NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1512063858|gb|RNJ64519|]
View 

DNA mismatch repair protein MutS [Porphyrobacter sp. IPPAS B-1204]

Protein Classification

DNA mismatch repair protein MutS( domain architecture ID 11415631)

DNA mismatch repair protein MutS, binds to DNA with mismatched base pairs and initiates repair

Gene Symbol:  mutS
Gene Ontology:  GO:0030983|GO:1990710|GO:0032300|GO:0043531|GO:0005524|GO:0016887|GO:0140664|GO:0003684|GO:0006974|GO:0006298
PubMed:  9722651|26163658
SCOP:  4004015

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
1-864 0e+00

DNA mismatch repair ATPase MutS [Replication, recombination and repair];


:

Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 1157.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858   1 MMAQYLALREEAGDALLFYRMGDFFELFFEDARTAAQILDIALTTRGEHGGAPIPMCGVPVHSAEGYLARLIKAGCRVAI 80
Cdd:COG0249    10 MMQQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGEPIPMAGVPYHAAEGYLAKLVKAGYKVAI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  81 AEQVETPDEAKArakregtpssktLVGRAIVRLVTAGTLTEEALLEPRRANVLAALAELRGAVGIAAVDVSTGAMVLEEC 160
Cdd:COG0249    90 CEQVEDPAEAKG------------LVKREVVRVVTPGTLTEDALLDAKRNNYLAAVARDKGRYGLAWLDISTGEFLVTEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 161 A-ADQLGAALARLSPSEVVVPEDWQHGPD--EAI--------HRPRSTFASDAGAERLKAVHGVATLDAFG-DFSRAMLG 228
Cdd:COG0249   158 DgEEALLDELARLAPAEILVPEDLPDPEEllELLrergaavtRLPDWAFDPDAARRRLLEQFGVASLDGFGlEDLPAAIA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 229 AAGGLIAYLDHVGRGRLPLLLPPVARAGEAGMAMDAATRASLEILESTTGGRSGSLIGAVDRCVTGAGSRLLAEDLSAPL 308
Cdd:COG0249   238 AAGALLAYLEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGGRKGSLLSVLDRTVTAMGSRLLRRWLLRPL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 309 LDAAAIEARLALVQFWLTRPIERAQLRDALRGIPDLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLSGAPdrPSLL 388
Cdd:COG0249   318 RDRAAIEARLDAVEELLEDPLLREELRELLKGVYDLERLLSRIALGRANPRDLAALRDSLAALPELKELLAELD--SPLL 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 389 DQVLAKLTGHGALTDWLGRALVPNPPTERGSGGYIADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGV 468
Cdd:COG0249   396 AELAEALDPLEDLAELLERAIVDEPPLLIRDGGVIREGYDAELDELRELSENGKEWLAELEARERERTGIKSLKVGYNKV 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 469 LGYFIEVSARHADRLmaPDSgFTHRQTMKDAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAA 548
Cdd:COG0249   476 FGYYIEVTKANADKV--PDD-YIRKQTLKNAERYITPELKELEDKILSAEERALALEYELFEELREEVAAHIERLQALAR 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 549 ALARLDVGAGNAERASEADWCRPDIAEDAGLAITAGRHPVVEAALAkaGDRFVANDCQLADTNRLWLIGGPNMGGKSTFL 628
Cdd:COG0249   553 ALAELDVLASLAEVAVENNYVRPELDDSPGIEIEGGRHPVVEQALP--GEPFVPNDCDLDPDRRILLITGPNMAGKSTYM 630

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 629 RQNALIVLLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDG 708
Cdd:COG0249   631 RQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDG 710

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 709 LALAWAVAEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAP 788
Cdd:COG0249   711 LSIAWAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSYGIHVAKLAGLPAS 790

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512063858 789 VVARAKAVLEKLEAtREATGGIAAGLGDLPLFAMLAAQPpqaspeQQLADALRTADLDALTPREALDLLYEWKRNL 864
Cdd:COG0249   791 VIERAREILAELEK-GEAAAAGKAAPDQLSLFAAADPEP------SPVLEELKALDPDELTPREALNLLYELKKLL 859
 
Name Accession Description Interval E-value
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
1-864 0e+00

DNA mismatch repair ATPase MutS [Replication, recombination and repair];


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 1157.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858   1 MMAQYLALREEAGDALLFYRMGDFFELFFEDARTAAQILDIALTTRGEHGGAPIPMCGVPVHSAEGYLARLIKAGCRVAI 80
Cdd:COG0249    10 MMQQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGEPIPMAGVPYHAAEGYLAKLVKAGYKVAI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  81 AEQVETPDEAKArakregtpssktLVGRAIVRLVTAGTLTEEALLEPRRANVLAALAELRGAVGIAAVDVSTGAMVLEEC 160
Cdd:COG0249    90 CEQVEDPAEAKG------------LVKREVVRVVTPGTLTEDALLDAKRNNYLAAVARDKGRYGLAWLDISTGEFLVTEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 161 A-ADQLGAALARLSPSEVVVPEDWQHGPD--EAI--------HRPRSTFASDAGAERLKAVHGVATLDAFG-DFSRAMLG 228
Cdd:COG0249   158 DgEEALLDELARLAPAEILVPEDLPDPEEllELLrergaavtRLPDWAFDPDAARRRLLEQFGVASLDGFGlEDLPAAIA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 229 AAGGLIAYLDHVGRGRLPLLLPPVARAGEAGMAMDAATRASLEILESTTGGRSGSLIGAVDRCVTGAGSRLLAEDLSAPL 308
Cdd:COG0249   238 AAGALLAYLEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGGRKGSLLSVLDRTVTAMGSRLLRRWLLRPL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 309 LDAAAIEARLALVQFWLTRPIERAQLRDALRGIPDLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLSGAPdrPSLL 388
Cdd:COG0249   318 RDRAAIEARLDAVEELLEDPLLREELRELLKGVYDLERLLSRIALGRANPRDLAALRDSLAALPELKELLAELD--SPLL 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 389 DQVLAKLTGHGALTDWLGRALVPNPPTERGSGGYIADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGV 468
Cdd:COG0249   396 AELAEALDPLEDLAELLERAIVDEPPLLIRDGGVIREGYDAELDELRELSENGKEWLAELEARERERTGIKSLKVGYNKV 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 469 LGYFIEVSARHADRLmaPDSgFTHRQTMKDAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAA 548
Cdd:COG0249   476 FGYYIEVTKANADKV--PDD-YIRKQTLKNAERYITPELKELEDKILSAEERALALEYELFEELREEVAAHIERLQALAR 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 549 ALARLDVGAGNAERASEADWCRPDIAEDAGLAITAGRHPVVEAALAkaGDRFVANDCQLADTNRLWLIGGPNMGGKSTFL 628
Cdd:COG0249   553 ALAELDVLASLAEVAVENNYVRPELDDSPGIEIEGGRHPVVEQALP--GEPFVPNDCDLDPDRRILLITGPNMAGKSTYM 630

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 629 RQNALIVLLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDG 708
Cdd:COG0249   631 RQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDG 710

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 709 LALAWAVAEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAP 788
Cdd:COG0249   711 LSIAWAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSYGIHVAKLAGLPAS 790

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512063858 789 VVARAKAVLEKLEAtREATGGIAAGLGDLPLFAMLAAQPpqaspeQQLADALRTADLDALTPREALDLLYEWKRNL 864
Cdd:COG0249   791 VIERAREILAELEK-GEAAAAGKAAPDQLSLFAAADPEP------SPVLEELKALDPDELTPREALNLLYELKKLL 859
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 1-866 0e+00

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 1154.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858   1 MMAQYLALREEAGDALLFYRMGDFFELFFEDARTAAQILDIALTTRGEHGGAPIPMCGVPVHSAEGYLARLIKAGCRVAI 80
Cdd:PRK05399   11 MMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVPYHAAEGYLAKLVKKGYKVAI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  81 AEQVETPDEAKArakregtpssktLVGRAIVRLVTAGTLTEEALLEPRRANVLAALAELRGAVGIAAVDVSTGAMVLEEC 160
Cdd:PRK05399   91 CEQVEDPATAKG------------PVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGGYGLAYLDLSTGEFRVTEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 161 AADQLGAALARLSPSEVVVPEDWQHGPDEAIHRPRST-----FASDAGAERLKAVHGVATLDAFGDFSRAMLGAAGGLIA 235
Cdd:PRK05399  159 DEEELLAELARLNPAEILVPEDFSEDELLLLRRGLRRrppweFDLDTAEKRLLEQFGVASLDGFGVDLPLAIRAAGALLQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 236 YLDHVGRGRLPLLLPPVARAGEAGMAMDAATRASLEILESTTGGRSGSLIGAVDRCVTGAGSRLLAEDLSAPLLDAAAIE 315
Cdd:PRK05399  239 YLKETQKRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 316 ARLALVQFWLTRPIERAQLRDALRGIPDLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLSGAPdrPSLLDQVLAKL 395
Cdd:PRK05399  319 ARLDAVEELLEDPLLREDLRELLKGVYDLERLLSRIALGRANPRDLAALRDSLEALPELKELLAELD--SPLLAELAEQL 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 396 TGHGALTDWLGRALVPNPPTERGSGGYIADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGVLGYFIEV 475
Cdd:PRK05399  397 DPLEELADLLERAIVEEPPLLIRDGGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIEV 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 476 SARHADrlMAPDsGFTHRQTMKDAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAAALARLDV 555
Cdd:PRK05399  477 TKANLD--KVPE-DYIRRQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDV 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 556 GAGNAERASEADWCRPDIAEDAGLAITAGRHPVVEAALAkaGDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIV 635
Cdd:PRK05399  554 LASLAEVAEENNYVRPEFTDDPGIDIEEGRHPVVEQVLG--GEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIV 631

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 636 LLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAV 715
Cdd:PRK05399  632 LLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAV 711

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 716 AEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKA 795
Cdd:PRK05399  712 AEYLHDKIGAKTLFATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRARE 791

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512063858 796 VLEKLEATREATGGIAAGLGDLPLFAmlaaqppqASPEQQLADALRTADLDALTPREALDLLYEWKRNLPK 866
Cdd:PRK05399  792 ILAQLESASEKAKAASAEEDQLSLFA--------EPEESPLLEALKALDPDNLTPREALNLLYELKKLLKK 854
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
 1-862 0e+00

DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 730.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858   1 MMAQYLALREEAGDALLFYRMGDFFELFFEDARTAAQILDIALTTRGEHGGAPIPMCGVPVHSAEGYLARLIKAGCRVAI 80
Cdd:TIGR01070   4 MMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADEPIPMAGIPYHAVEAYLEKLVKQGESVAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  81 AEQVETPDEAKARAKREgtpssktlvgraIVRLVTAGTLTEEALLEPRRANVLAALAELRGAVGIAAVDVSTGAMVLEEC 160
Cdd:TIGR01070  84 CEQIEDPKTAKGPVERE------------VVQLITPGTVSDEALLPERQDNLLAAIAQESNGFGLATLDLTTGEFKVTEL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 161 AA-DQLGAALARLSPSEVVVPEDWQHGpDEAIHRPrstFASDAGAERLKAVHGVATLDAFG-DFSRAMLGAAGGLIAYLD 238
Cdd:TIGR01070 152 ADkETLYAELQRLNPAEVLLAEDLSEM-EAIELRE---FRKDTAVMSLEAQFGTEDLGGLGlRNAPLGLTAAGCLLQYAK 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 239 HVGRGRLPLLLPPVARAGEAGMAMDAATRASLEILESTTGGRSGSLIGAVDRCVTGAGSRLLAEDLSAPLLDAAAIEARL 318
Cdd:TIGR01070 228 RTQRTALPHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQNTLFSVLDETKTAMGSRLLKRWLHRPLRDREVLEARQ 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 319 ALVQFWLTRPIERAQLRDALRGIPDLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLsgAPDRPSLLDQVLAKLTGH 398
Cdd:TIGR01070 308 DTVEVLLRHFFLREGLRPLLKEVGDLERLAARVALGNARPRDLARLRTSLEQLPELRALL--EELEGPTLQALAAQIDDF 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 399 GALTDWLGRALVPNPPTERGSGGYIADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGVLGYFIEVSAR 478
Cdd:TIGR01070 386 SELLELLEAALIENPPLVVRDGGLIREGYDEELDELRAASREGTDYLARLEARERERTGIPTLKVGYNAVFGYYIEVTRG 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 479 HADRLMApdsGFTHRQTMKDAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAAALARLDVGAG 558
Cdd:TIGR01070 466 QLHLVPA---HYRRRQTLKNAERYITPELKEKEDKVLEAEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLAN 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 559 NAERASEADWCRPDIAEDAGLAITAGRHPVVEAALAKAgdrFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLA 638
Cdd:TIGR01070 543 LAEVAETLHYTRPRFGDDPQLRIREGRHPVVEQVLRTP---FVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLA 619

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 639 QAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEA 718
Cdd:TIGR01070 620 QIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEY 699

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 719 VHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKAVLE 798
Cdd:TIGR01070 700 LHEHIRAKTLFATHYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILT 779

                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512063858 799 KLEATREATggiaaglgDLPLFAMLAAQPPQASP-----EQQLADALRTADLDALTPREALDLLYEWKR 862
Cdd:TIGR01070 780 QLEARSTES--------EAPQRKAQTSAPEQISLfdeaeTHPLLEELAKLDPDDLTPLQALNLLYELKK 840
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
 581-797 1.32e-118

ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213251 [Multi-domain]  Cd Length: 216  Bit Score: 358.50  E-value: 1.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 581 ITAGRHPVVEAALAKagDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFSR 660
Cdd:cd03284     2 IEGGRHPVVEQVLDN--EPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 661 VGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARLA 740
Cdd:cd03284    80 IGASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTELE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512063858 741 ETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKAVL 797
Cdd:cd03284   160 GKLPRVKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERAREIL 216
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 614-801 6.75e-106

MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters.


Pssm-ID: 425714 [Multi-domain]  Cd Length: 188  Bit Score: 324.15  E-value: 6.75e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 614 WLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSF 693
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 694 VILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADR 773
Cdd:pfam00488  81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAADK 160

                         170       180
                  ....*....|....*....|....*...
gi 1512063858 774 SYGLAVARLAGVPAPVVARAKAVLEKLE 801
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERAREILAELE 188
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
613-797 1.21e-90

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 284.06  E-value: 1.21e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  613 LWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRS 692
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  693 FVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPAD 772
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVAG 160

                          170       180
                   ....*....|....*....|....*
gi 1512063858  773 RSYGLAVARLAGVPAPVVARAKAVL 797
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
 
Name Accession Description Interval E-value
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
1-864 0e+00

DNA mismatch repair ATPase MutS [Replication, recombination and repair];


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 1157.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858   1 MMAQYLALREEAGDALLFYRMGDFFELFFEDARTAAQILDIALTTRGEHGGAPIPMCGVPVHSAEGYLARLIKAGCRVAI 80
Cdd:COG0249    10 MMQQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGEPIPMAGVPYHAAEGYLAKLVKAGYKVAI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  81 AEQVETPDEAKArakregtpssktLVGRAIVRLVTAGTLTEEALLEPRRANVLAALAELRGAVGIAAVDVSTGAMVLEEC 160
Cdd:COG0249    90 CEQVEDPAEAKG------------LVKREVVRVVTPGTLTEDALLDAKRNNYLAAVARDKGRYGLAWLDISTGEFLVTEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 161 A-ADQLGAALARLSPSEVVVPEDWQHGPD--EAI--------HRPRSTFASDAGAERLKAVHGVATLDAFG-DFSRAMLG 228
Cdd:COG0249   158 DgEEALLDELARLAPAEILVPEDLPDPEEllELLrergaavtRLPDWAFDPDAARRRLLEQFGVASLDGFGlEDLPAAIA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 229 AAGGLIAYLDHVGRGRLPLLLPPVARAGEAGMAMDAATRASLEILESTTGGRSGSLIGAVDRCVTGAGSRLLAEDLSAPL 308
Cdd:COG0249   238 AAGALLAYLEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGGRKGSLLSVLDRTVTAMGSRLLRRWLLRPL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 309 LDAAAIEARLALVQFWLTRPIERAQLRDALRGIPDLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLSGAPdrPSLL 388
Cdd:COG0249   318 RDRAAIEARLDAVEELLEDPLLREELRELLKGVYDLERLLSRIALGRANPRDLAALRDSLAALPELKELLAELD--SPLL 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 389 DQVLAKLTGHGALTDWLGRALVPNPPTERGSGGYIADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGV 468
Cdd:COG0249   396 AELAEALDPLEDLAELLERAIVDEPPLLIRDGGVIREGYDAELDELRELSENGKEWLAELEARERERTGIKSLKVGYNKV 475

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 469 LGYFIEVSARHADRLmaPDSgFTHRQTMKDAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAA 548
Cdd:COG0249   476 FGYYIEVTKANADKV--PDD-YIRKQTLKNAERYITPELKELEDKILSAEERALALEYELFEELREEVAAHIERLQALAR 552

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 549 ALARLDVGAGNAERASEADWCRPDIAEDAGLAITAGRHPVVEAALAkaGDRFVANDCQLADTNRLWLIGGPNMGGKSTFL 628
Cdd:COG0249   553 ALAELDVLASLAEVAVENNYVRPELDDSPGIEIEGGRHPVVEQALP--GEPFVPNDCDLDPDRRILLITGPNMAGKSTYM 630

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 629 RQNALIVLLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDG 708
Cdd:COG0249   631 RQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDG 710

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 709 LALAWAVAEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAP 788
Cdd:COG0249   711 LSIAWAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSYGIHVAKLAGLPAS 790

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512063858 789 VVARAKAVLEKLEAtREATGGIAAGLGDLPLFAMLAAQPpqaspeQQLADALRTADLDALTPREALDLLYEWKRNL 864
Cdd:COG0249   791 VIERAREILAELEK-GEAAAAGKAAPDQLSLFAAADPEP------SPVLEELKALDPDELTPREALNLLYELKKLL 859
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 1-866 0e+00

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 1154.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858   1 MMAQYLALREEAGDALLFYRMGDFFELFFEDARTAAQILDIALTTRGEHGGAPIPMCGVPVHSAEGYLARLIKAGCRVAI 80
Cdd:PRK05399   11 MMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVPYHAAEGYLAKLVKKGYKVAI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  81 AEQVETPDEAKArakregtpssktLVGRAIVRLVTAGTLTEEALLEPRRANVLAALAELRGAVGIAAVDVSTGAMVLEEC 160
Cdd:PRK05399   91 CEQVEDPATAKG------------PVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGGYGLAYLDLSTGEFRVTEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 161 AADQLGAALARLSPSEVVVPEDWQHGPDEAIHRPRST-----FASDAGAERLKAVHGVATLDAFGDFSRAMLGAAGGLIA 235
Cdd:PRK05399  159 DEEELLAELARLNPAEILVPEDFSEDELLLLRRGLRRrppweFDLDTAEKRLLEQFGVASLDGFGVDLPLAIRAAGALLQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 236 YLDHVGRGRLPLLLPPVARAGEAGMAMDAATRASLEILESTTGGRSGSLIGAVDRCVTGAGSRLLAEDLSAPLLDAAAIE 315
Cdd:PRK05399  239 YLKETQKRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 316 ARLALVQFWLTRPIERAQLRDALRGIPDLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLSGAPdrPSLLDQVLAKL 395
Cdd:PRK05399  319 ARLDAVEELLEDPLLREDLRELLKGVYDLERLLSRIALGRANPRDLAALRDSLEALPELKELLAELD--SPLLAELAEQL 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 396 TGHGALTDWLGRALVPNPPTERGSGGYIADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGVLGYFIEV 475
Cdd:PRK05399  397 DPLEELADLLERAIVEEPPLLIRDGGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIEV 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 476 SARHADrlMAPDsGFTHRQTMKDAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAAALARLDV 555
Cdd:PRK05399  477 TKANLD--KVPE-DYIRRQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDV 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 556 GAGNAERASEADWCRPDIAEDAGLAITAGRHPVVEAALAkaGDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIV 635
Cdd:PRK05399  554 LASLAEVAEENNYVRPEFTDDPGIDIEEGRHPVVEQVLG--GEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIV 631

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 636 LLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAV 715
Cdd:PRK05399  632 LLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAV 711

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 716 AEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKA 795
Cdd:PRK05399  712 AEYLHDKIGAKTLFATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRARE 791

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512063858 796 VLEKLEATREATGGIAAGLGDLPLFAmlaaqppqASPEQQLADALRTADLDALTPREALDLLYEWKRNLPK 866
Cdd:PRK05399  792 ILAQLESASEKAKAASAEEDQLSLFA--------EPEESPLLEALKALDPDNLTPREALNLLYELKKLLKK 854
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
 1-862 0e+00

DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 730.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858   1 MMAQYLALREEAGDALLFYRMGDFFELFFEDARTAAQILDIALTTRGEHGGAPIPMCGVPVHSAEGYLARLIKAGCRVAI 80
Cdd:TIGR01070   4 MMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADEPIPMAGIPYHAVEAYLEKLVKQGESVAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  81 AEQVETPDEAKARAKREgtpssktlvgraIVRLVTAGTLTEEALLEPRRANVLAALAELRGAVGIAAVDVSTGAMVLEEC 160
Cdd:TIGR01070  84 CEQIEDPKTAKGPVERE------------VVQLITPGTVSDEALLPERQDNLLAAIAQESNGFGLATLDLTTGEFKVTEL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 161 AA-DQLGAALARLSPSEVVVPEDWQHGpDEAIHRPrstFASDAGAERLKAVHGVATLDAFG-DFSRAMLGAAGGLIAYLD 238
Cdd:TIGR01070 152 ADkETLYAELQRLNPAEVLLAEDLSEM-EAIELRE---FRKDTAVMSLEAQFGTEDLGGLGlRNAPLGLTAAGCLLQYAK 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 239 HVGRGRLPLLLPPVARAGEAGMAMDAATRASLEILESTTGGRSGSLIGAVDRCVTGAGSRLLAEDLSAPLLDAAAIEARL 318
Cdd:TIGR01070 228 RTQRTALPHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQNTLFSVLDETKTAMGSRLLKRWLHRPLRDREVLEARQ 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 319 ALVQFWLTRPIERAQLRDALRGIPDLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLsgAPDRPSLLDQVLAKLTGH 398
Cdd:TIGR01070 308 DTVEVLLRHFFLREGLRPLLKEVGDLERLAARVALGNARPRDLARLRTSLEQLPELRALL--EELEGPTLQALAAQIDDF 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 399 GALTDWLGRALVPNPPTERGSGGYIADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGVLGYFIEVSAR 478
Cdd:TIGR01070 386 SELLELLEAALIENPPLVVRDGGLIREGYDEELDELRAASREGTDYLARLEARERERTGIPTLKVGYNAVFGYYIEVTRG 465

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 479 HADRLMApdsGFTHRQTMKDAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAAALARLDVGAG 558
Cdd:TIGR01070 466 QLHLVPA---HYRRRQTLKNAERYITPELKEKEDKVLEAEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLAN 542

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 559 NAERASEADWCRPDIAEDAGLAITAGRHPVVEAALAKAgdrFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLA 638
Cdd:TIGR01070 543 LAEVAETLHYTRPRFGDDPQLRIREGRHPVVEQVLRTP---FVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLA 619

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 639 QAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEA 718
Cdd:TIGR01070 620 QIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEY 699

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 719 VHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKAVLE 798
Cdd:TIGR01070 700 LHEHIRAKTLFATHYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILT 779

                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512063858 799 KLEATREATggiaaglgDLPLFAMLAAQPPQASP-----EQQLADALRTADLDALTPREALDLLYEWKR 862
Cdd:TIGR01070 780 QLEARSTES--------EAPQRKAQTSAPEQISLfdeaeTHPLLEELAKLDPDDLTPLQALNLLYELKK 840
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
 581-797 1.32e-118

ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213251 [Multi-domain]  Cd Length: 216  Bit Score: 358.50  E-value: 1.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 581 ITAGRHPVVEAALAKagDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFSR 660
Cdd:cd03284     2 IEGGRHPVVEQVLDN--EPFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 661 VGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARLA 740
Cdd:cd03284    80 IGASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTELE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512063858 741 ETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKAVL 797
Cdd:cd03284   160 GKLPRVKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERAREIL 216
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 614-801 6.75e-106

MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters.


Pssm-ID: 425714 [Multi-domain]  Cd Length: 188  Bit Score: 324.15  E-value: 6.75e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 614 WLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSF 693
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 694 VILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADR 773
Cdd:pfam00488  81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAADK 160

                         170       180
                  ....*....|....*....|....*...
gi 1512063858 774 SYGLAVARLAGVPAPVVARAKAVLEKLE 801
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERAREILAELE 188
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
613-797 1.21e-90

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 284.06  E-value: 1.21e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  613 LWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRS 692
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  693 FVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARLAETCEALSLHHVRAREWQGDLVLLHELADGPAD 772
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVAG 160

                          170       180
                   ....*....|....*....|....*
gi 1512063858  773 RSYGLAVARLAGVPAPVVARAKAVL 797
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
 581-801 7.86e-83

ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213252 [Multi-domain]  Cd Length: 222  Bit Score: 265.01  E-value: 7.86e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 581 ITAGRHPVVEAALAKAgdrFVANDCQLA-DTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFS 659
Cdd:cd03285     2 LKEARHPCVEAQDDVA---FIPNDVTLTrGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 660 RVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARL 739
Cdd:cd03285    79 RVGASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQIKCFCLFATHFHELTAL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512063858 740 AETCEALSLHHVRAR--EWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKAVLEKLE 801
Cdd:cd03285   159 ADEVPNVKNLHVTALtdDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQKALELE 222
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
 580-785 2.92e-81

ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213210 [Multi-domain]  Cd Length: 202  Bit Score: 259.87  E-value: 2.92e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 580 AITAGRHPVVEAALAkaGDRFVANDCQLADTnRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFS 659
Cdd:cd03243     1 EIKGGRHPVLLALTK--GETFVPNDINLGSG-RLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 660 RVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHtQIRCRCLFATHYHELARL 739
Cdd:cd03243    78 RIGAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLL-EKGCRTLFATHFHELADL 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1512063858 740 AETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGV 785
Cdd:cd03243   157 PEQVPGVKNLHMEELITTGGLTFTYKLIDGICDPSYALQIAELAGL 202
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
 579-793 6.17e-67

ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213254 [Multi-domain]  Cd Length: 222  Bit Score: 222.36  E-value: 6.17e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 579 LAITAGRHPVVEAALakaGDRFVANDCQL-ADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRL 657
Cdd:cd03287     1 ILIKEGRHPMIESLL---DKSFVPNDIHLsAEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 658 FSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELA 737
Cdd:cd03287    78 LTRMGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEKKCLVLFVTHYPSLG 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512063858 738 RLAETCE-ALSLHHVRAREWQ--------GDLVLLHELADGPADRSYGLAVARLAGVPAPVVARA 793
Cdd:cd03287   158 EILRRFEgSIRNYHMSYLESQkdfetsdsQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
MutS_III pfam05192
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 265-537 1.91e-66

MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam05188, pfam01624 and pfam05190. The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain III, which is central to the structure of Thermus aquaticus MutS as characterized in.


Pssm-ID: 461579 [Multi-domain]  Cd Length: 291  Bit Score: 223.44  E-value: 1.91e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 265 ATRASLEILESTTGGRSGSLIGAVDRCVTGAGSRLLAEDLSAPLLDAAAIEARLALVQFWLTRPIERAQLRDALRGIPDL 344
Cdd:pfam05192   1 ATLRNLELTENLRGGKEGSLLGLLDRTKTPMGSRLLRQWLLQPLTDLEEINERLDAVEELLENSELREDLRELLRRLPDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 345 GRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLSGAPDRPSLLDQVLAKLtghgaltdwLGRALVPNPPTERGSGGYIA 424
Cdd:pfam05192  81 ERLLSRIALGKATPRDLLALLDSLEKLPLLKELLLEEKSALLGELASLAEL---------LEEAIDEEPPALLRDGGVIR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 425 DGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGVLGY-------FIEVSARHADRLmapDSGFTHRQTMK 497
Cdd:pfam05192 152 DGYDEELDELRDLLLDGKRLLAKLEARERERTGIKSLKVLYNKVFGYylllveyYIEVSKSQKDKV---PDDYIRIQTTK 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1512063858 498 DAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIV 537
Cdd:pfam05192 229 NAERYITPELKELERKILQAEERLLALEKELFEELLEEVL 268
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
 584-793 1.29e-65

ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213253 [Multi-domain]  Cd Length: 218  Bit Score: 218.45  E-value: 1.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 584 GRHPVVEAALAKAgdrFVANDCQLADTN-RLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFSRVG 662
Cdd:cd03286     5 LRHPCLNASTASS---FVPNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFTRIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 663 AADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARLAET 742
Cdd:cd03286    82 ARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKCLTLFSTHYHSLCDEFHE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512063858 743 CEALSLHHV------RAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARA 793
Cdd:cd03286   162 HGGVRLGHMacavknESDPTIRDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
281-591 7.44e-57

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 197.91  E-value: 7.44e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  281 SGSLIGAVDRCVTGAGSRLLAEDLSAPLLDAAAIEARLALVQFWLTRPIERAQLRDALRGIPDLGRALGRVVAGRGSPRD 360
Cdd:smart00533   1 KGSLFELLNHTKTPMGKRLLRRWLLQPLLDLKEINERLDAVEELVENPELRQKLRQLLKRIPDLERLLSRIERGRASPRD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  361 LGQLRDGLSEAMRLHHWLSGAPDRP-SLLDQVLakLTGHGALTDWLGRALVPNPPTERGSGGYIADGYDAALDELRATSG 439
Cdd:smart00533  81 LLRLYDSLEGLKEIRQLLESLDGPLlGLLLKVI--LEPLLELLELLLELLNDDDPLEVNDGGLIKDGFDPELDELREKLE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  440 DARRAIAAMEARYRDETGIATLKIRHNGVLGYFIEVSARHADRLmapDSGFTHRQTMKDAVRFNSLKLHEEAARIAEAGG 519
Cdd:smart00533 159 ELEEELEELLKKEREELGIDSLKLGYNKVHGYYIEVTKSEAKKV---PKDFIRRSSLKNTERFTTPELKELENELLEAKE 235

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1512063858  520 HALAAEEAHFEELVETIVTAREAIAATAAALARLDVGAGNAERASEADWCRPDIAEDAGLAITAGRHPVVEA 591
Cdd:smart00533 236 EIERLEKEILRELLEKVLEYLEELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSGELEIKNGRHPVLEL 307
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
 581-785 2.31e-52

ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213248 [Multi-domain]  Cd Length: 213  Bit Score: 181.73  E-value: 2.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 581 ITAGRHPVVEAALakagDRFVANDCQLA-DTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFS 659
Cdd:cd03281     2 IQGGRHPLLELFV----DSFVPNDTEIGgGGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 660 RVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEavHTQ---IRC-RCLFATHYHE 735
Cdd:cd03281    78 RMSSRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIE--HLLkrgPECpRVIVSTHFHE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1512063858 736 LARLAETCEALSLHH----VR----AREWQGDLVLLHELADGPADRSYGLAVARLAGV 785
Cdd:cd03281   156 LFNRSLLPERLKIKFltmeVLlnptSTSPNEDITYLYRLVPGLADTSFAIHCAKLAGI 213
MutS_I pfam01624
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 1-123 7.39e-47

MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam05188, pfam05192 and pfam05190. The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with globular domain I, which is involved in DNA binding, in Thermus aquaticus MutS as characterized in.


Pssm-ID: 426350 [Multi-domain]  Cd Length: 113  Bit Score: 162.37  E-value: 7.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858   1 MMAQYLALREEAGDALLFYRMGDFFELFFEDARTAAQILDIALTTRGEHGGAPIPMCGVPVHSAEGYLARLIKAGCRVAI 80
Cdd:pfam01624   3 MMRQYLELKSKYPDAVLFFRVGDFYELFGEDAEIAARELGITLTVRKGGSGKRIPMAGVPEHAFERYARRLVNKGYKVAI 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1512063858  81 AEQVETPDEAKARAKREgtpssktlvgraIVRLVTAGTLTEEA 123
Cdd:pfam01624  83 CEQTETPAEAKGVVKRE------------VVRVVTPGTLTDDE 113
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
 580-783 1.29e-46

ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213249 [Multi-domain]  Cd Length: 204  Bit Score: 165.25  E-value: 1.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 580 AITAGRHPVVEAALAKagdrFVANDCQLA-DTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLF 658
Cdd:cd03282     1 IIRDSRHPILDRDKKN----FIPNDIYLTrGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 659 SRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVhTQIRCRCLFATHYHELAR 738
Cdd:cd03282    77 SRLSNDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECL-IKKESTVFFATHFRDIAA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1512063858 739 LAETCEALSLHHVRAREWQ-GDLVLLHELADGPADR-SYGLAVARLA 783
Cdd:cd03282   156 ILGNKSCVVHLHMKAQSINsNGIEMAYKLVLGLYRIvDDGIRFVRVL 202
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
 580-784 1.11e-29

ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213250 [Multi-domain]  Cd Length: 199  Bit Score: 116.63  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 580 AITAGRHPVVEAALAkagdrfVANDCQLADTNrLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIgLVDRLFS 659
Cdd:cd03283     1 EAKNLGHPLIGREKR------VANDIDMEKKN-GILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFEL-PPVKIFT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 660 RVGAADNLARGRSTFMVEMVETAAIL--AQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQiRCRCLFATHYHELA 737
Cdd:cd03283    73 SIRVSDDLRDGISYFYAELRRLKEIVekAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNK-NTIGIISTHDLELA 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1512063858 738 RLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAG 784
Cdd:cd03283   152 DLLDLDSAVRNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIG 198
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
289-806 1.93e-28

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 122.56  E-value: 1.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 289 DRCVTGAGsRLLAEDLSaPLLDAAAIEARLALVQFWLTRPIERAQLRdaLRGIPDLGRALGRvvAGRG---SPRDLGQLR 365
Cdd:COG1193    20 EYAVSELG-KELARKLR-PSTDLEEVERLLAETAEARRLLRLEGGLP--LGGIPDIRPLLKR--AEEGgvlSPEELLDIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 366 DGLSEAMRLHHWLSGAPDRPSLLDQVLAKLTGHGALTDWLGRALVPNpptergsgGYIADGydaALDELRatsgDARRAI 445
Cdd:COG1193    94 RTLRAARRLKRFLEELEEEYPALKELAERLPPLPELEKEIDRAIDED--------GEVKDS---ASPELR----RIRREI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 446 AAMEARYRDetgiaTLK--IRHNGVLGYFIE--VSARHaDRLMAP-----------------DSGfthrQTM----KDAV 500
Cdd:COG1193   159 RSLEQRIRE-----KLEsiLRSASYQKYLQDaiITIRN-GRYVIPvkaeykgkipgivhdqsASG----QTLfiepMAVV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 501 RFN----SLKL--HEEAARIAEAGGHALAAEEAHFEELVETIVTAreaiaataaalarlDVGAGNAERASEADWCRPDIA 574
Cdd:COG1193   229 ELNnelrELEAeeRREIERILRELSALVREYAEELLENLEILAEL--------------DFIFAKARYALELKAVKPELN 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 575 EDAGLAITAGRHPVVEAalakagDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASA-ARIGL 653
Cdd:COG1193   295 DEGYIKLKKARHPLLDL------KKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEgSELPV 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 654 VDRLFSRVGaaD------NLargrSTF---MVEMVEtaaILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHtQIR 724
Cdd:COG1193   369 FDNIFADIG--DeqsieqSL----STFsshMTNIVE---ILEKADENSLVLLDELGAGTDPQEGAALAIAILEELL-ERG 438

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 725 CRCLFATHYHELARLAETCEALSLHHVRArewqgDLVLLH---ELADGPADRSYGLAVARLAGVPAPVVARAKA------ 795
Cdd:COG1193   439 ARVVATTHYSELKAYAYNTEGVENASVEF-----DVETLSptyRLLIGVPGRSNAFEIARRLGLPEEIIERAREllgees 513

                         570
                  ....*....|....*.
gi 1512063858 796 -----VLEKLEATREA 806
Cdd:COG1193   514 idvekLIEELERERRE 529
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
 581-746 7.47e-28

ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213247 [Multi-domain]  Cd Length: 200  Bit Score: 111.57  E-value: 7.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 581 ITAGRHPVveaaLAKAGDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPAS-AARIGLVDRLFS 659
Cdd:cd03280     2 LREARHPL----LPLQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAeGSSLPVFENIFA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 660 RVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQiRCRCLFATHYHELARL 739
Cdd:cd03280    78 DIGDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLER-GALVIATTHYGELKAY 156


                  ....*..
gi 1512063858 740 AETCEAL 746
Cdd:cd03280   157 AYKREGV 163
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 580-754 4.70e-26

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: 105.13  E-value: 4.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 580 AITAGRHPVVeaalakagdrFVANDCQLADTnRLWLIGGPNMGGKSTFLRQNALIVLLA----------QAGCFVPASAA 649
Cdd:cd03227     1 KIVLGRFPSY----------FVPNDVTFGEG-SLTIITGPNGSGKSTILDAIGLALGGAqsatrrrsgvKAGCIVAAVSA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 650 RIglvdrLFSRVGAadnlargrSTFMVEMVETAAILAQATH--RSFVILDEVGRGTSTYDGLALAWAVAEavHTQIRCRC 727
Cdd:cd03227    70 EL-----IFTRLQL--------SGGEKELSALALILALASLkpRPLYILDEIDRGLDPRDGQALAEAILE--HLVKGAQV 134

                         170       180
                  ....*....|....*....|....*..
gi 1512063858 728 LFATHYHELARLAETcealsLHHVRAR 754
Cdd:cd03227   135 IVITHLPELAELADK-----LIHIKKV 156
mutS2 TIGR01069
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ...
 571-804 1.03e-23

MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch repair protein. It is likely a DNA mismatch binding protein of unknown cellular function. [DNA metabolism, Other]


Pssm-ID: 130141 [Multi-domain]  Cd Length: 771  Bit Score: 107.60  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 571 PDIAEDAGLAITAGRHPVVEAalakagDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASA-A 649
Cdd:TIGR01069 288 PMPSFTGKIILENARHPLLKE------PKVVPFTLNLKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEhS 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 650 RIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQiRCRCLF 729
Cdd:TIGR01069 362 EIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENSLVLFDELGAGTDPDEGSALAISILEYLLKQ-NAQVLI 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 730 ATHYHELARLAETCEALSLHHVRAREWQgdLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKA-----------VLE 798
Cdd:TIGR01069 441 TTHYKELKALMYNNEGVENASVLFDEET--LSPTYKLLKGIPGESYAFEIAQRYGIPHFIIEQAKTfygefkeeinvLIE 518


                  ....*.
gi 1512063858 799 KLEATR 804
Cdd:TIGR01069 519 KLSALE 524
MutS_IV pfam05190
MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch ...
 426-517 5.78e-23

MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam00488. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds in part with globular domain IV, which is involved in DNA binding, in Thermus aquaticus MutS as characterized in.


Pssm-ID: 398730 [Multi-domain]  Cd Length: 92  Bit Score: 93.83  E-value: 5.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 426 GYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGVLGYFIEVSARHADRLmaPDSgFTHRQTMKDAVRFNSL 505
Cdd:pfam05190   1 GFDEELDELRDLLDELEKELEELEKKEREKLGIKSLKVGYNKVFGYYIEVTRSEAKKV--PSN-YIRRQTLKNGVRFTTP 77

                          90
                  ....*....|..
gi 1512063858 506 KLHEEAARIAEA 517
Cdd:pfam05190  78 ELKKLEDELLEA 89
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 570-801 5.75e-18

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 89.12  E-value: 5.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 570 RPDIAEDAGLAITAGRHPvveaALAKagDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASA- 648
Cdd:PRK00409  292 FPLFNDEGKIDLRQARHP----LLDG--EKVVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEp 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 649 ARIGLVDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHtQIRCRCL 728
Cdd:PRK00409  366 SEIPVFKEIFADIGDEQSIEQSLSTFSGHMTNIVRILEKADKNSLVLFDELGAGTDPDEGAALAISILEYLR-KRGAKII 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 729 FATHYHELArlaetceALSLHHVR----AREWqgDLVLL---HELADGPADRSYGLAVARLAGVPAPVVARAKAVL---- 797
Cdd:PRK00409  445 ATTHYKELK-------ALMYNREGvenaSVEF--DEETLrptYRLLIGIPGKSNAFEIAKRLGLPENIIEEAKKLIgedk 515


                  ....
gi 1512063858 798 EKLE 801
Cdd:PRK00409  516 EKLN 519
MutS_II pfam05188
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 131-248 5.52e-15

MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam01624, pfam05192 and pfam05190. The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. This domain corresponds to domain II in Thermus aquaticus MutS as characterized in, and has similarity resembles RNAse-H-like domains (see pfam00075).


Pssm-ID: 398728 [Multi-domain]  Cd Length: 133  Bit Score: 72.38  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 131 NVLAALAELRG-AVGIAAVDVSTGAMVLEECA-ADQLGAALARLSPSEVVVPEDWQH---GPDEAIHRPRST-------- 197
Cdd:pfam05188   1 NYLAAISRGDGnRYGLAFLDLSTGEFGVSEFEdFEELLAELSRLSPKELLLPESLSSstvAESQKLLELRLRvgrrptwl 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1512063858 198 FASDAGAERLKAVHGVATLDAFG-DFSRAMLGAAGGLIAYLDHVGRGRLPLL 248
Cdd:pfam05188  81 FELEHAYEDLNEDFGVEDLDGFGlEELPLALCAAGALISYLKETQKENLPHI 132
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 611-740 3.25e-09

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: 56.48  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858 611 NRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGLVDRLFSRVGAADNLARGrstfMVEMVETAAILAQAth 690
Cdd:cd00267    25 GEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQLSGG----QRQRVALARALLLN-- 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1512063858 691 RSFVILDEVGRGTSTYDGLALAWAVAEavHTQIRCRCLFATHYHELARLA 740
Cdd:cd00267    99 PDLLLLDEPTSGLDPASRERLLELLRE--LAEEGRTVIIVTHDPELAELA 146
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 192-792 4.01e-05

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 47.56  E-value: 4.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  192 HRPRSTFASDAGAERLKAVHgVATLDAFGDFSRAMLGAAGGLIAY---LD----HVGRGRLPLLLP--PVARAGEAGMAM 262
Cdd:COG3321    800 GPVLTGLVRQCLAAAGDAVV-LPSLRRGEDELAQLLTALAQLWVAgvpVDwsalYPGRGRRRVPLPtyPFQREDAAAALL 878

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  263 DAATRASLEILESTTGGRSGSLIGAVDRcvtgAGSRLLAEDLSAPLLDAAAIEARLALVQFWLTRPIERAQLRDALRGIP 342
Cdd:COG3321    879 AAALAAALAAAAALGALLLAALAAALAA----ALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAA 954

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  343 DLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLSGAPDRPSLLDQVLAKLTGHGALTDWLGRALVPNPPTERGSGGY 422
Cdd:COG3321    955 ALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAA 1034

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  423 IADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGVLGYFIEVSARHADrlmapdsgfthrqtmkDAVRF 502
Cdd:COG3321   1035 LAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA----------------ALALA 1098

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  503 NSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAAALARLDVGAGNAERASEADWCRPDIAEDAGLAIT 582
Cdd:COG3321   1099 LAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALA 1178

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  583 AGRHPVVEAALAKAGDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGcfVPASAARIGLVDRLFSRVG 662
Cdd:COG3321   1179 LALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLA--LAAAAAAVAALAAAAAALL 1256

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  663 AADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHYHELARLAET 742
Cdd:COG3321   1257 AALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAA 1336

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|
gi 1512063858  743 CEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVAR 792
Cdd:COG3321   1337 VAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 153-847 2.73e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 41.40  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  153 GAMVLEECAADQLGAALARL---------SPSEVVVPedwqhGPDEAIhrprstfasDAGAERLKA----VHGVATLDAF 219
Cdd:COG3321    657 GAMLAVGLSEEEVEALLAGYdgvsiaavnGPRSTVVS-----GPAEAV---------EALAARLEArgirARRLPVSHAF 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  220 gdFSRAMLGAAGGLIAYLDHV--GRGRLPL----------------------LLPPVARAGEAGMAMDAATRASLEIles 275
Cdd:COG3321    723 --HSPLMEPALEEFRAALAGVtpRAPRIPLisnvtgtwltgealdadywvrhLRQPVRFADAVEALLADGVRVFLEV--- 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  276 ttgGRSGSLIGAVDRCVTGAGSRLLAEDLSAPLLDAAAIeaRLALVQFWL----------------------TRPIERAQ 333
Cdd:COG3321    798 ---GPGPVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQL--LTALAQLWVagvpvdwsalypgrgrrrvplpTYPFQRED 872

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  334 LRDALRGIPDLGRALGRVVAGRGSPRDLGQLRDGLSEAMRLHHWLSGAPDRPSLLDQVLAKLTGHGALTDWLGRALVPNP 413
Cdd:COG3321    873 AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAA 952

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  414 PTERGSGGYIADGYDAALDELRATSGDARRAIAAMEARYRDETGIATLKIRHNGVLGYFIEVSARHADRLMAPDSGFTHR 493
Cdd:COG3321    953 AAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAA 1032

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  494 QTMKDAVRFNSLKLHEEAARIAEAGGHALAAEEAHFEELVETIVTAREAIAATAAALARLDVGAGNAERASEADWCRPDI 573
Cdd:COG3321   1033 AALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALL 1112

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  574 AEDAGLAITAGRHPVVEAALAKAGDRFVANDCQLADTNRLWLIGGPNMGGKSTFLRQNALIVLLAQAGCFVPASAARIGL 653
Cdd:COG3321   1113 AALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGL 1192

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  654 VDRLFSRVGAADNLARGRSTFMVEMVETAAILAQATHRSFVILDEVGRGTSTYDGLALAWAVAEAVHTQIRCRCLFATHY 733
Cdd:COG3321   1193 AALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLA 1272

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512063858  734 HELARLAETCEALSLHHVRAREWQGDLVLLHELADGPADRSYGLAVARLAGVPAPVVARAKAVLEKLEATREATGGIAAG 813
Cdd:COG3321   1273 ALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAA 1352

                          730       740       750
                   ....*....|....*....|....*....|....
gi 1512063858  814 LGDLPLFAMLAAQPPQASPEQQLADALRTADLDA 847
Cdd:COG3321   1353 AAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH