEQVKKRRYd 1064
Cdd:PRK01156  697 RaRLESTIEILRTRINELSDRIndinetLESMKKIKKAIGDLKRLREAF--DKSGVPAMiRKSA----SQAMTSLTRKY- 769

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1065 LFTQCFEHVSISIDQIYK-KLCRNNSAQAflspenpeepylegisyncvapgkrfmpMDNLSGGEKCVAALALLFAVHSF 1143
Cdd:PRK01156  770 LFEFNLDFDDIDVDQDFNiTVSRGGMVEG----------------------------IDSLSGGEKTAVAFALRVAVAQF 821

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199 1144 RPA--PFFVLDEVDAALDN---TNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGI 1199
Cdd:PRK01156  822 LNNdkSLLIMDEPTAFLDEdrrTNLKDIIEYSLKDSSDIPQVIMISHHRELLSVADVAYEV 882
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
 1121-1162 8.15e-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: 44.90  E-value: 8.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 613410199 1121 MDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTN 1162
Cdd:cd03276   107 VKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN 148
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 27-235 8.75e-05

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 45.84  E-value: 8.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199    27 FTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAHIGKPISSSASVKIIYVEESGEEKTFARIIRggcSEFR 106
Cdd:pfam13304    1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYR---YGLD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   107 FNDNLVSRSVY-IAELEKIGIIVKAQNClvFQGTVESISVKKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFN 185
Cdd:pfam13304   78 LEREDVEEKLSsKPTLLEKRLLLREDSE--EREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLL 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 613410199   186 FNKKKNIAAERRQAKLEKEEAeRYQSLLEELK--MNKIQLQLFQLYHNEKKI 235
Cdd:pfam13304  156 LLDEGLLLEDWAVLDLAADLA-LFPDLKELLQrlVRGLKLADLNLSDLGEGI 206
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 666-929 9.74e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.55  E-value: 9.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   666 WDEKELKNLrdrrSQKIQELKGLMKTLrkETDLKQIQTLIQGTQTRLKYSQNELEMIKKK--HLVAFYQEQSQLQSELLN 743
Cdd:TIGR04523  149 KKEKELEKL----NNKYNDLKKQKEEL--ENELNLLEKEKLNIQKNIDKIKNKLLKLELLlsNLKKKIQKNKSLESQISE 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   744 IESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHFCEEIgvENIREFENKhvkrQQEIDQ---KRLEFEKQKTRLNVQ 820
Cdd:TIGR04523  223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN--KIKKQLSEK----QKELEQnnkKIKELEKQLNQLKSE 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   821 LEYSRShlKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKkfla 900
Cdd:TIGR04523  297 ISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN---- 370

                          250       260
                   ....*....|....*....|....*....
gi 613410199   901 vdrEVGKLQKEVVSIQTSLEQKRLEKHNL 929
Cdd:TIGR04523  371 ---EIEKLKKENQSYKQEIKNLESQINDL 396
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 170-457 1.30e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.27  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   170 EKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKE-EAERYQSL-----LEELKMNKIQLQLFQLYHNEKKIHLLNTKLE 243
Cdd:pfam17380  313 ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERErELERIRQEerkreLERIRQEEIAMEISRMRELERLQMERQQKNE 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   244 HVNRDLSVKREslshheniVKARKKEHgmlTRQLQQTEKELKSVETLLNQKRPQYIKA-KENTSHHLKKLDVAKKSIKDS 322
Cdd:pfam17380  393 RVRQELEAARK--------VKILEEER---QRKIQQQKVEMEQIRAEQEEARQREVRRlEEERAREMERVRLEEQERQQQ 461

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   323 EKQCSKQEDDIKALETELADldaawRSFEKQIEEEILHKKRDIELEAsqldRYKELKEQVRKKVATMTQQLEKLQWEQKT 402
Cdd:pfam17380  462 VERLRQQEEERKRKKLELEK-----EKRDRKRAEEQRRKILEKELEE----RKQAMIEEERKRKLLEKEMEERQKAIYEE 532

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199   403 DEERLAFEKRRHGEVQGNLKQIKEQI---EDHKKRIEKLEEYTKTCMDCLKEKKQQEE 457
Cdd:pfam17380  533 ERRREAEEERRKQQEMEERRRIQEQMrkaTEERSRLEAMEREREMMRQIVESEKARAE 590
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 137-509 1.40e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.58  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   137 QGTVESISVKKPKERTQFFEEISTSGELIG----EYEEKKRKLQKAEEDAQfnfNKKKNIAAERRQAKLEKEEAERYQSL 212
Cdd:TIGR00606  711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDlkekEIPELRNKLQKVNRDIQ---RLKNDIEEQETLLGTIMPEEESAKVC 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   213 LEELKMnkIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARK-KEHGMLTRQLQQTEkelksvetll 291
Cdd:TIGR00606  788 LTDVTI--MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvVSKIELNRKLIQDQ---------- 855

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   292 nQKRPQYIKAKENtshhlkKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQ 371
Cdd:TIGR00606  856 -QEQIQHLKSKTN------ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   372 LDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRH-GEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLK 450
Cdd:TIGR00606  929 ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID 1008

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199   451 EKKQQEETLVDEIEKTKSR--MSEVNEELNLIRSELQNAGIdTHEGKRQQKRAEVLEHLKR 509
Cdd:TIGR00606 1009 TQKIQERWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQV-LQMKQEHQKLEENIDLIKR 1068
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 167-484 1.53e-04

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: 46.17  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   167 EYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEElKMNKIQLQLFQLyHNEKK---IHLLNTKLE 243
Cdd:TIGR04523  240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-QLNQLKSEISDL-NNQKEqdwNKELKSELK 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   244 HVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSE 323
Cdd:TIGR04523  318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   324 KQCSKQEDDIKALETELADLDAAWRSFEKQIEEeilhKKRDIELEASQLDRYKELKEQVRKKVatmtQQLEKLQWEQKTD 403
Cdd:TIGR04523  398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER----LKETIIKNNSEIKDLTNQDSVKELII----KNLDNTRESLETQ 469

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   404 EERLafeKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSE 483
Cdd:TIGR04523  470 LKVL---SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546


                   .
gi 613410199   484 L 484
Cdd:TIGR04523  547 L 547
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 159-483 1.77e-04

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: 45.78  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   159 STSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEElKMNKIQLQLFQLYHNEKKIHLL 238
Cdd:TIGR04523  356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE-QIKKLQQEKELLEKEIERLKET 434

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   239 NTKLEHVNRDL----SVKRESLSHHENIVKARKKEHGMLTRQ-------LQQTEKELKSVETLLNQKRPQYIKAKENTSH 307
Cdd:TIGR04523  435 IIKNNSEIKDLtnqdSVKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   308 HLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSfeKQIEEEILHKKRDIE--------LEASQlDRYKELK 379
Cdd:TIGR04523  515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEelkqtqksLKKKQ-EEKQELI 591

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   380 EQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETL 459
Cdd:TIGR04523  592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671

                          330       340
                   ....*....|....*....|....
gi 613410199   460 VDEIEKTKSRMSEVNEELNLIRSE 483
Cdd:TIGR04523  672 KTKIDDIIELMKDWLKELSLHYKK 695
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 679-923 2.01e-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: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  679 SQKIQELKGLMKTLRKEtdLKQIQTLIQGTQTRLKYSQNELEMIKKKhlvafyqeQSQLQSELLNIESQCIMLSEGIKER 758
Cdd:COG4942    19 ADAAAEAEAELEQLQQE--IAELEKELAALKKEEKALLKQLAALERR--------IAALARRIRALEQELAALEAELAEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  759 QRRIKEFQEKIDKVEDDIFQHFceeigvenirefenkhVKRQQEIDQKRLEF---EKQKTRLNVQLEYSRSHLKKKLNKI 835
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELL----------------RALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  836 NTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSI 915
Cdd:COG4942   153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232


                  ....*...
gi 613410199  916 QTSLEQKR 923
Cdd:COG4942   233 EAEAAAAA 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
187-509 2.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  187 NKKKNIAAERRQAKLEKEEAERYQSLLEELKmNKIQLQLFQLYHNEKKIHLLNTKLehvnRDLSVKRESLSHHENIVKAR 266
Cdd:PRK03918  162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSEL----PELREELEKLEKEVKELEEL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  267 KKEHGMLTRQLQQTEKELKSVETLLNQKRpQYIKAKENTSHHLKKLDVAKKSIKDSEKQ-------CSKQEDDIKALETE 339
Cdd:PRK03918  237 KEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELKELKEKAEEyiklsefYEEYLDELREIEKR 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  340 LADLDAAWRSFEKQIEE---------EILHKKRDIELEASQLDRYKELKEQVRKKVATMTQ---------------QLEK 395
Cdd:PRK03918  316 LSRLEEEINGIEERIKEleekeerleELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltgltpeklekELEE 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  396 LQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKK----------------RIEKLEEYTKTCMDCLKEKKQQEE-- 457
Cdd:PRK03918  396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEke 475

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  458 ------------------------TLVDEIEKTKSRMSEVN---------------EELNLIRSELQNAGIDTHEGKRQQ 498
Cdd:PRK03918  476 rklrkelrelekvlkkeseliklkELAEQLKELEEKLKKYNleelekkaeeyeklkEKLIKLKGEIKSLKKELEKLEELK 555

                         410
                  ....*....|.
gi 613410199  499 KRAEVLEHLKR 509
Cdd:PRK03918  556 KKLAELEKKLD 566
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
149-485 2.52e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  149 KERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQLFQL 228
Cdd:PRK03918  300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKK 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  229 YHNEKKIHLLNTKLEHVNRdlsvKRESLSHHENIVKARKkehgmltRQLQQTEKEL-KSVETLLNQKRPQYIKAKENTSH 307
Cdd:PRK03918  380 RLTGLTPEKLEKELEELEK----AKEEIEEEISKITARI-------GELKKEIKELkKAIEELKKAKGKCPVCGRELTEE 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  308 HLKKLdvakksIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEilhkkrdieleaSQLDRYKELKEQVRKkva 387
Cdd:PRK03918  449 HRKEL------LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE------------SELIKLKELAEQLKE--- 507

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  388 tMTQQLEKLqweqktDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTK 467
Cdd:PRK03918  508 -LEEKLKKY------NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580

                         330
                  ....*....|....*...
gi 613410199  468 SRMSEVNEELNLIRSELQ 485
Cdd:PRK03918  581 ELGFESVEELEERLKELE 598
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 183-401 2.74e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 45.12  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   183 QFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQlfqlyhnekkihllntKLEHVNRDLSVKRESLSHHENI 262
Cdd:pfam05557   42 QLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK----------------YLEALNKKLNEKESQLADAREV 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   263 VKARKKEHGMLTRQLQQTEKELKSVET----------LLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDD 332
Cdd:pfam05557  106 ISCLKNELSELRRQIQRAELELQSTNSeleelqerldLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQD 185

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199   333 ---IKALETELADLdAAWRSFEKQIEEEILH---KKRDIELEASQLDRYK---ELKEQVRKKVATMTQQLEKLQWEQK 401
Cdd:pfam05557  186 seiVKNSKSELARI-PELEKELERLREHNKHlneNIENKLLLKEEVEDLKrklEREEKYREEAATLELEKEKLEQELQ 262
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 169-546 2.92e-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: 45.21  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   169 EEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSL-LEELKMNKIQL-QLFQLYHNEKKihllnTKLEHVN 246
Cdd:pfam12128  600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFaRTALKNARLDLrRLFDEKQSEKD-----KKNKALA 674

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   247 RDLSVKRESLSHHENIVKARKKEHGMLtrqLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKK-LDVAKKSIKDSEKQ 325
Cdd:pfam12128  675 ERKDSANERLNSLEAQLKQLDKKHQAW---LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAaIAARRSGAKAELKA 751

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   326 CSKQED-DIKAL---ETELADLDAAWRSFEKQIEE------EILHKKRDI-ELEASQLDRYKELKEQVRKKVATMTQQLE 394
Cdd:pfam12128  752 LETWYKrDLASLgvdPDVIAKLKREIRTLERKIERiavrrqEVLRYFDWYqETWLQRRPRLATQLSNIERAISELQQQLA 831

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   395 KLQWEQKTDeeRLAFEKRRHG------EVQGNLKQIKEQIE-----DHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEI 463
Cdd:pfam12128  832 RLIADTKLR--RAKLEMERKAsekqqvRLSENLRGLRCEMSklatlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESV 909

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   464 EKTKSRMSEVNEELNliRSEL----QNAGIDTHEgkrQQKRAEVLEHLKRLYPdsVFGRLFDLCHPIHKKYQLAVTKVFG 539
Cdd:pfam12128  910 KKYVEHFKNVIADHS--GSGLaetwESLREEDHY---QNDKGIRLLDYRKLVP--YLEQWFDVRVPQSIMVLREQVSILG 982


                   ....*..
gi 613410199   540 RFITAIV 546
Cdd:pfam12128  983 VDLTEFY 989
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 230-923 3.88e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.72  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   230 HNEKKIHL------LNTKLEhvnrDLSVKRESLShheNIVKARKKEHGMLTRQLQQTEKELKSV----ETLLNQKRPQYI 299
Cdd:pfam15921  101 HEKQKFYLrqsvidLQTKLQ----EMQMERDAMA---DIRRRESQSQEDLRNQLQNTVHELEAAkclkEDMLEDSNTQIE 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   300 KAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALET-ELADLDAAWRSFEKQIEEEILH-KKRDIELEasqlDRYKE 377
Cdd:pfam15921  174 QLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmHFRSLGSAISKILRELDTEISYlKGRIFPVE----DQLEA 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   378 LKEQVRKKVATMTQQ----LEKLQWEQKTD----EERLAFEKRRHGEVQGNLKQIKEQIED----HKKRIEKLEEYTKTC 445
Cdd:pfam15921  250 LKSESQNKIELLLQQhqdrIEQLISEHEVEitglTEKASSARSQANSIQSQLEIIQEQARNqnsmYMRQLSDLESTVSQL 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   446 MDCLKEKKQQEETLVDEIEKtksrmsevneELNLIRSELQNAgiDTHEGKRQQKRAEVLEHLKRLYPDsvfgrlfdlchp 525
Cdd:pfam15921  330 RSELREAKRMYEDKIEELEK----------QLVLANSELTEA--RTERDQFSQESGNLDDQLQKLLAD------------ 385

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   526 IHKKyqlavtkvfgrfitaivvasEKVakdcirfLKEERAEPETFLALDYLDIKPINERLRELKGCKMVIDVIKTQFPQL 605
Cdd:pfam15921  386 LHKR--------------------EKE-------LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAM 438

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   606 KKViqfvcgnglvCETMEEARHIALSGperqKTVALDGTLFLKSgvisggssdlkykarcwdekELKNLRDRRSQKIQEL 685
Cdd:pfam15921  439 KSE----------CQGQMERQMAAIQG----KNESLEKVSSLTA--------------------QLESTKEMLRKVVEEL 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   686 KGLMKTLRK-ETDLKQIQTLIQGTQTRLKYSQNELEMIKKKHLVAFyQEQSQLQSE---LLNIESQCIMLSEGIKERQRR 761
Cdd:pfam15921  485 TAKKMTLESsERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKL-QELQHLKNEgdhLRNVQTECEALKLQMAEKDKV 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   762 IKEFQEKIDKVEDDIFQHFceeigvENIREFENKHVKRQQEIDQKRLEFEKQKTrLNVQLEYSRSHLKKKLNKINTLK-E 840
Cdd:pfam15921  564 IEILRQQIENMTQLVGQHG------RTAGAMQVEKAQLEKEINDRRLELQEFKI-LKDKKDAKIRELEARVSDLELEKvK 636

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   841 TIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLkdirvtqNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLE 920
Cdd:pfam15921  637 LVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL-------NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709


                   ...
gi 613410199   921 QKR 923
Cdd:pfam15921  710 QTR 712
AAA_29 pfam13555
P-loop containing region of AAA domain;
4-49 4.26e-04

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 39.51  E-value: 4.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 613410199     4 LELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVM 49
Cdd:pfam13555    1 LTRLQLINWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 227-1015 4.36e-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: 4.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   227 QLYHNEKKIHLLNTKLEhvnRDLSVKRESLSHHENIVKARKKEHGMLtrQLQQTEKELKSVETLlnQKRPQYIKAKENTS 306
Cdd:pfam05483   82 KLYKEAEKIKKWKVSIE---AELKQKENKLQENRKIIEAQRKAIQEL--QFENEKVSLKLEEEI--QENKDLIKENNATR 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   307 HHLKKLdvakksikdsEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEIL-HKKRDIELEASQLDRYKELKEQvRKK 385
Cdd:pfam05483  155 HLCNLL----------KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILaFEELRVQAENARLEMHFKLKED-HEK 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   386 VATMTQQLEKlqwEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEK 465
Cdd:pfam05483  224 IQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   466 TKSRMSEVNEELNLIRSELQNAGIDTHEgKRQQKRAEVLEHLKrlypdsvfgrlfdlchpihkkyqlavTKVFGRFITAI 545
Cdd:pfam05483  301 IKMSLQRSMSTQKALEEDLQIATKTICQ-LTEEKEAQMEELNK--------------------------AKAAHSFVVTE 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   546 VVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLRELkgckmvidvikTQFPQLKKViqfvcgnglvceTMEEA 625
Cdd:pfam05483  354 FEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM-----------TKFKNNKEV------------ELEEL 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   626 RhialsgperqKTVALDGTLFlksgvisggssdlkykarcWDEKELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQtlI 705
Cdd:pfam05483  411 K----------KILAEDEKLL-------------------DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ--L 459

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   706 QGTQTRLKYSQNELEMIKkkhlvafyqeqSQLQSE-LLNIE--SQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQH-FC 781
Cdd:pfam05483  460 TAIKTSEEHYLKEVEDLK-----------TELEKEkLKNIEltAHCDKLLLENKELTQEASDMTLELKKHQEDIINCkKQ 528

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   782 EEIGVENIREFENKHVKRQQEIDQKRLEFEKQKTRLNVQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQ 861
Cdd:pfam05483  529 EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   862 TVNELMAKQQQLKdirvtQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVV--SIQTSLEQKRLEKHNLLLD---CKVQ 936
Cdd:pfam05483  609 NIEELHQENKALK-----KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidNYQKEIEDKKISEEKLLEEvekAKAI 683

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   937 DIEIILLSGSLD-----DIIEVEMGTEAESTQ---------ATIDIYEKEE--------AFEIDYSSLKEDLKALQSDQE 994
Cdd:pfam05483  684 ADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQydkiieerdSELGLYKNKEqeqssakaALEIELSNIKAELLSLKKQLE 763

                          810       820
                   ....*....|....*....|.
gi 613410199   995 IEAHLRLLLQQVASQEDILLK 1015
Cdd:pfam05483  764 IEKEEKEKLKMEAKENTAILK 784
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
149-510 4.55e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  149 KERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLE-ELKMNKIQLQLFQ 227
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAlEAELAELPERLEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  228 LYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEhgmltrQLQQTEKELKSVETLLNQKRPQYIKAKENTSH 307
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  308 HLKKLD-VAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEE--------------EILHKKRDIELEASQL 372
Cdd:COG4717   225 LEEELEqLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEA 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  373 DRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHkkrieKLEEYTKTCMDCLKEK 452
Cdd:COG4717   305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAEA 379

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199  453 KQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRL 510
Cdd:COG4717   380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL 437
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 1050-1202 4.83e-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: 42.31  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199 1050 LCRQEFEQVKKRRYDLFTQCFEHVS-ISIDQIyKKLCRNnsaqaflspenpeepyleGISYncVAPGKrfmPMDNLSGGE 1128
Cdd:cd03238    37 LVNEGLYASGKARLISFLPKFSRNKlIFIDQL-QFLIDV------------------GLGY--LTLGQ---KLSTLSGGE 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613410199 1129 KCVAALALLFAVHSFRPapFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGIYPE 1202
Cdd:cd03238    93 LQRVKLASELFSEPPGT--LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
46 PHA02562
endonuclease subunit; Provisional
 257-491 5.27e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.23  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  257 SHHENIVKARKKEHGMLTR------QLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKqe 330
Cdd:PHA02562  199 TYNKNIEEQRKKNGENIARkqnkydELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK-- 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  331 ddikaleteladldaawrsfekqiEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEER---L 407
Cdd:PHA02562  277 ------------------------VIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEImdeF 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  408 AFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEE---LNLIRSEL 484
Cdd:PHA02562  333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEkyhRGIVTDLL 412


                  ....*..
gi 613410199  485 QNAGIDT 491
Cdd:PHA02562  413 KDSGIKA 419
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-486 5.27e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  163 ELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERY-----QSLLEELKMNKIQLQLFQLYHNEKKIHL 237
Cdd:PRK03918  391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKE 470

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  238 LNTKLEHVNRDLSVKRESLSHHENIVKARKkehgmLTRQLQQTEKELKSVET-LLNQKRPQYIKAKENtshhLKKLDVAK 316
Cdd:PRK03918  471 IEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKELEEKLKKYNLeELEKKAEEYEKLKEK----LIKLKGEI 541

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  317 KSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQL----DRYKELKEqVRKKVATMTQQ 392
Cdd:PRK03918  542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELepfyNEYLELKD-AEKELEREEKE 620

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  393 LEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQI--EDHKKRIEKLEEYTKTcMDCLKEKKQQEETLVDEIEKTKSRM 470
Cdd:PRK03918  621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseEEYEELREEYLELSRE-LAGLRAELEELEKRREEIKKTLEKL 699

                         330
                  ....*....|....*.
gi 613410199  471 SEVNEELNLIRSELQN 486
Cdd:PRK03918  700 KEELEEREKAKKELEK 715
PRK01156 PRK01156
chromosome segregation protein; Provisional
 28-486 7.61e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   28 TCIIGPNGSGKSNVMDALSFVMgekIANLRVKNIQELIhgahigKPISSSASVKIIYVEESGEEKTFARIIRGGC----- 102
Cdd:PRK01156   26 NIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMI------KKGKNNLEVELEFRIGGHVYQIRRSIERRGKgsrre 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  103 SEFRFNDNLVSRSV-----YIaELEKIGII--VKAQNCLVFQGTVESISVKKPKERTQFFEEISTsgelIGEYEEKKRKL 175
Cdd:PRK01156   97 AYIKKDGSIIAEGFddttkYI-EKNILGISkdVFLNSIFVGQGEMDSLISGDPAQRKKILDEILE----INSLERNYDKL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  176 QKAEEDAQFNFNKKKNIaaerrqakleKEEAERYQSLLEELKMnkiqlqlfQLYHNEKKIHLLNTKLEHVNRDLSVKRES 255
Cdd:PRK01156  172 KDVIDMLRAEISNIDYL----------EEKLKSSNLELENIKK--------QIADDEKSHSITLKEIERLSIEYNNAMDD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  256 LSHheniVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKA 335
Cdd:PRK01156  234 YNN----LKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIEN 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  336 LETELADLDAAWRSFEKqieeeiLHKKrdieLEASQLDRYKELKEQVRKkvatmtQQLEKLQWEQKTDEErlafekrrhg 415
Cdd:PRK01156  310 KKQILSNIDAEINKYHA------IIKK----LSVLQKDYNDYIKKKSRY------DDLNNQILELEGYEM---------- 363

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613410199  416 evqgNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIektKSRMSEVNEELNLIRSELQN 486
Cdd:PRK01156  364 ----DYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI---KKELNEINVKLQDISSKVSS 427
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
3-65 7.79e-04

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 42.68  E-value: 7.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613410199    3 HLELLLVENFKSWRGRQV-IGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELI 65
Cdd:COG3950     2 RIKSLTIENFRGFEDLEIdFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 218-386 8.56e-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: 42.22  E-value: 8.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  218 MNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQ 297
Cdd:COG1579     2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  298 YIKAKENT--SHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEIlhKKRDIELEA--SQLD 373
Cdd:COG1579    82 LGNVRNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK--AELDEELAEleAELE 159

                         170
                  ....*....|...
gi 613410199  374 RYKELKEQVRKKV 386
Cdd:COG1579   160 ELEAEREELAAKI 172
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 757-926 9.12e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 9.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   757 ERQRRIKEFQEKIDKVEDDIFQHfcEEIGVE--NIREFENKHVKRQQEIDQKRLEFEKQKTRLNVQLEYSRSHLKKKLNK 834
Cdd:pfam17380  345 ERERELERIRQEERKRELERIRQ--EEIAMEisRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   835 INTLKETIQKGSEDIDHLKKAEENCLQTVN-ELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEV- 912
Cdd:pfam17380  423 EQIRAEQEEARQREVRRLEEERAREMERVRlEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELe 502

                          170
                   ....*....|....
gi 613410199   913 VSIQTSLEQKRLEK 926
Cdd:pfam17380  503 ERKQAMIEEERKRK 516
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
245-510 9.15e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  245 VNRDLSVKRESLSHHENIVKArkKEHGMLTRQLQQTEKELKSVETLL---NQKRPQYIKAKENTSHHLKKLDVAKKSIKD 321
Cdd:PRK02224  178 VERVLSDQRGSLDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIeryEEQREQARETRDEADEVLEEHEERREELET 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  322 SEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeiLHKKRDIELEASQLDRYkelkeqvrkkvatmtqqleklqwEQK 401
Cdd:PRK02224  256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEE--LEEERDDLLAEAGLDDA-----------------------DAE 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  402 TDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIR 481
Cdd:PRK02224  311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390

                         250       260       270
                  ....*....|....*....|....*....|....
gi 613410199  482 SELQN-----AGIDTHEGKRQQKRAEVLEHLKRL 510
Cdd:PRK02224  391 EEIEElrerfGDAPVDLGNAEDFLEELREERDEL 424
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 7-47 1.04e-03

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 41.87  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 613410199    7 LLVENFKSWRGRQVI----GPFRRFTCIIGPNGSGKSNVMDALSF 47
Cdd:cd03279     6 LELKNFGPFREEQVIdftgLDNNGLFLICGPTGAGKSTILDAITY 50
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 153-405 1.09e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 43.08  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  153 QFFEEISTSGELIGEYE------EKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAeryqslleELKMNKIQLQLF 226
Cdd:NF033838  129 QFKKDTLEPGKKVAEATkkveeaEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--------ELELVKEEAKEP 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  227 QlyhNEKKIHLLNTKLEHvnrdlsvKRESLSHHENIVKARKKEHGMLTRQLQQTEKEL--KSVETLLNQKRPQYIK---- 300
Cdd:NF033838  201 R---DEEKIKQAKAKVES-------KKAEATRLEKIKTDREKAEEEAKRRADAKLKEAveKNVATSEQDKPKRRAKrgvl 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  301 -------AKENTSHHL-----------------KKLDVAKKSIKDSEKQCSKQEDD---------IKALETELADLDAAW 347
Cdd:NF033838  271 gepatpdKKENDAKSSdssvgeetlpspslkpeKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntYKTLELEIAESDVKV 350

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199  348 RSFEKQIEEEILHKKRDIEleasqldRYKELKEQVRKKVATMTqQLEKLQWEQKTDEE 405
Cdd:NF033838  351 KEAELELVKEEAKEPRNEE-------KIKQAKAKVESKKAEAT-RLEKIKTDRKKAEE 400
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 210-477 1.34e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 43.09  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   210 QSLLEELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHeniVKARKKEHGMLTRQLQQTEKELKSVET 289
Cdd:pfam05667  206 PSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQ---LRSAALAGTEATSGASRSAQDLAELLS 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   290 LLNQKRP-QYIKAKENTSHHLKKLDVAK---------KSIKDSEKQC-SKQEDDIKALETELADLDA----------AWR 348
Cdd:pfam05667  283 SFSGSSTtDTGLTKGSRFTHTEKLQFTNeapaatsspPTKVETEEELqQQREEELEELQEQLEDLESsiqelekeikKLE 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   349 SFEKQIEEEIlhkkRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAfekrrhgevqgnlkQIKEQI 428
Cdd:pfam05667  363 SSIKQVEEEL----EELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLV--------------ELAGQW 424

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 613410199   429 EDHKKR-IEKLEEYTKTCMDCLKEKKQQeetlVDEIEKTKSRMSEVNEEL 477
Cdd:pfam05667  425 EKHRVPlIEEYRALKEAKSNKEDESQRK----LEEIKELREKIKEVAEEA 470
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 213-883 1.38e-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: 43.18  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   213 LEELK---MNKIQLQLFQlyhNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKAR--------KKEHGMLTRQLQQTE 281
Cdd:pfam15921  247 LEALKsesQNKIELLLQQ---HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQleiiqeqaRNQNSMYMRQLSDLE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   282 KELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIK-ALETELADLDAawRSFEKQIEEE--- 357
Cdd:pfam15921  324 STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDdQLQKLLADLHK--REKELSLEKEqnk 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   358 ------------ILHKKRDIELEASQLDRYKELKEQVRKKV-ATMTQQLEKLQWEQKTDEERLAFEKRRHgEVQGNLKQI 424
Cdd:pfam15921  402 rlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQGKNESLEKVSSLTAQLE-STKEMLRKV 480

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   425 KEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSE---LQNAGIDTHEGKRQQ-KR 500
Cdd:pfam15921  481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMaEK 560

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   501 AEVLEHLKRlypdsvfgrlfdlchPIHKKYQLAVTKvfGRFITAIVVasekvakdcirflkeERAEPEtflaldyldiKP 580
Cdd:pfam15921  561 DKVIEILRQ---------------QIENMTQLVGQH--GRTAGAMQV---------------EKAQLE----------KE 598

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   581 INERLRELKGCKMVIDVIKTQFPQLKkviqfvcgnGLVCETMEEARHIALSGPERQKTValdgtlflksgvisggsSDLK 660
Cdd:pfam15921  599 INDRRLELQEFKILKDKKDAKIRELE---------ARVSDLELEKVKLVNAGSERLRAV-----------------KDIK 652

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   661 yKARCWDEKELKNLRDRRSQKIQELKGLMKTLRKETDlkQIQTLIQGTQTRLKYSQNELEmikkkhlvafyQEQSQLQSe 740
Cdd:pfam15921  653 -QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE--EMETTTNKLKMQLKSAQSELE-----------QTRNTLKS- 717

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   741 LLNIESQCIMLSEGIkerQRRIKEFQEKIDKVEDDIfqHFCEEIGVENIREfenKHVKRQQ--EIDQKRLEFEKQKTRLN 818
Cdd:pfam15921  718 MEGSDGHAMKVAMGM---QKQITAKRGQIDALQSKI--QFLEEAMTNANKE---KHFLKEEknKLSQELSTVATEKNKMA 789

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199   819 VQLEYSRSHLKKKLNKINTLKETIQKGS----EDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSS 883
Cdd:pfam15921  790 GELEVLRSQERRLKEKVANMEVALDKASlqfaECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSS 858
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 669-923 1.43e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   669 KELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQ-TLIQGTQTRLK---YSQNELEMIKKKhlvaFYQEQSQLQSELLNI 744
Cdd:pfam01576  152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHeAMISDLEERLKkeeKGRQELEKAKRK----LEGESTDLQEQIAEL 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   745 ESQcimLSEGIKERQRRIKEFQEKIDKVEDDIFQhfcEEIGVENIREFENKHVKRQQEIDQKRL---EFEKQKTRLNVQL 821
Cdd:pfam01576  228 QAQ---IAELRAQLAKKEEELQAALARLEEETAQ---KNNALKKIRELEAQISELQEDLESERAarnKAEKQRRDLGEEL 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   822 EYSRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEEnclqtvNELMAKQQQLKDIRVTQNSSAEKVQTQIEEER------ 895
Cdd:pfam01576  302 EALKTELEDTLDTTAAQQELRSKREQEVTELKKALE------EETRSHEAQLQEMRQKHTQALEELTEQLEQAKrnkanl 375

                          250       260       270
                   ....*....|....*....|....*....|..
gi 613410199   896 -KKFLAVDREVGKLQKEVVSIQTS---LEQKR 923
Cdd:pfam01576  376 eKAKQALESENAELQAELRTLQQAkqdSEHKR 407
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
149-478 1.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  149 KERTQFFEEISTSGELIGEYEEKKRKLQKAEEdaqfnfnKKKNIaaERRQAKLEK--EEAERYQSLLEELKMNKIQLQLF 226
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERLEELKK-------KLKEL--EKRLEELEErhELYEEAKAKKEELERLKKRLTGL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  227 QLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLT----------RQL-QQTEKELKSVETLLNQKR 295
Cdd:PRK03918  385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELtEEHRKELLEEYTAELKRI 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  296 PQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQE---DDIKALETELA-----DLDAAWRSFEKqIEEEILHKKRDIEL 367
Cdd:PRK03918  465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKkynleELEKKAEEYEK-LKEKLIKLKGEIKS 543

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  368 EASQLDRYKELKEQvRKKVATMTQQLEKLQWEQKTDEERLAFEKRRhgEVQGNLKQIKE------QIEDHKKRIEKLEEY 441
Cdd:PRK03918  544 LKKELEKLEELKKK-LAELEKKLDELEEELAELLKELEELGFESVE--ELEERLKELEPfyneylELKDAEKELEREEKE 620

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 613410199  442 TKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELN 478
Cdd:PRK03918  621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
COG5022 COG5022
Myosin heavy chain [General function prediction only];
251-506 1.62e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  251 VKRESLSHHENIVKARKKEHGMLTRQLQQTEKEL---KSVETLLN--QKRPQYiKAKENTSHHLKKLDVAKKSIkdseKQ 325
Cdd:COG5022   760 LRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWrlfIKLQPLLSllGSRKEY-RSYLACIIKLQKTIKREKKL----RE 834

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  326 CSKQEDDIKALETeladLDAAWRSFEKQIEEEILHKKRDIELEASQLD----RYKELKEQVrKKVATMTQQLEKLQWE-- 399
Cdd:COG5022   835 TEEVEFSLKAEVL----IQKFGRSLKAKKRFSLLKKETIYLQSAQRVElaerQLQELKIDV-KSISSLKLVNLELESEii 909

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  400 -----QKTDE-ERLAFEKRRHGEVQGNLK--QIKEQIEDHKKRIEKLEEYTKTCMDcLKEKKQQEETLVDEIEKTKSRMS 471
Cdd:COG5022   910 elkksLSSDLiENLEFKTELIARLKKLLNniDLEEGPSIEYVKLPELNKLHEVESK-LKETSEEYEDLLKKSTILVREGN 988

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 613410199  472 EVNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEH 506
Cdd:COG5022   989 KANSELKNFKKELAELSKQYGALQESTKQLKELPV 1023
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 310-509 2.15e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  310 KKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIeeeilhkkRDIELEASQLdrykelkeqvRKKVATM 389
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------RALEQELAAL----------EAELAEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  390 TQQLEKLQWEQKTDEERLA------FEKRRHGEVQGNLKQikEQIEDHKKRIEKLEEYT---KTCMDCLKEKKQQEETLV 460
Cdd:COG4942    89 EKEIAELRAELEAQKEELAellralYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAparREQAEELRADLAELAALR 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 613410199  461 DEIEKTKSRMSEVNEELNLIRSELQNAgidthegkrQQKRAEVLEHLKR 509
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEAL---------KAERQKLLARLEK 206
recF PRK00064
recombination protein F; Reviewed
 3-47 2.19e-03

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 41.68  E-value: 2.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 613410199    3 HLELLLVENFKSWRgRQVIGPFRRFTCIIGPNGSGKSNVMDALSF 47
Cdd:PRK00064    2 YLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYL 45
PTZ00121 PTZ00121
MAEBL; Provisional
 141-509 2.37e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  141 ESISVKKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNK 220
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  221 IQLQlfQLYHNEKKIHLLNtKLEHVNRDLSVKR-------ESLSHHENIVK---------ARKKEHGMLTRQLQQTEKEL 284
Cdd:PTZ00121 1166 AEEA--RKAEDAKKAEAAR-KAEEVRKAEELRKaedarkaEAARKAEEERKaeearkaedAKKAEAVKKAEEAKKDAEEA 1242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  285 KSVETLLNQ---------------KRPQYIKAKE-NTSHHLKKLDVAKKS--IKDSEKQCSKQEDDIKALETELADlDAA 346
Cdd:PTZ00121 1243 KKAEEERNNeeirkfeearmahfaRRQAAIKAEEaRKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEEAKKAD-EAK 1321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  347 WRSFEKQIEEEILHKKRDielEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKE 426
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAE---EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  427 QIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAgidtHEGKRQQKRAEVLEH 506
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA----EEAKKKAEEAKKADE 1474


                  ...
gi 613410199  507 LKR 509
Cdd:PTZ00121 1475 AKK 1477
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 26-99 2.37e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 39.92  E-value: 2.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199   26 RFTCIIGPNGSGKSNVMDALSFVmgekianLRVKNIQELIHGAHIGKPISSSASVKIIYVEE-SGEEKTFARIIR 99
Cdd:cd00267    26 EIVALVGPNGSGKSTLLRAIAGL-------LKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlSGGQRQRVALAR 93
COG4938 COG4938
Predicted ATPase [General function prediction only];
9-53 3.22e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443965 [Multi-domain]  Cd Length: 277  Bit Score: 41.11  E-value: 3.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 613410199    9 VENFKSWRGRQVigPFRRFTCIIGPNGSGKSNVMDALSFVMGEKI 53
Cdd:COG4938     6 IKNFGPFKEAEL--ELKPLTLLIGPNGSGKSTLIQALLLLLQSNF 48
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 181-408 3.23e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  181 DAQFNFNKKKNIAAERRQAKLEKEeaerYQSLLEELkmNKIQLQLFQLyhnEKKIHLLNTKLEHVNRDLSVKRESLSHHE 260
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAE----LDALQAEL--EELNEEYNEL---QAELEALQAEIDKLQAEIAEAEAEIEERR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  261 NIVKARkkehgmlTRQLQQTEKELKSVETLLNQkrpqyikakENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETEL 340
Cdd:COG3883    86 EELGER-------ARALYRSGGSVSYLDVLLGS---------ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKK 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199  341 ADLDAAWRSFEKQIEEEILHKKrdiELEAsQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLA 408
Cdd:COG3883   150 AELEAKLAELEALKAELEAAKA---ELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 190-510 3.32e-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: 41.96  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   190 KNIAAERRQAKLEKEEAERYQSLLE---ELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENI---V 263
Cdd:TIGR00606  698 SDLQSKLRLAPDKLKSTESELKKKEkrrDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtI 777

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   264 KARKKEHGMLTRQ---LQQTEKELKSVETLLNQKRPQ---------YIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQED 331
Cdd:TIGR00606  778 MPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKlqgsdldrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   332 DIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKeQVRKKVATMTQQLEKLQWEQKTDEERLAFEK 411
Cdd:TIGR00606  858 QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK-DAKEQDSPLETFLEKDQQEKEELISSKETSN 936

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   412 RRHGEVQGNLKQIKEQIEDHKKRIEKleEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGIDT 491
Cdd:TIGR00606  937 KKAQDKVNDIKEKVKNIHGYMKDIEN--KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014

                          330
                   ....*....|....*....
gi 613410199   492 HEGKRQQKRAEVLEHLKRL 510
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEV 1033
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 315-477 3.36e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  315 AKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeiLHKKRDIELEASQLDRYKelkeQVRKKVATMTQQLE 394
Cdd:PRK05771   84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER--LEPWGNFDLDLSLLLGFK----YVSVFVGTVPEDKL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  395 KLQwEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLE------EYTKTCMDCLKEKKQQEETLVDEIEKTKS 468
Cdd:PRK05771  158 EEL-KLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGferlelEEEGTPSELIREIKEELEEIEKERESLLE 236


                  ....*....
gi 613410199  469 RMSEVNEEL 477
Cdd:PRK05771  237 ELKELAKKY 245
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 820-1048 3.88e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  820 QLEYSRSHLKKKLNKINTLKETIQKGSEDIDhlkKAEENCLQTVNELMAKQQQLKDIrvtqNSSAEKVQTQIEEERKkfl 899
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELE---ELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERRE--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  900 avdrevgKLQKEVVSIQTSLEQkrlekhnllldckVQDIEIILLSGSLDDIIE--VEMGTEAESTQATIDiyekeeafei 977
Cdd:COG3883    87 -------ELGERARALYRSGGS-------------VSYLDVLLGSESFSDFLDrlSALSKIADADADLLE---------- 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613410199  978 DYSSLKEDLKALQSD-QEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKFQESTDAFEASRKEA 1048
Cdd:COG3883   137 ELKADKAELEAKKAElEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
149-397 4.08e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  149 KERTQFFEEistsgeligEYEEKKRKLQKAEEDAQfNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQlfql 228
Cdd:COG3206   174 RKALEFLEE---------QLPELRKELEEAEAALE-EFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE---- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  229 yhnekkihllnTKLEHVNRDLSVKRESLSHHENIVKARKkehgmLTRQLQQTEKELKSVETLLNQKRPQYIKAKEntshh 308
Cdd:COG3206   240 -----------ARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRA----- 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  309 lkKLDVAKKSIKDSEKQcskqedDIKALETELADLDAAWRSFEKQIEEEilhkKRDIELEASQLDRYKELKEQVRKKVAT 388
Cdd:COG3206   299 --QIAALRAQLQQEAQR------ILASLEAELEALQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVAREL 366


                  ....*....
gi 613410199  389 MTQQLEKLQ 397
Cdd:COG3206   367 YESLLQRLE 375
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 232-456 4.11e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   232 EKKIHLLNTKLEHV---NRDLSVKRESLSHHENIVKARKKEHGMLTRQLQqteKELKSVETLLNQKRPQYIKAKENTSHH 308
Cdd:pfam05557   33 EKKASALKRQLDREsdrNQELQKRIRLLEKREAEAEEALREQAELNRLKK---KYLEALNKKLNEKESQLADAREVISCL 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   309 LKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEeiLHKKRDIELEASQ----LDRYKELKEQVRK 384
Cdd:pfam05557  110 KNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN--LEKQQSSLAEAEQrikeLEFEIQSQEQDSE 187

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613410199   385 KVATMTQQLEKLQwEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEY--TKTCMDCLKEKKQQE 456
Cdd:pfam05557  188 IVKNSKSELARIP-ELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYreEAATLELEKEKLEQE 260
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 655-895 4.22e-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: 41.36  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   655 GSSDLKYKARCwDEKELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQTLI---------QGTQTRLKYSQNELEMIKKK 725
Cdd:pfam12128  284 TSAELNQLLRT-LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAfldadietaAADQEQLPSWQSELENLEER 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   726 HlVAFYQEQSQLQSEL----LNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHFCEEIgvenirefenkhvkrQQ 801
Cdd:pfam12128  363 L-KALTGKHQDVTAKYnrrrSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL---------------RE 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   802 EIDQKRLEFEKQKTRLNVQLEysrsHLKKKLNKINT---LKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRV 878
Cdd:pfam12128  427 QLEAGKLEFNEEEYRLKSRLG----ELKLRLNQATAtpeLLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502

                          250
                   ....*....|....*..
gi 613410199   879 TQNSSAEKVQTQIEEER 895
Cdd:pfam12128  503 QASEALRQASRRLEERQ 519
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 170-474 4.41e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.58  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   170 EKKRKLQKAEEDAQFNFNKKKNiaaerrqakleKEEAERYQSLLEELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDL 249
Cdd:TIGR01612  974 DKINELDKAFKDASLNDYEAKN-----------NELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNI 1042

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   250 SvkRESLSHHENIVKARKKEHGMLTRQLQQTEKE-LKSVETLLNQ--KRPQYIK-------AKENTSHHLKKLDVAKKSI 319
Cdd:TIGR01612 1043 P--NIEIAIHTSIYNIIDEIEKEIGKNIELLNKEiLEEAEINITNfnEIKEKLKhynfddfGKEENIKYADEINKIKDDI 1120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   320 KDSEKQC-----------SKQEDDIKALETELADL-DAAWRSFEKQIEEEILHKKRDIeleASQLDRYKELKEQVrKKVA 387
Cdd:TIGR01612 1121 KNLDQKIdhhikaleeikKKSENYIDEIKAQINDLeDVADKAISNDDPEEIEKKIENI---VTKIDKKKNIYDEI-KKLL 1196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   388 TMTQQLEKlqweQKTDEERLAFEKRRHGEVQGNLkqIKEQIEDHKKR----IEKLEEYTKTcMDCLKEKKQQEETLVDEI 463
Cdd:TIGR01612 1197 NEIAEIEK----DKTSLEEVKGINLSYGKNLGKL--FLEKIDEEKKKsehmIKAMEAYIED-LDEIKEKSPEIENEMGIE 1269

                          330
                   ....*....|.
gi 613410199   464 EKTKSRMSEVN 474
Cdd:TIGR01612 1270 MDIKAEMETFN 1280
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 169-357 4.56e-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: 40.90  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  169 EEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEElKMNKIQLQLFQLyhnEKKIHLLNTKLEHVNRD 248
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAAL---EAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  249 LSVKRESLSH--------------------------------HENIVKARKKehgmLTRQLQQTEKELKSVETLLNQKRP 296
Cdd:COG4942    99 LEAQKEELAEllralyrlgrqpplalllspedfldavrrlqyLKYLAPARRE----QAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199  297 QYIKAKENTSHHLKKLDVAKKS----IKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEE 357
Cdd:COG4942   175 ELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
 1125-1182 4.71e-03

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


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 39.89  E-value: 4.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199 1125 SGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVssyikeqtqdqFQMIV 1182
Cdd:cd03277   128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKV-----------FDMLV 174
46 PHA02562
endonuclease subunit; Provisional
 297-486 4.82e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  297 QYIKAKENTSHHLK-KLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRy 375
Cdd:PHA02562  181 QQIQTLDMKIDHIQqQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK- 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  376 kelkeqVRKKVATMTQQLEKLQWEQKTDEErlafekrrHGEVqgnlKQIKEQIEDHKKRIEKLEEYTKTC---MDCLKEK 452
Cdd:PHA02562  260 ------LNTAAAKIKSKIEQFQKVIKMYEK--------GGVC----PTCTQQISEGPDRITKIKDKLKELqhsLEKLDTA 321

                         170       180       190
                  ....*....|....*....|....*....|....
gi 613410199  453 KQQEETLVDEIEKTKSRMSEVNEELNLIRSELQN 486
Cdd:PHA02562  322 IDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT 355
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
372-510 5.54e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 5.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  372 LDRYKELKEQVRKKV----------------ATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQikEQIEDHKKRI 435
Cdd:COG2433   345 YDAYKNKFERVEKKVppdvdrdevkarvirgLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEE--EEIRRLEEQV 422

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613410199  436 EKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSE---VNEELNLIRSELQNAgidTHEGKRQQKRAEVLE-HLKRL 510
Cdd:COG2433   423 ERLEAEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERL---ERELEEERERIEELKrKLERL 498
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 668-921 6.22e-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: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   668 EKELKNLRDRRSQKIQELKGLMKTLR-KETDLKQIQTLIQGTQTRLKYSQNELEMIKkkhlvafyQEQSQLQSELLNIES 746
Cdd:TIGR04523  425 EKEIERLKETIIKNNSEIKDLTNQDSvKELIIKNLDNTRESLETQLKVLSRSINKIK--------QNLEQKQKELKSKEK 496

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   747 QCIMLSEGIKERQRRIKEFQEKIDKVEddifqhfceeigvENIREFENKHVKRQQEIDQKRLEFEKQKTRLNvqleysRS 826
Cdd:TIGR04523  497 ELKKLNEEKKELEEKVKDLTKKISSLK-------------EKIEKLESEKKEKESKISDLEDELNKDDFELK------KE 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   827 HLKKKLNKINtlkETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVG 906
Cdd:TIGR04523  558 NLEKEIDEKN---KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634

                          250
                   ....*....|....*
gi 613410199   907 KLQKEVVSIQTSLEQ 921
Cdd:TIGR04523  635 NIKSKKNKLKQEVKQ 649
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 260-474 6.65e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.78  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   260 ENIVKARKKEHGMLTRQLQQT-------EKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIK---DSEKQCSKQ 329
Cdd:pfam05667  327 EELQQQREEELEELQEQLEDLessiqelEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDllpDAEENIAKL 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   330 EDDIKALETELADLDAAWrsfEKqieeeilHKKRDIEleasqldRYKELKEQVRKKVATMTQQLEKLQwEQKTDEERLAF 409
Cdd:pfam05667  407 QALVDASAQRLVELAGQW---EK-------HRVPLIE-------EYRALKEAKSNKEDESQRKLEEIK-ELREKIKEVAE 468

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199   410 EKRRHGEVQgnlKQIKEQIEDHKKRIEKlEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVN 474
Cdd:pfam05667  469 EAKQKEELY---KQLVAEYERLPKDVSR-SAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEIN 529
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
 310-476 6.78e-03

CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). 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: 129661 [Multi-domain]  Cd Length: 309  Bit Score: 40.17  E-value: 6.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   310 KKLDVAKKSIKDSekqcSKQEDDIKALeteladldAAWRSFEKQIEEEILHKKRDIELEASQ--LDRYKELKEQVRKKva 387
Cdd:TIGR00570   70 KEVDIRKRVLKIY----NKREEDFPSL--------REYNDYLEEVEDIVYNLTNNIDLENTKkkIETYQKENKDVIQK-- 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   388 tmtqQLEKLQWEQKTDEERLAFEkrrhgevqgnlkqiKEQIEDHKKRIEKLEEYTKtcmdclKEKKQQEETLVDEIEKTK 467
Cdd:TIGR00570  136 ----NKEKSTREQEELEEALEFE--------------KEEEEQRRLLLQKEEEEQQ------MNKRKNKQALLDELETST 191


                   ....*....
gi 613410199   468 SRMSEVNEE 476
Cdd:TIGR00570  192 LPAAELIAQ 200
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 201-473 6.79e-03

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 39.94  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   201 LEKEEA--ERYQSLLEELKMNKIQLQLfqlyhNEKKIHLLNTKLEHVnrdlsvkresLSHHENIVKARKKEHGmLTRQLQ 278
Cdd:pfam09728   17 EEKLAAlcKKYAELLEEMKRLQKDLKK-----LKKKQDQLQKEKDQL----------QSELSKAILAKSKLEK-LCRELQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   279 QTEKELKsvETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEei 358
Cdd:pfam09728   81 KQNKKLK--EESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEK-- 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   359 LHKKRDIE-------LEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDH 431
Cdd:pfam09728  157 LLKTKELEvqlaeakLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTF 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 613410199   432 KKRIEKLeeyTKTCMDCLKE----KKQQEET---LVDEIEKTKSRMSEV 473
Cdd:pfam09728  237 KKEMEKM---SKKIKKLEKEnltwKRKWEKSnkaLLEMAEERQKLKEEL 282
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 288-487 7.10e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 7.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  288 ETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLdaawrsfEKQIEeeilhkkrdiEL 367
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-------QAEIA----------EA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  368 EASQLDRYKELKEQVR------------------KKVATMTQQLEKLQWEQKTDEERLAfekrrhgevqgNLKQIKEQIE 429
Cdd:COG3883    78 EAEIEERREELGERARalyrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLE-----------ELKADKAELE 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 613410199  430 DHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNA 487
Cdd:COG3883   147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
149-510 7.12e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  149 KERTQFFEEISTSGELIGEYEEKKRKLQKAEEDaqfnfnkkkniaAERRQAKLEKEEAERyQSLLEELKMNKIQLQlfql 228
Cdd:PRK02224  227 EQREQARETRDEADEVLEEHEERREELETLEAE------------IEDLRETIAETERER-EELAEEVRDLRERLE---- 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  229 yhnekkihllntKLEHVNRDLSVKRESLSHHENIVKARKKEhgmLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHH 308
Cdd:PRK02224  290 ------------ELEEERDDLLAEAGLDDADAEAVEARREE---LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  309 LKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEilhkkrDIELEASQ--LDRYKELKEQVRKKV 386
Cdd:PRK02224  355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA------PVDLGNAEdfLEELREERDELRERE 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  387 ATMTQQL----------EKLQWEQKTDE-----------ERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTC 445
Cdd:PRK02224  429 AELEATLrtarerveeaEALLEAGKCPEcgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE 508

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613410199  446 --MDCLKEKKQQEETLVDEIEKTKSRMSEVNEELNLIRSELQNAGiDTHEGKRQQKRAEVLEHLKRL 510
Cdd:PRK02224  509 drIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA-EEKREAAAEAEEEAEEAREEV 574
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 162-510 8.53e-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: 40.26  E-value: 8.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   162 GELIGEYEEKKRKLQKAEEDaqfnfNKKKNIAAERRQAKLE------KEEAERYQSLLEELKMNKIQLQLFQLYHNEKKI 235
Cdd:pfam07888   44 AELLQAQEAANRQREKEKER-----YKRDREQWERQRRELEsrvaelKEELRQSREKHEELEEKYKELSASSEELSEEKD 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   236 HLLNTKLEHVNR------DLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQkrpqyikaKENTSHHL 309
Cdd:pfam07888  119 ALLAQRAAHEARireleeDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ--------TEEELRSL 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   310 -KKLDVAKKSIKDSEKQCSKQEDDIKALETEladLDAAWRsfeKQIEEEILHK-------------------KRDIELEA 369
Cdd:pfam07888  191 sKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHR---KEAENEALLEelrslqerlnaserkveglGEELSSMA 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   370 SQLDRYKELKEQVRKKVATMTQQLEKLQWEQKtdEERLAFEKRRHGeVQGNLKQIKEQIEDHKKRIEKLEEYtktcmdcL 449
Cdd:pfam07888  265 AQRDRTQAELHQARLQAAQLTLQLADASLALR--EGRARWAQERET-LQQSAEADKDRIEKLSAELQRLEER-------L 334

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199   450 KEKKQQEETLVDEI--EKTKSR--MSEVNEELNLIRSELQNAgiDTHEGKRQQKRAEVLEHLKRL 510
Cdd:pfam07888  335 QEERMEREKLEVELgrEKDCNRvqLSESRRELQELKASLRVA--QKEKEQLQAEKQELLEYIRQL 397
46 PHA02562
endonuclease subunit; Provisional
 331-501 8.69e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 8.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  331 DDIKALETELADLDAAWRSFEKQIEeeiLHKKRDIELEASQ---LDRYKELKEQVRKKVATMTQQLEKLQweqktdEERL 407
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQQIK---TYNKNIEEQRKKNgenIARKQNKYDELVEEAKTIKAEIEELT------DELL 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  408 AFEKRRhGEVQGNLK-------QIKEQIEDHKKRIEKLEEYTkTCMDClkekKQQEETLVDEIEKTKSRMSEVNEELNLI 480
Cdd:PHA02562  245 NLVMDI-EDPSAALNklntaaaKIKSKIEQFQKVIKMYEKGG-VCPTC----TQQISEGPDRITKIKDKLKELQHSLEKL 318

                         170       180
                  ....*....|....*....|.
gi 613410199  481 RSELQNAGIDTHEGKRQQKRA 501
Cdd:PHA02562  319 DTAIDELEEIMDEFNEQSKKL 339
46 PHA02562
endonuclease subunit; Provisional
 630-927 8.77e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 8.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  630 LSGPERQKTVAlDgtlFLKSGVISGGSSDLKYKARCWDE--KELKNLRDRRSQKIQELKGLMKTLRKETDLKQiqtliqg 707
Cdd:PHA02562  147 LSAPARRKLVE-D---LLDISVLSEMDKLNKDKIRELNQqiQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENI------- 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  708 TQTRLKYSQNeLEMIKKKHlvafyQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIfqHFCEEIGV- 786
Cdd:PHA02562  216 ARKQNKYDEL-VEEAKTIK-----AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVI--KMYEKGGVc 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199  787 ----ENIREFENKHVKRQQEIDQKRLEFEKQKTRlnvqleysRSHLKKKLNKINTLKetiqkgsedidhlkkaeenclQT 862
Cdd:PHA02562  288 ptctQQISEGPDRITKIKDKLKELQHSLEKLDTA--------IDELEEIMDEFNEQS---------------------KK 338

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613410199  863 VNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKH 927
Cdd:PHA02562  339 LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY 403
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 26-65 8.91e-03

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: 38.57  E-value: 8.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 613410199   26 RFTCIIGPNGSGKSNVMDALS----------FVMGEKIANLRVKNIQELI 65
Cdd:cd03214    26 EIVGILGPNGAGKSTLLKTLAgllkpssgeiLLDGKDLASLSPKELARKI 75
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 160-495 8.92e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   160 TSGELIGEYEEKKRKLQKAEEDAQFNfnkkkniaaeRRQAKLEKEEAERYQSLLEELKMNKIQL--QLFQLYHNEKKIHL 237
Cdd:TIGR00606  823 TVQQVNQEKQEKQHELDTVVSKIELN----------RKLIQDQQEQIQHLKSKTNELKSEKLQIgtNLQRRQQFEEQLVE 892

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   238 LNTKLEHVNRDLSVKRESLSHHEnivkarkkehgmltrqlQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKK 317
Cdd:TIGR00606  893 LSTEVQSLIREIKDAKEQDSPLE-----------------TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHG 955

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   318 SIKDSEKQCSKQEDD-IKALETELADLDAAWRSFEK---QIEEEILHKKRDIELEASQ-------------LDRYKELKE 380
Cdd:TIGR00606  956 YMKDIENKIQDGKDDyLKQKETELNTVNAQLEECEKhqeKINEDMRLMRQDIDTQKIQerwlqdnltlrkrENELKEVEE 1035

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613410199   381 QVRKKVATMTQ-QLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEkleeyTKTCMDClkEKKQQEETL 459
Cdd:TIGR00606 1036 ELKQHLKEMGQmQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELR-----EPQFRDA--EEKYREMMI 1108

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 613410199   460 VDEIEKtksrmsEVNEELNLIRSELQNAGIDTHEGK 495
Cdd:TIGR00606 1109 VMRTTE------LVNKDLDIYYKTLDQAIMKFHSMK 1138
 
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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