NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|498484674|ref|WP_010786454|]
View 

DNA mismatch repair protein MutS [Glaesserella parasuis]

Protein Classification

DNA mismatch repair protein MutS( domain architecture ID 11480839)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
9-865 0e+00

DNA mismatch repair protein MutS; Provisional


:

Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 1424.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   9 QHTPMMAQYLQLKAQNPDILLFYRMGDFYELFYDDAKKAAALLDISLTKRGQSAGEPIPMAGVPYHAVEGYLAKLVALGE 88
Cdd:PRK05399   7 KLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVPYHAAEGYLAKLVKKGY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  89 SVAICEQIGDPATSKGPVERKVVRIITPGTVSDEALLPERQDNLVAAIYQEKGVFALATLDMASGRFLISELpNKEALSA 168
Cdd:PRK05399  87 KVAICEQVEDPATAKGPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGGYGLAYLDLSTGEFRVTEL-DEEELLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 169 ELQRTEPAEILYPEDFSDVGILQGYKGLRRRPVWEFELVTAIQLLNRQFGTQNLTGFGVEkAVVALCAAGCVLHYAQETQ 248
Cdd:PRK05399 166 ELARLNPAEILVPEDFSEDELLLLRRGLRRRPPWEFDLDTAEKRLLEQFGVASLDGFGVD-LPLAIRAAGALLQYLKETQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 249 RTALPHINSIHLAQNSDTVLLDSATRRNLELTTNLAGGTENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHTRQQTI 328
Cdd:PRK05399 245 KRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLDAV 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 329 LALQKNERI-EPLQPLLQQVGDMERILARVALRTARPRDLTRLRTALEHIPDIVKH-SQHQTACLDNTLQQIADFSELFE 406
Cdd:PRK05399 325 EELLEDPLLrEDLRELLKGVYDLERLLSRIALGRANPRDLAALRDSLEALPELKELlAELDSPLLAELAEQLDPLEELAD 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 407 LLNQAIIDNPPQLIRDGGVIAEGYNAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQGQAHKA 486
Cdd:PRK05399 405 LLERAIVEEPPLLIRDGGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIEVTKANLDKV 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 487 PIHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDELFELLMPRLGELQLASFVLAELDVLTNLAERAESL 566
Cdd:PRK05399 485 PEDYIRRQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDVLASLAEVAEEN 564
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 567 NYVMPSFSHQRGVNIKGGRHPVVEQVL-KTPFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADS 645
Cdd:PRK05399 565 NYVRPEFTDDPGIDIEEGRHPVVEQVLgGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAES 644
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 646 AEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTL 725
Cdd:PRK05399 645 ARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIGAKTL 724
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 726 FATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQLERLSQQTA 805
Cdd:PRK05399 725 FATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREILAQLESASEKAK 804
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 806 QLDANQQQDLLFSANlqnaepispliEPSKVEQALAEIDPDELTPKQALEMLYRLKLLIK 865
Cdd:PRK05399 805 AASAEEDQLSLFAEP-----------EESPLLEALKALDPDNLTPREALNLLYELKKLLK 853
 
Name Accession Description Interval E-value
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
9-865 0e+00

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 1424.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   9 QHTPMMAQYLQLKAQNPDILLFYRMGDFYELFYDDAKKAAALLDISLTKRGQSAGEPIPMAGVPYHAVEGYLAKLVALGE 88
Cdd:PRK05399   7 KLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVPYHAAEGYLAKLVKKGY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  89 SVAICEQIGDPATSKGPVERKVVRIITPGTVSDEALLPERQDNLVAAIYQEKGVFALATLDMASGRFLISELpNKEALSA 168
Cdd:PRK05399  87 KVAICEQVEDPATAKGPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGGYGLAYLDLSTGEFRVTEL-DEEELLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 169 ELQRTEPAEILYPEDFSDVGILQGYKGLRRRPVWEFELVTAIQLLNRQFGTQNLTGFGVEkAVVALCAAGCVLHYAQETQ 248
Cdd:PRK05399 166 ELARLNPAEILVPEDFSEDELLLLRRGLRRRPPWEFDLDTAEKRLLEQFGVASLDGFGVD-LPLAIRAAGALLQYLKETQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 249 RTALPHINSIHLAQNSDTVLLDSATRRNLELTTNLAGGTENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHTRQQTI 328
Cdd:PRK05399 245 KRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLDAV 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 329 LALQKNERI-EPLQPLLQQVGDMERILARVALRTARPRDLTRLRTALEHIPDIVKH-SQHQTACLDNTLQQIADFSELFE 406
Cdd:PRK05399 325 EELLEDPLLrEDLRELLKGVYDLERLLSRIALGRANPRDLAALRDSLEALPELKELlAELDSPLLAELAEQLDPLEELAD 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 407 LLNQAIIDNPPQLIRDGGVIAEGYNAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQGQAHKA 486
Cdd:PRK05399 405 LLERAIVEEPPLLIRDGGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIEVTKANLDKV 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 487 PIHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDELFELLMPRLGELQLASFVLAELDVLTNLAERAESL 566
Cdd:PRK05399 485 PEDYIRRQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDVLASLAEVAEEN 564
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 567 NYVMPSFSHQRGVNIKGGRHPVVEQVL-KTPFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADS 645
Cdd:PRK05399 565 NYVRPEFTDDPGIDIEEGRHPVVEQVLgGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAES 644
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 646 AEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTL 725
Cdd:PRK05399 645 ARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIGAKTL 724
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 726 FATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQLERLSQQTA 805
Cdd:PRK05399 725 FATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREILAQLESASEKAK 804
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 806 QLDANQQQDLLFSANlqnaepispliEPSKVEQALAEIDPDELTPKQALEMLYRLKLLIK 865
Cdd:PRK05399 805 AASAEEDQLSLFAEP-----------EESPLLEALKALDPDNLTPREALNLLYELKKLLK 853
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
9-865 0e+00

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 1403.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   9 QHTPMMAQYLQLKAQNPDILLFYRMGDFYELFYDDAKKAAALLDISLTKRGQSAGEPIPMAGVPYHAVEGYLAKLVALGE 88
Cdd:COG0249    6 KLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGEPIPMAGVPYHAAEGYLAKLVKAGY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  89 SVAICEQIGDPATSKGPVERKVVRIITPGTVSDEALLPERQDNLVAAIYQEKGVFALATLDMASGRFLISELPNKEALSA 168
Cdd:COG0249   86 KVAICEQVEDPAEAKGLVKREVVRVVTPGTLTEDALLDAKRNNYLAAVARDKGRYGLAWLDISTGEFLVTELDGEEALLD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 169 ELQRTEPAEILYPEDFSDVGILQGY-----KGLRRRPVWEFELVTAIQLLNRQFGTQNLTGFGVEKAVVALCAAGCVLHY 243
Cdd:COG0249  166 ELARLAPAEILVPEDLPDPEELLELlrergAAVTRLPDWAFDPDAARRRLLEQFGVASLDGFGLEDLPAAIAAAGALLAY 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 244 AQETQRTALPHINSIHLAQNSDTVLLDSATRRNLELTTNLAGGTENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHT 323
Cdd:COG0249  246 LEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGGRKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 324 RQQTILALQKNERI-EPLQPLLQQVGDMERILARVALRTARPRDLTRLRTALEHIPDIVKH-SQHQTACLDNTLQQIADF 401
Cdd:COG0249  326 RLDAVEELLEDPLLrEELRELLKGVYDLERLLSRIALGRANPRDLAALRDSLAALPELKELlAELDSPLLAELAEALDPL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 402 SELFELLNQAIIDNPPQLIRDGGVIAEGYNAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQG 481
Cdd:COG0249  406 EDLAELLERAIVDEPPLLIRDGGVIREGYDAELDELRELSENGKEWLAELEARERERTGIKSLKVGYNKVFGYYIEVTKA 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 482 QAHKAPIHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDELFELLMPRLGELQLASFVLAELDVLTNLAE 561
Cdd:COG0249  486 NADKVPDDYIRKQTLKNAERYITPELKELEDKILSAEERALALEYELFEELREEVAAHIERLQALARALAELDVLASLAE 565
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 562 RAESLNYVMPSFSHQRGVNIKGGRHPVVEQVLK-TPFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSF 640
Cdd:COG0249  566 VAVENNYVRPELDDSPGIEIEGGRHPVVEQALPgEPFVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSF 645
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 641 VPADSAEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKT 720
Cdd:COG0249  646 VPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKI 725
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 721 QSLTLFATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQLERL 800
Cdd:COG0249  726 RARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSYGIHVAKLAGLPASVIERAREILAELEKG 805
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498484674 801 SQQTAQLDANQQQDLLFSANlqnaepisplIEPSKVEQALAEIDPDELTPKQALEMLYRLKLLIK 865
Cdd:COG0249  806 EAAAAGKAAPDQLSLFAAAD----------PEPSPVLEELKALDPDELTPREALNLLYELKKLLK 860
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
10-861 0e+00

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


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 1253.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   10 HTPMMAQYLQLKAQNPDILLFYRMGDFYELFYDDAKKAAALLDISLTKRGQSAGEPIPMAGVPYHAVEGYLAKLVALGES 89
Cdd:TIGR01070   1 LTPMMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADEPIPMAGIPYHAVEAYLEKLVKQGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   90 VAICEQIGDPATSKGPVERKVVRIITPGTVSDEALLPERQDNLVAAIYQEKGVFALATLDMASGRFLISELPNKEALSAE 169
Cdd:TIGR01070  81 VAICEQIEDPKTAKGPVEREVVQLITPGTVSDEALLPERQDNLLAAIAQESNGFGLATLDLTTGEFKVTELADKETLYAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  170 LQRTEPAEILYPEDFSDVGILQGYkglrrrpvwEFELVTAIQLLNRQFGTQNLTGFGVEKAVVALCAAGCVLHYAQETQR 249
Cdd:TIGR01070 161 LQRLNPAEVLLAEDLSEMEAIELR---------EFRKDTAVMSLEAQFGTEDLGGLGLRNAPLGLTAAGCLLQYAKRTQR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  250 TALPHINSIHLAQNSDTVLLDSATRRNLELTTNLAGGTENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHTRQQTIL 329
Cdd:TIGR01070 232 TALPHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQNTLFSVLDETKTAMGSRLLKRWLHRPLRDREVLEARQDTVE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  330 ALQKN-ERIEPLQPLLQQVGDMERILARVALRTARPRDLTRLRTALEHIPDIVKH-SQHQTACLDNTLQQIADFSELFEL 407
Cdd:TIGR01070 312 VLLRHfFLREGLRPLLKEVGDLERLAARVALGNARPRDLARLRTSLEQLPELRALlEELEGPTLQALAAQIDDFSELLEL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  408 LNQAIIDNPPQLIRDGGVIAEGYNAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQGQAHKAP 487
Cdd:TIGR01070 392 LEAALIENPPLVVRDGGLIREGYDEELDELRAASREGTDYLARLEARERERTGIPTLKVGYNAVFGYYIEVTRGQLHLVP 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  488 IHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDELFELLMPRLGELQLASFVLAELDVLTNLAERAESLN 567
Cdd:TIGR01070 472 AHYRRRQTLKNAERYITPELKEKEDKVLEAEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAEVAETLH 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  568 YVMPSFSHQRGVNIKGGRHPVVEQVLKTPFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAE 647
Cdd:TIGR01070 552 YTRPRFGDDPQLRIREGRHPVVEQVLRTPFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAE 631
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  648 IGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFA 727
Cdd:TIGR01070 632 LPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRAKTLFA 711
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  728 THYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQLERLS------ 801
Cdd:TIGR01070 712 THYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEARSteseap 791
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  802 QQTAQLDANQQQDLLFSAnlqnaepispliEPSKVEQALAEIDPDELTPKQALEMLYRLK 861
Cdd:TIGR01070 792 QRKAQTSAPEQISLFDEA------------ETHPLLEELAKLDPDDLTPLQALNLLYELK 839
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
581-794 2.54e-128

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: 383.54  E-value: 2.54e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 581 IKGGRHPVVEQVLKT-PFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIG 659
Cdd:cd03284    2 IEGGRHPVVEQVLDNePFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTRIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 660 ASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLPNQ 739
Cdd:cd03284   82 ASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTELEGK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 498484674 740 LKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKL 794
Cdd:cd03284  162 LPRVKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERAREIL 216
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
611-798 3.01e-120

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: 361.51  E-value: 3.01e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  611 LIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSL 690
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  691 VLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASK 770
Cdd:pfam00488  81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAADK 160
                         170       180
                  ....*....|....*....|....*...
gi 498484674  771 SYGLAVAALAGVPKQVIQLAKQKLTQLE 798
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERAREILAELE 188
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
610-794 6.51e-104

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 319.12  E-value: 6.51e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   610 LLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENS 689
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   690 LVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAAS 769
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVAG 160
                          170       180
                   ....*....|....*....|....*
gi 498484674   770 KSYGLAVAALAGVPKQVIQLAKQKL 794
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
 
Name Accession Description Interval E-value
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
9-865 0e+00

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 1424.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   9 QHTPMMAQYLQLKAQNPDILLFYRMGDFYELFYDDAKKAAALLDISLTKRGQSAGEPIPMAGVPYHAVEGYLAKLVALGE 88
Cdd:PRK05399   7 KLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVPYHAAEGYLAKLVKKGY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  89 SVAICEQIGDPATSKGPVERKVVRIITPGTVSDEALLPERQDNLVAAIYQEKGVFALATLDMASGRFLISELpNKEALSA 168
Cdd:PRK05399  87 KVAICEQVEDPATAKGPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGGYGLAYLDLSTGEFRVTEL-DEEELLA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 169 ELQRTEPAEILYPEDFSDVGILQGYKGLRRRPVWEFELVTAIQLLNRQFGTQNLTGFGVEkAVVALCAAGCVLHYAQETQ 248
Cdd:PRK05399 166 ELARLNPAEILVPEDFSEDELLLLRRGLRRRPPWEFDLDTAEKRLLEQFGVASLDGFGVD-LPLAIRAAGALLQYLKETQ 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 249 RTALPHINSIHLAQNSDTVLLDSATRRNLELTTNLAGGTENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHTRQQTI 328
Cdd:PRK05399 245 KRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLDAV 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 329 LALQKNERI-EPLQPLLQQVGDMERILARVALRTARPRDLTRLRTALEHIPDIVKH-SQHQTACLDNTLQQIADFSELFE 406
Cdd:PRK05399 325 EELLEDPLLrEDLRELLKGVYDLERLLSRIALGRANPRDLAALRDSLEALPELKELlAELDSPLLAELAEQLDPLEELAD 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 407 LLNQAIIDNPPQLIRDGGVIAEGYNAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQGQAHKA 486
Cdd:PRK05399 405 LLERAIVEEPPLLIRDGGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIEVTKANLDKV 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 487 PIHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDELFELLMPRLGELQLASFVLAELDVLTNLAERAESL 566
Cdd:PRK05399 485 PEDYIRRQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDVLASLAEVAEEN 564
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 567 NYVMPSFSHQRGVNIKGGRHPVVEQVL-KTPFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADS 645
Cdd:PRK05399 565 NYVRPEFTDDPGIDIEEGRHPVVEQVLgGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAES 644
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 646 AEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTL 725
Cdd:PRK05399 645 ARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIGAKTL 724
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 726 FATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQLERLSQQTA 805
Cdd:PRK05399 725 FATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREILAQLESASEKAK 804
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 806 QLDANQQQDLLFSANlqnaepispliEPSKVEQALAEIDPDELTPKQALEMLYRLKLLIK 865
Cdd:PRK05399 805 AASAEEDQLSLFAEP-----------EESPLLEALKALDPDNLTPREALNLLYELKKLLK 853
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
9-865 0e+00

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 1403.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   9 QHTPMMAQYLQLKAQNPDILLFYRMGDFYELFYDDAKKAAALLDISLTKRGQSAGEPIPMAGVPYHAVEGYLAKLVALGE 88
Cdd:COG0249    6 KLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGEPIPMAGVPYHAAEGYLAKLVKAGY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  89 SVAICEQIGDPATSKGPVERKVVRIITPGTVSDEALLPERQDNLVAAIYQEKGVFALATLDMASGRFLISELPNKEALSA 168
Cdd:COG0249   86 KVAICEQVEDPAEAKGLVKREVVRVVTPGTLTEDALLDAKRNNYLAAVARDKGRYGLAWLDISTGEFLVTELDGEEALLD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 169 ELQRTEPAEILYPEDFSDVGILQGY-----KGLRRRPVWEFELVTAIQLLNRQFGTQNLTGFGVEKAVVALCAAGCVLHY 243
Cdd:COG0249  166 ELARLAPAEILVPEDLPDPEELLELlrergAAVTRLPDWAFDPDAARRRLLEQFGVASLDGFGLEDLPAAIAAAGALLAY 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 244 AQETQRTALPHINSIHLAQNSDTVLLDSATRRNLELTTNLAGGTENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHT 323
Cdd:COG0249  246 LEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGGRKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 324 RQQTILALQKNERI-EPLQPLLQQVGDMERILARVALRTARPRDLTRLRTALEHIPDIVKH-SQHQTACLDNTLQQIADF 401
Cdd:COG0249  326 RLDAVEELLEDPLLrEELRELLKGVYDLERLLSRIALGRANPRDLAALRDSLAALPELKELlAELDSPLLAELAEALDPL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 402 SELFELLNQAIIDNPPQLIRDGGVIAEGYNAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQG 481
Cdd:COG0249  406 EDLAELLERAIVDEPPLLIRDGGVIREGYDAELDELRELSENGKEWLAELEARERERTGIKSLKVGYNKVFGYYIEVTKA 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 482 QAHKAPIHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDELFELLMPRLGELQLASFVLAELDVLTNLAE 561
Cdd:COG0249  486 NADKVPDDYIRKQTLKNAERYITPELKELEDKILSAEERALALEYELFEELREEVAAHIERLQALARALAELDVLASLAE 565
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 562 RAESLNYVMPSFSHQRGVNIKGGRHPVVEQVLK-TPFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSF 640
Cdd:COG0249  566 VAVENNYVRPELDDSPGIEIEGGRHPVVEQALPgEPFVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSF 645
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 641 VPADSAEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKT 720
Cdd:COG0249  646 VPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKI 725
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 721 QSLTLFATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQLERL 800
Cdd:COG0249  726 RARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSYGIHVAKLAGLPASVIERAREILAELEKG 805
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498484674 801 SQQTAQLDANQQQDLLFSANlqnaepisplIEPSKVEQALAEIDPDELTPKQALEMLYRLKLLIK 865
Cdd:COG0249  806 EAAAAGKAAPDQLSLFAAAD----------PEPSPVLEELKALDPDELTPREALNLLYELKKLLK 860
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
10-861 0e+00

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


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 1253.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   10 HTPMMAQYLQLKAQNPDILLFYRMGDFYELFYDDAKKAAALLDISLTKRGQSAGEPIPMAGVPYHAVEGYLAKLVALGES 89
Cdd:TIGR01070   1 LTPMMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADEPIPMAGIPYHAVEAYLEKLVKQGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   90 VAICEQIGDPATSKGPVERKVVRIITPGTVSDEALLPERQDNLVAAIYQEKGVFALATLDMASGRFLISELPNKEALSAE 169
Cdd:TIGR01070  81 VAICEQIEDPKTAKGPVEREVVQLITPGTVSDEALLPERQDNLLAAIAQESNGFGLATLDLTTGEFKVTELADKETLYAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  170 LQRTEPAEILYPEDFSDVGILQGYkglrrrpvwEFELVTAIQLLNRQFGTQNLTGFGVEKAVVALCAAGCVLHYAQETQR 249
Cdd:TIGR01070 161 LQRLNPAEVLLAEDLSEMEAIELR---------EFRKDTAVMSLEAQFGTEDLGGLGLRNAPLGLTAAGCLLQYAKRTQR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  250 TALPHINSIHLAQNSDTVLLDSATRRNLELTTNLAGGTENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHTRQQTIL 329
Cdd:TIGR01070 232 TALPHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQNTLFSVLDETKTAMGSRLLKRWLHRPLRDREVLEARQDTVE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  330 ALQKN-ERIEPLQPLLQQVGDMERILARVALRTARPRDLTRLRTALEHIPDIVKH-SQHQTACLDNTLQQIADFSELFEL 407
Cdd:TIGR01070 312 VLLRHfFLREGLRPLLKEVGDLERLAARVALGNARPRDLARLRTSLEQLPELRALlEELEGPTLQALAAQIDDFSELLEL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  408 LNQAIIDNPPQLIRDGGVIAEGYNAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQGQAHKAP 487
Cdd:TIGR01070 392 LEAALIENPPLVVRDGGLIREGYDEELDELRAASREGTDYLARLEARERERTGIPTLKVGYNAVFGYYIEVTRGQLHLVP 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  488 IHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDELFELLMPRLGELQLASFVLAELDVLTNLAERAESLN 567
Cdd:TIGR01070 472 AHYRRRQTLKNAERYITPELKEKEDKVLEAEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAEVAETLH 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  568 YVMPSFSHQRGVNIKGGRHPVVEQVLKTPFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAE 647
Cdd:TIGR01070 552 YTRPRFGDDPQLRIREGRHPVVEQVLRTPFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAE 631
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  648 IGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFA 727
Cdd:TIGR01070 632 LPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRAKTLFA 711
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  728 THYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQLERLS------ 801
Cdd:TIGR01070 712 THYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEARSteseap 791
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  802 QQTAQLDANQQQDLLFSAnlqnaepispliEPSKVEQALAEIDPDELTPKQALEMLYRLK 861
Cdd:TIGR01070 792 QRKAQTSAPEQISLFDEA------------ETHPLLEELAKLDPDDLTPLQALNLLYELK 839
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
581-794 2.54e-128

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: 383.54  E-value: 2.54e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 581 IKGGRHPVVEQVLKT-PFIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIG 659
Cdd:cd03284    2 IEGGRHPVVEQVLDNePFVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTRIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 660 ASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLPNQ 739
Cdd:cd03284   82 ASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTELEGK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 498484674 740 LKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKL 794
Cdd:cd03284  162 LPRVKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERAREIL 216
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
611-798 3.01e-120

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: 361.51  E-value: 3.01e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  611 LIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSL 690
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  691 VLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAASK 770
Cdd:pfam00488  81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAADK 160
                         170       180
                  ....*....|....*....|....*...
gi 498484674  771 SYGLAVAALAGVPKQVIQLAKQKLTQLE 798
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERAREILAELE 188
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
610-794 6.51e-104

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 319.12  E-value: 6.51e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   610 LLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENS 689
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   690 LVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLPNQLKGVANIHLDALEHNDTIAFMHSVQEGAAS 769
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVAG 160
                          170       180
                   ....*....|....*....|....*
gi 498484674   770 KSYGLAVAALAGVPKQVIQLAKQKL 794
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
288-592 4.66e-95

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 300.37  E-value: 4.66e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   288 ENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHTRQQTILALQKN-ERIEPLQPLLQQVGDMERILARVALRTARPRD 366
Cdd:smart00533   1 KGSLFELLNHTKTPMGKRLLRRWLLQPLLDLKEINERLDAVEELVENpELRQKLRQLLKRIPDLERLLSRIERGRASPRD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   367 LTRLRTALEHIPDIVKHSQHQTACLDNTLQQ--IADFSELFELLNQAIIDNPPQLIRDGGVIAEGYNAELDEWRSLAEGA 444
Cdd:smart00533  81 LLRLYDSLEGLKEIRQLLESLDGPLLGLLLKviLEPLLELLELLLELLNDDDPLEVNDGGLIKDGFDPELDELREKLEEL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   445 TKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQGQAHKAPIHYVRRQTLKNAERYIIPELKTYEDKVLKAKGASLAL 524
Cdd:smart00533 161 EEELEELLKKEREELGIDSLKLGYNKVHGYYIEVTKSEAKKVPKDFIRRSSLKNTERFTTPELKELENELLEAKEEIERL 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498484674   525 EKQLYDELFELLMPRLGELQLASFVLAELDVLTNLAERAESLNYVMPSFSHQRGVNIKGGRHPVVEQV 592
Cdd:smart00533 241 EKEILRELLEKVLEYLEELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSGELEIKNGRHPVLELQ 308
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
581-798 2.52e-91

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: 287.35  E-value: 2.52e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 581 IKGGRHPVVEQVLKTPFIANPV-LLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIG 659
Cdd:cd03285    2 LKEARHPCVEAQDDVAFIPNDVtLTRGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILARVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 660 ASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLPNQ 739
Cdd:cd03285   82 ASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQIKCFCLFATHFHELTALADE 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498484674 740 LKGVANIHLDAL--EHNDTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQLE 798
Cdd:cd03285  162 VPNVKNLHVTALtdDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQKALELE 222
MutS_III pfam05192
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair ...
272-560 1.82e-88

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: 282.37  E-value: 1.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  272 ATRRNLELTTNLAGGTENTLTSVLDKCVTSMGSRLLKRWIHQPIRDLAKLHTRQQTILALQKNERI-EPLQPLLQQVGDM 350
Cdd:pfam05192   1 ATLRNLELTENLRGGKEGSLLGLLDRTKTPMGSRLLRQWLLQPLTDLEEINERLDAVEELLENSELrEDLRELLRRLPDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  351 ERILARVALRTARPRDLTRLRTALEHIPDIvkhsqhQTACLDNTLQQIADFSELFELLNQAIIDNPPQLIRDGGVIAEGY 430
Cdd:pfam05192  81 ERLLSRIALGKATPRDLLALLDSLEKLPLL------KELLLEEKSALLGELASLAELLEEAIDEEPPALLRDGGVIRDGY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  431 NAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGY-------YIQISQGQAHKAPIHYVRRQTLKNAERYI 503
Cdd:pfam05192 155 DEELDELRDLLLDGKRLLAKLEARERERTGIKSLKVLYNKVFGYylllveyYIEVSKSQKDKVPDDYIRIQTTKNAERYI 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 498484674  504 IPELKTYEDKVLKAKGASLALEKQLYDELFELLMPRLGELQLASFVLAELDVLTNLA 560
Cdd:pfam05192 235 TPELKELERKILQAEERLLALEKELFEELLEEVLEYIEVLRRAAEALAELDVLLSLA 291
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
580-782 4.51e-87

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: 275.28  E-value: 4.51e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 580 NIKGGRHPVVEQVLKTP-FIANPVLLNPQRhLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRI 658
Cdd:cd03243    1 EIKGGRHPVLLALTKGEtFVPNDINLGSGR-LLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 659 GASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKtQSLTLFATHYFELTSLPN 738
Cdd:cd03243   80 GAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEK-GCRTLFATHFHELADLPE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 498484674 739 QLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAGV 782
Cdd:cd03243  159 QVPGVKNLHMEELITTGGLTFTYKLIDGICDPSYALQIAELAGL 202
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
580-790 3.64e-74

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: 241.56  E-value: 3.64e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 580 NIKGGRHPVVEQVLKTPFIANPVLLNPQR-HLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRI 658
Cdd:cd03286    1 CFEELRHPCLNASTASSFVPNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFTRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 659 GASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLPN 738
Cdd:cd03286   81 GARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKCLTLFSTHYHSLCDEFH 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498484674 739 QLKGVANIHLDALEHND------TIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLA 790
Cdd:cd03286  161 EHGGVRLGHMACAVKNEsdptirDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
579-790 4.85e-70

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: 230.84  E-value: 4.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 579 VNIKGGRHPVVEQVLKTPFIANPVLLNPQR-HLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTR 657
Cdd:cd03287    1 ILIKEGRHPMIESLLDKSFVPNDIHLSAEGgYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVLTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 658 IGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQSLTLFATHYFELTSLP 737
Cdd:cd03287   81 MGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEKKCLVLFVTHYPSLGEIL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498484674 738 NQLKG-VANIHLDALEHN--------DTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLA 790
Cdd:cd03287  161 RRFEGsIRNYHMSYLESQkdfetsdsQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
581-782 6.88e-56

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: 191.75  E-value: 6.88e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 581 IKGGRHPVVEQVLKTpFIANPVLLNPQRH-LLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIG 659
Cdd:cd03281    2 IQGGRHPLLELFVDS-FVPNDTEIGGGGPsIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFTRMS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 660 ASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQS--LTLFATHYFEL--TS 735
Cdd:cd03281   81 SRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRGPEcpRVIVSTHFHELfnRS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 498484674 736 LPNQLKGVANIHLDAL------EHNDTIAFMHSVQEGAASKSYGLAVAALAGV 782
Cdd:cd03281  161 LLPERLKIKFLTMEVLlnptstSPNEDITYLYRLVPGLADTSFAIHCAKLAGI 213
MutS_I pfam01624
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ...
11-123 1.57e-55

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: 186.64  E-value: 1.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674   11 TPMMAQYLQLKAQNPDILLFYRMGDFYELFYDDAKKAAALLDISLTKRGQSAGEPIPMAGVPYHAVEGYLAKLVALGESV 90
Cdd:pfam01624   1 TPMMRQYLELKSKYPDAVLFFRVGDFYELFGEDAEIAARELGITLTVRKGGSGKRIPMAGVPEHAFERYARRLVNKGYKV 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 498484674   91 AICEQIGDPATSKGPVERKVVRIITPGTVSDEA 123
Cdd:pfam01624  81 AICEQTETPAEAKGVVKREVVRVVTPGTLTDDE 113
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
581-780 1.38e-49

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: 173.73  E-value: 1.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 581 IKGGRHPVVEQVLKTpFIANPVLLNPQRHLL-IVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIGPIDRIFTRIG 659
Cdd:cd03282    2 IRDSRHPILDRDKKN-FIPNDIYLTRGSSRFhIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLSRLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 660 ASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKtQSLTLFATHYFELTSLPNQ 739
Cdd:cd03282   81 NDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKK-ESTVFFATHFRDIAAILGN 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 498484674 740 LKGVANIHLDALEHNDT-IAFMHSVQEGA-ASKSYGLAVAALA 780
Cdd:cd03282  160 KSCVVHLHMKAQSINSNgIEMAYKLVLGLyRIVDDGIRFVRVL 202
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
581-781 3.86e-38

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: 140.90  E-value: 3.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 581 IKGGRHPVVEQVLKtpfIANPVLLNPqRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADSAEIgPIDRIFTRIGA 660
Cdd:cd03283    2 AKNLGHPLIGREKR---VANDIDMEK-KNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFEL-PPVKIFTSIRV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 661 SDDLASGRSTFMVEMTEMANILHQ--SSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKtQSLTLFATHYFELTSLPN 738
Cdd:cd03283   77 SDDLRDGISYFYAELRRLKEIVEKakKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNK-NTIGIISTHDLELADLLD 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 498484674 739 QLKGVANIHLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAG 781
Cdd:cd03283  156 LDSAVRNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIG 198
mutS2 TIGR01069
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ...
328-840 3.62e-37

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: 149.97  E-value: 3.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  328 ILALQKNERIEpLQPLLQQVGDMERILARVALRTA--RPRDLTRLRTALEHIPDI--VKHSQHQTACLDNTLQQIADFSE 403
Cdd:TIGR01069  47 IIKLTALGSIE-NNVRFFGFEDIRELLKRAELGGIvkGLEYILVIQNALKTVKHLkvLSEHVLDLEILFHLRLNLITLPP 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  404 LFELLNQaiidnppqLIRDGGVIAEGYNAELD----EWRSLAEGATKFLEDLEAR-ERAKTGIDTLkigFNAVHGYY-IQ 477
Cdd:TIGR01069 126 LENDIIA--------CIDDDGKVKDGASEELDaireSLKALEEEVVKRLHKIIRSkELAKYLSDTI---VTIRNGRYvLP 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  478 ISQGQAHKAP--IH---------YVRRQT---LKNAERYIIPELKTYEDKVLKAKGASLALEKQLYDELFEllmprlgel 543
Cdd:TIGR01069 195 LKSGFKGKIKgiVHdtsssgetfYIEPQAivkLNNKLAQLKNEEECEIEKILRTLSEKVQEYLLELKFLFK--------- 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  544 qlasfVLAELDVLTNLAERAESLNYVMPSFSHQRGVNIKGGRHPVveqvLKTP-FIANPVLLNPQRHLLIVTGPNMGGKS 622
Cdd:TIGR01069 266 -----EFDFLDSLQARARYAKAVKGEFPMPSFTGKIILENARHPL----LKEPkVVPFTLNLKFEKRVLAITGPNTGGKT 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  623 TYMRQIALITLMAYIGSFVPADSAEIGPI-DRIFTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTS 701
Cdd:TIGR01069 337 VTLKTLGLLALMFQSGIPIPANEHSEIPYfEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENSLVLFDELGAGTD 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  702 TYDGLSLAWACAEWLaKKTQSLTLFATHYFELTSLPNQLKGVANihLDALEHNDTIAFMHSVQEGAASKSYGLAVAALAG 781
Cdd:TIGR01069 417 PDEGSALAISILEYL-LKQNAQVLITTHYKELKALMYNNEGVEN--ASVLFDEETLSPTYKLLKGIPGESYAFEIAQRYG 493
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  782 VPKQVIQLAKQKLT-QLERLSQQTAQLDANQQQDLLFSANLQNAepispLIEPSKVEQAL 840
Cdd:TIGR01069 494 IPHFIIEQAKTFYGeFKEEINVLIEKLSALEKELEQKNEHLEKL-----LKEQEKLKKEL 548
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
296-813 3.68e-37

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 149.91  E-value: 3.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 296 DKCVTSMGSRLLKRWihQPIRDLAKLHTRQQ------TILALQKN---ERIEPLQPLLQQVG-----DMERILA-RVALR 360
Cdd:COG1193   20 EYAVSELGKELARKL--RPSTDLEEVERLLAetaearRLLRLEGGlplGGIPDIRPLLKRAEeggvlSPEELLDiARTLR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 361 TARprdltRLRTALEHIPDIVKHsqhqtacLDNTLQQIADFSELFELLNQAIIDNppqlirdgGVIAEGYNAEL----DE 436
Cdd:COG1193   98 AAR-----RLKRFLEELEEEYPA-------LKELAERLPPLPELEKEIDRAIDED--------GEVKDSASPELrrirRE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 437 WRSLAEGATKFLEDLEARERAKTgidtlkigfnavhgyYIQISqgqahkapihYVrrqTLKNaERYIIPeLKT-YEDKV- 514
Cdd:COG1193  158 IRSLEQRIREKLESILRSASYQK---------------YLQDA----------II---TIRN-GRYVIP-VKAeYKGKIp 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 515 -----LKAKGASLALE-----------KQLYD-----------ELFELLMPRLGELQLASFVLAELDVLTNLAERAESLN 567
Cdd:COG1193  208 givhdQSASGQTLFIEpmavvelnnelRELEAeerreierilrELSALVREYAEELLENLEILAELDFIFAKARYALELK 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 568 YVMPSFSHQRGVNIKGGRHP--VVEQVlktpfIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPA-D 644
Cdd:COG1193  288 AVKPELNDEGYIKLKKARHPllDLKKV-----VPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAaE 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 645 SAEIGPIDRIFTRIGasD------DLasgrSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAK 718
Cdd:COG1193  363 GSELPVFDNIFADIG--DeqsieqSL----STFSSHMTNIVEILEKADENSLVLLDELGAGTDPQEGAALAIAILEELLE 436
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 719 KtQSLTLFATHYFELTSLPNQLKGVANIhldALEHN-DTIAFMHSVQEGAASKSYGLAVAALAGVPKQVIQLAKQKLTQ- 796
Cdd:COG1193  437 R-GARVVATTHYSELKAYAYNTEGVENA---SVEFDvETLSPTYRLLIGVPGRSNAFEIARRLGLPEEIIERARELLGEe 512
                        570       580
                 ....*....|....*....|....
gi 498484674 797 -------LERLSQQTAQLDANQQQ 813
Cdd:COG1193  513 sidveklIEELERERRELEEEREE 536
MutS_IV pfam05190
MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch ...
429-518 8.53e-35

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: 127.34  E-value: 8.53e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  429 GYNAELDEWRSLAEGATKFLEDLEARERAKTGIDTLKIGFNAVHGYYIQISQGQAHKAPIHYVRRQTLKNAERYIIPELK 508
Cdd:pfam05190   1 GFDEELDELRDLLDELEKELEELEKKEREKLGIKSLKVGYNKVFGYYIEVTRSEAKKVPSNYIRRQTLKNGVRFTTPELK 80
                          90
                  ....*....|
gi 498484674  509 TYEDKVLKAK 518
Cdd:pfam05190  81 KLEDELLEAE 90
MutS_II pfam05188
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair ...
131-255 2.98e-33

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: 124.77  E-value: 2.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674  131 NLVAAIY-QEKGVFALATLDMASGRFLISELPNKEALSAELQRTEPAEILYPEDFSD------VGILQGYKGLRRRPVWE 203
Cdd:pfam05188   1 NYLAAISrGDGNRYGLAFLDLSTGEFGVSEFEDFEELLAELSRLSPKELLLPESLSSstvaesQKLLELRLRVGRRPTWL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 498484674  204 FELVTAIQLLNRQFGTQNLTGFGVEKAVVALCAAGCVLHYAQETQRTALPHI 255
Cdd:pfam05188  81 FELEHAYEDLNEDFGVEDLDGFGLEELPLALCAAGALISYLKETQKENLPHI 132
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
496-825 5.90e-31

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 130.33  E-value: 5.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 496 LKNAERYIIPELKTYEDKVLKAKGASLAleKQLyDELFELLmprlgelqlasFVLAELDVLTNLAERAESLNYVMPSFSH 575
Cdd:PRK00409 232 LNNEIRELRNKEEQEIERILKELSAKVA--KNL-DFLKFLN-----------KIFDELDFIFARARYAKALKATFPLFND 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 576 QRGVNIKGGRHPVVEQVLKTPfiaNPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPADS-AEIGPIDRI 654
Cdd:PRK00409 298 EGKIDLRQARHPLLDGEKVVP---KDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPANEpSEIPVFKEI 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 655 FTRIGASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQsLTLFATHYFELT 734
Cdd:PRK00409 375 FADIGDEQSIEQSLSTFSGHMTNIVRILEKADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGA-KIIATTHYKELK 453
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 735 SLPNQLKGVANIhldALEHND-----TIAFMHsvqeGAASKSYGLAVAALAGVPKQVIQLAKQKLT----QLERLSQQTA 805
Cdd:PRK00409 454 ALMYNREGVENA---SVEFDEetlrpTYRLLI----GIPGKSNAFEIAKRLGLPENIIEEAKKLIGedkeKLNELIASLE 526
                        330       340
                 ....*....|....*....|.
gi 498484674 806 QLDANQQQDLLFSANL-QNAE 825
Cdd:PRK00409 527 ELERELEQKAEEAEALlKEAE 547
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
580-745 9.03e-31

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: 120.05  E-value: 9.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 580 NIKGGRHPVVEQVLKTPfIANPVLLNPQRHLLIVTGPNMGGKSTYMRQIALITLMAYIGSFVPAD-SAEIGPIDRIFTRI 658
Cdd:cd03280    1 RLREARHPLLPLQGEKV-VPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAeGSSLPVFENIFADI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 659 GASDDLASGRSTFMVEMTEMANILHQSSENSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKtQSLTLFATHYFELTSLPN 738
Cdd:cd03280   80 GDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLER-GALVIATTHYGELKAYAY 158

                 ....*..
gi 498484674 739 QLKGVAN 745
Cdd:cd03280  159 KREGVEN 165
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
581-743 8.66e-30

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: 115.92  E-value: 8.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 581 IKGGRHPVVeqvlktpFIANPVLLNPQRhLLIVTGPNMGGKSTYMRQIALITLMAY----------IGSFVPADSAEIgp 650
Cdd:cd03227    2 IVLGRFPSY-------FVPNDVTFGEGS-LTIITGPNGSGKSTILDAIGLALGGAQsatrrrsgvkAGCIVAAVSAEL-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 651 idrIFTRIGASddlaSGrstfMVEMTEMANILHQSSEN--SLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQslTLFAT 728
Cdd:cd03227   72 ---IFTRLQLS----GG----EKELSALALILALASLKprPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ--VIVIT 138
                        170
                 ....*....|....*
gi 498484674 729 HYFELTSLPNQLKGV 743
Cdd:cd03227  139 HLPELAELADKLIHI 153
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
581-733 4.16e-10

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: 59.18  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 581 IKGGRHPVVEQVLktpFIANPVLLNPQRHLLIVtGPNMGGKSTYMRQIALITlmayigsFVPADSAEIGPID-------R 653
Cdd:cd00267    2 IENLSFRYGGRTA---LDNVSLTLKAGEIVALV-GPNGSGKSTLLRAIAGLL-------KPTSGEILIDGKDiaklpleE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498484674 654 IFTRIGASDDLASGrstfMVEMTEMANILHQSSenSLVLVDEIGRGTSTYDGLSLAWACAEWLAKKTQslTLFATHYFEL 733
Cdd:cd00267   71 LRRRIGYVPQLSGG----QRQRVALARALLLNP--DLLLLDEPTSGLDPASRERLLELLRELAEEGRT--VIIVTHDPEL 142
 
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