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Conserved domains on  [gi|2234294342|ref|WP_248594699|]
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DNA mismatch repair protein MutS [Candidatus Accumulibacter contiguus]

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

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List of domain hits

Name Accession Description Interval E-value
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
11-870 0e+00

DNA mismatch repair protein MutS; Provisional


:

Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 1335.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  11 DVTGHTPMMQQYLRIKAEHPGILLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGQPIKMAGVPYHAVEQYLAKLVR 90
Cdd:PRK05399    4 DMSKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVPYHAAEGYLAKLVK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  91 LGESVVICEQIGDPATSKGPVERAVARIVTPGTLTDAALLDEKRNTLLLSLCASKQFAGLAWINLASGDFRVCEVAPSKL 170
Cdd:PRK05399   84 KGYKVAICEQVEDPATAKGPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGGYGLAYLDLSTGEFRVTELDEEEL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 171 AATLDRIRPAEIIVPESLGLTFTPEV--ALTRQPDWHFDVEAARRELCTHFATRSLAGFGADaLRPAIAAAGALLRYAKA 248
Cdd:PRK05399  164 LAELARLNPAEILVPEDFSEDELLLLrrGLRRRPPWEFDLDTAEKRLLEQFGVASLDGFGVD-LPLAIRAAGALLQYLKE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 249 TQTRALPHLRALIVERDATFLGLDTATRRNLELTETLRGQPAPTLCSLLDNCVTAMGARLLRHALHHPWRDPTIPAARHA 328
Cdd:PRK05399  243 TQKRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 329 AIAMLLDDDGrTLHALRQALRGFADIERIAGRIALCSARPRDLSSLRDSLQRLHELRAPLAAMLSIAAAAAPLlaelhaQ 408
Cdd:PRK05399  323 AVEELLEDPL-LREDLRELLKGVYDLERLLSRIALGRANPRDLAALRDSLEALPELKELLAELDSPLLAELAE------Q 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 409 LATPDAALDLLCRAILPEPAALIRDGGVIAKGFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRVHGFYIE 488
Cdd:PRK05399  396 LDPLEELADLLERAIVEEPPLLIRDGGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIE 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 489 VSHANATRVPDDYRRRQTLKNAERYLTPELKAFEDKALSAQERGLAREKLLYEGLLATLQDDLPQLQQIAQAVAGIDLLS 568
Cdd:PRK05399  476 VTKANLDKVPEDYIRRQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDVLA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 569 GFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVEeQIGGGESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLA 648
Cdd:PRK05399  556 SLAEVAEENNYVRPEFTDDPGIDIEEGRHPVVE-QVLGGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLA 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 649 HVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRH 728
Cdd:PRK05399  635 QIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEY 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 729 LLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAARRQLR 808
Cdd:PRK05399  715 LHDKIGAKTLFATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREILA 794
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234294342 809 EFEQR------ASINPLQPDLFatalanaaeaQEHPTPPAIERLRSIDPDRLTPREALDALYELKSLL 870
Cdd:PRK05399  795 QLESAsekakaASAEEDQLSLF----------AEPEESPLLEALKALDPDNLTPREALNLLYELKKLL 852
 
Name Accession Description Interval E-value
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
11-870 0e+00

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 1335.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  11 DVTGHTPMMQQYLRIKAEHPGILLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGQPIKMAGVPYHAVEQYLAKLVR 90
Cdd:PRK05399    4 DMSKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVPYHAAEGYLAKLVK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  91 LGESVVICEQIGDPATSKGPVERAVARIVTPGTLTDAALLDEKRNTLLLSLCASKQFAGLAWINLASGDFRVCEVAPSKL 170
Cdd:PRK05399   84 KGYKVAICEQVEDPATAKGPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGGYGLAYLDLSTGEFRVTELDEEEL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 171 AATLDRIRPAEIIVPESLGLTFTPEV--ALTRQPDWHFDVEAARRELCTHFATRSLAGFGADaLRPAIAAAGALLRYAKA 248
Cdd:PRK05399  164 LAELARLNPAEILVPEDFSEDELLLLrrGLRRRPPWEFDLDTAEKRLLEQFGVASLDGFGVD-LPLAIRAAGALLQYLKE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 249 TQTRALPHLRALIVERDATFLGLDTATRRNLELTETLRGQPAPTLCSLLDNCVTAMGARLLRHALHHPWRDPTIPAARHA 328
Cdd:PRK05399  243 TQKRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 329 AIAMLLDDDGrTLHALRQALRGFADIERIAGRIALCSARPRDLSSLRDSLQRLHELRAPLAAMLSIAAAAAPLlaelhaQ 408
Cdd:PRK05399  323 AVEELLEDPL-LREDLRELLKGVYDLERLLSRIALGRANPRDLAALRDSLEALPELKELLAELDSPLLAELAE------Q 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 409 LATPDAALDLLCRAILPEPAALIRDGGVIAKGFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRVHGFYIE 488
Cdd:PRK05399  396 LDPLEELADLLERAIVEEPPLLIRDGGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIE 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 489 VSHANATRVPDDYRRRQTLKNAERYLTPELKAFEDKALSAQERGLAREKLLYEGLLATLQDDLPQLQQIAQAVAGIDLLS 568
Cdd:PRK05399  476 VTKANLDKVPEDYIRRQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDVLA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 569 GFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVEeQIGGGESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLA 648
Cdd:PRK05399  556 SLAEVAEENNYVRPEFTDDPGIDIEEGRHPVVE-QVLGGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLA 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 649 HVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRH 728
Cdd:PRK05399  635 QIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEY 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 729 LLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAARRQLR 808
Cdd:PRK05399  715 LHDKIGAKTLFATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREILA 794
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234294342 809 EFEQR------ASINPLQPDLFatalanaaeaQEHPTPPAIERLRSIDPDRLTPREALDALYELKSLL 870
Cdd:PRK05399  795 QLESAsekakaASAEEDQLSLF----------AEPEESPLLEALKALDPDNLTPREALNLLYELKKLL 852
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
11-870 0e+00

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 1328.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  11 DVTGHTPMMQQYLRIKAEHPGILLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGQPIKMAGVPYHAVEQYLAKLVR 90
Cdd:COG0249     3 DMAKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGEPIPMAGVPYHAAEGYLAKLVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  91 LGESVVICEQIGDPATSKGPVERAVARIVTPGTLTDAALLDEKRNTLLLSLCASKQFAGLAWINLASGDFRVCEVA-PSK 169
Cdd:COG0249    83 AGYKVAICEQVEDPAEAKGLVKREVVRVVTPGTLTEDALLDAKRNNYLAAVARDKGRYGLAWLDISTGEFLVTELDgEEA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 170 LAATLDRIRPAEIIVPESLGLTF-------TPEVALTRQPDWHFDVEAARRELCTHFATRSLAGFGADALRPAIAAAGAL 242
Cdd:COG0249   163 LLDELARLAPAEILVPEDLPDPEellellrERGAAVTRLPDWAFDPDAARRRLLEQFGVASLDGFGLEDLPAAIAAAGAL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 243 LRYAKATQTRALPHLRALIVERDATFLGLDTATRRNLELTETLRGQPAPTLCSLLDNCVTAMGARLLRHALHHPWRDPTI 322
Cdd:COG0249   243 LAYLEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGGRKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 323 PAARHAAIAMLLDDdGRTLHALRQALRGFADIERIAGRIALCSARPRDLSSLRDSLQRLHELRAPLAAMLSIAAAAAPLl 402
Cdd:COG0249   323 IEARLDAVEELLED-PLLREELRELLKGVYDLERLLSRIALGRANPRDLAALRDSLAALPELKELLAELDSPLLAELAE- 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 403 aelhaQLATPDAALDLLCRAILPEPAALIRDGGVIAKGFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRV 482
Cdd:COG0249   401 -----ALDPLEDLAELLERAIVDEPPLLIRDGGVIREGYDAELDELRELSENGKEWLAELEARERERTGIKSLKVGYNKV 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 483 HGFYIEVSHANATRVPDDYRRRQTLKNAERYLTPELKAFEDKALSAQERGLAREKLLYEGLLATLQDDLPQLQQIAQAVA 562
Cdd:COG0249   476 FGYYIEVTKANADKVPDDYIRKQTLKNAERYITPELKELEDKILSAEERALALEYELFEELREEVAAHIERLQALARALA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 563 GIDLLSGFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVEEQIGGgESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTA 642
Cdd:COG0249   556 ELDVLASLAEVAVENNYVRPELDDSPGIEIEGGRHPVVEQALPG-EPFVPNDCDLDPDRRILLITGPNMAGKSTYMRQVA 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 643 LIALLAHVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALA 722
Cdd:COG0249   635 LIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIA 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 723 FAICRHLLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKA 802
Cdd:COG0249   715 WAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSYGIHVAKLAGLPASVIER 794
                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234294342 803 ARRQLREFEQRASIN-----PLQPDLFATAlanaaeaqEHPTPPAIERLRSIDPDRLTPREALDALYELKSLL 870
Cdd:COG0249   795 AREILAELEKGEAAAagkaaPDQLSLFAAA--------DPEPSPVLEELKALDPDELTPREALNLLYELKKLL 859
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
15-868 0e+00

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


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 995.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  15 HTPMMQQYLRIKAEHPGILLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGQPIKMAGVPYHAVEQYLAKLVRLGES 94
Cdd:TIGR01070   1 LTPMMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADEPIPMAGIPYHAVEAYLEKLVKQGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  95 VVICEQIGDPATSKGPVERAVARIVTPGTLTDAALLDEKRNTLLLSLCASKQFAGLAWINLASGDFRVCEVAP-SKLAAT 173
Cdd:TIGR01070  81 VAICEQIEDPKTAKGPVEREVVQLITPGTVSDEALLPERQDNLLAAIAQESNGFGLATLDLTTGEFKVTELADkETLYAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 174 LDRIRPAEIIVPESLGltftpevALTRQPDWHFDVEAARRELCTHFATRSLAGFGADALRPAIAAAGALLRYAKATQTRA 253
Cdd:TIGR01070 161 LQRLNPAEVLLAEDLS-------EMEAIELREFRKDTAVMSLEAQFGTEDLGGLGLRNAPLGLTAAGCLLQYAKRTQRTA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 254 LPHLRALIVERDATFLGLDTATRRNLELTETLRGQPAPTLCSLLDNCVTAMGARLLRHALHHPWRDPTIPAARHAAIAML 333
Cdd:TIGR01070 234 LPHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQNTLFSVLDETKTAMGSRLLKRWLHRPLRDREVLEARQDTVEVL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 334 LDDDGRTlHALRQALRGFADIERIAGRIALCSARPRDLSSLRDSLQRLHELRAPLAAMLSIAAAAAPLlaelhaQLATPD 413
Cdd:TIGR01070 314 LRHFFLR-EGLRPLLKEVGDLERLAARVALGNARPRDLARLRTSLEQLPELRALLEELEGPTLQALAA------QIDDFS 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 414 AALDLLCRAILPEPAALIRDGGVIAKGFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRVHGFYIEVSHAN 493
Cdd:TIGR01070 387 ELLELLEAALIENPPLVVRDGGLIREGYDEELDELRAASREGTDYLARLEARERERTGIPTLKVGYNAVFGYYIEVTRGQ 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 494 ATRVPDDYRRRQTLKNAERYLTPELKAFEDKALSAQERGLAREKLLYEGLLATLQDDLPQLQQIAQAVAGIDLLSGFADT 573
Cdd:TIGR01070 467 LHLVPAHYRRRQTLKNAERYITPELKEKEDKVLEAEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAEV 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 574 AQRRNYCRPLFSSEAGLLIEDGRHPVVEEQIGggESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSY 653
Cdd:TIGR01070 547 AETLHYTRPRFGDDPQLRIREGRHPVVEQVLR--TPFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSF 624
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 654 VPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKN 733
Cdd:TIGR01070 625 VPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHI 704
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 734 RCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAARRQLREFEQR 813
Cdd:TIGR01070 705 RAKTLFATHYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEAR 784
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2234294342 814 ASINPL-QPDLFATALANAAEAQEHPTPPAIERLRSIDPDRLTPREALDALYELKS 868
Cdd:TIGR01070 785 STESEApQRKAQTSAPEQISLFDEAETHPLLEELAKLDPDDLTPLQALNLLYELKK 840
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
591-807 8.71e-123

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: 369.29  E-value: 8.71e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 591 LIEDGRHPVVEEQIGGGEsFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFTR 670
Cdd:cd03284     1 EIEGGRHPVVEQVLDNEP-FVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 671 IGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTLLA 750
Cdd:cd03284    80 IGASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTELE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2234294342 751 NEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAARRQL 807
Cdd:cd03284   160 GKLPRVKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERAREIL 216
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
624-811 6.31e-112

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: 339.94  E-value: 6.31e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 624 LLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSL 703
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 704 VLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQ 783
Cdd:pfam00488  81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAADK 160
                         170       180
                  ....*....|....*....|....*...
gi 2234294342 784 SYGIQVAALAGIPSAVLKAARRQLREFE 811
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERAREILAELE 188
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
623-807 3.15e-97

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 301.40  E-value: 3.15e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  623 LLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHS 702
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  703 LVLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPAN 782
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVAG 160
                          170       180
                   ....*....|....*....|....*
gi 2234294342  783 QSYGIQVAALAGIPSAVLKAARRQL 807
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
 
Name Accession Description Interval E-value
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
11-870 0e+00

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 1335.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  11 DVTGHTPMMQQYLRIKAEHPGILLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGQPIKMAGVPYHAVEQYLAKLVR 90
Cdd:PRK05399    4 DMSKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDITLTKRGKSAGEPIPMAGVPYHAAEGYLAKLVK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  91 LGESVVICEQIGDPATSKGPVERAVARIVTPGTLTDAALLDEKRNTLLLSLCASKQFAGLAWINLASGDFRVCEVAPSKL 170
Cdd:PRK05399   84 KGYKVAICEQVEDPATAKGPVKREVVRIVTPGTVTDEALLDEKQNNYLAAIAQDGGGYGLAYLDLSTGEFRVTELDEEEL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 171 AATLDRIRPAEIIVPESLGLTFTPEV--ALTRQPDWHFDVEAARRELCTHFATRSLAGFGADaLRPAIAAAGALLRYAKA 248
Cdd:PRK05399  164 LAELARLNPAEILVPEDFSEDELLLLrrGLRRRPPWEFDLDTAEKRLLEQFGVASLDGFGVD-LPLAIRAAGALLQYLKE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 249 TQTRALPHLRALIVERDATFLGLDTATRRNLELTETLRGQPAPTLCSLLDNCVTAMGARLLRHALHHPWRDPTIPAARHA 328
Cdd:PRK05399  243 TQKRSLPHLRSPKRYEESDYLILDAATRRNLELTENLRGGRKNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 329 AIAMLLDDDGrTLHALRQALRGFADIERIAGRIALCSARPRDLSSLRDSLQRLHELRAPLAAMLSIAAAAAPLlaelhaQ 408
Cdd:PRK05399  323 AVEELLEDPL-LREDLRELLKGVYDLERLLSRIALGRANPRDLAALRDSLEALPELKELLAELDSPLLAELAE------Q 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 409 LATPDAALDLLCRAILPEPAALIRDGGVIAKGFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRVHGFYIE 488
Cdd:PRK05399  396 LDPLEELADLLERAIVEEPPLLIRDGGVIADGYDAELDELRALSDNGKDWLAELEARERERTGISSLKVGYNKVFGYYIE 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 489 VSHANATRVPDDYRRRQTLKNAERYLTPELKAFEDKALSAQERGLAREKLLYEGLLATLQDDLPQLQQIAQAVAGIDLLS 568
Cdd:PRK05399  476 VTKANLDKVPEDYIRRQTLKNAERYITPELKELEDKILSAEEKALALEYELFEELREEVAEHIERLQKLAKALAELDVLA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 569 GFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVEeQIGGGESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLA 648
Cdd:PRK05399  556 SLAEVAEENNYVRPEFTDDPGIDIEEGRHPVVE-QVLGGEPFVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLA 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 649 HVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRH 728
Cdd:PRK05399  635 QIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEY 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 729 LLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAARRQLR 808
Cdd:PRK05399  715 LHDKIGAKTLFATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREILA 794
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234294342 809 EFEQR------ASINPLQPDLFatalanaaeaQEHPTPPAIERLRSIDPDRLTPREALDALYELKSLL 870
Cdd:PRK05399  795 QLESAsekakaASAEEDQLSLF----------AEPEESPLLEALKALDPDNLTPREALNLLYELKKLL 852
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
11-870 0e+00

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 1328.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  11 DVTGHTPMMQQYLRIKAEHPGILLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGQPIKMAGVPYHAVEQYLAKLVR 90
Cdd:COG0249     3 DMAKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDITLTKRGKGAGEPIPMAGVPYHAAEGYLAKLVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  91 LGESVVICEQIGDPATSKGPVERAVARIVTPGTLTDAALLDEKRNTLLLSLCASKQFAGLAWINLASGDFRVCEVA-PSK 169
Cdd:COG0249    83 AGYKVAICEQVEDPAEAKGLVKREVVRVVTPGTLTEDALLDAKRNNYLAAVARDKGRYGLAWLDISTGEFLVTELDgEEA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 170 LAATLDRIRPAEIIVPESLGLTF-------TPEVALTRQPDWHFDVEAARRELCTHFATRSLAGFGADALRPAIAAAGAL 242
Cdd:COG0249   163 LLDELARLAPAEILVPEDLPDPEellellrERGAAVTRLPDWAFDPDAARRRLLEQFGVASLDGFGLEDLPAAIAAAGAL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 243 LRYAKATQTRALPHLRALIVERDATFLGLDTATRRNLELTETLRGQPAPTLCSLLDNCVTAMGARLLRHALHHPWRDPTI 322
Cdd:COG0249   243 LAYLEETQKGALPHLRRLRRYEEDDYLILDAATRRNLELTETLRGGRKGSLLSVLDRTVTAMGSRLLRRWLLRPLRDRAA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 323 PAARHAAIAMLLDDdGRTLHALRQALRGFADIERIAGRIALCSARPRDLSSLRDSLQRLHELRAPLAAMLSIAAAAAPLl 402
Cdd:COG0249   323 IEARLDAVEELLED-PLLREELRELLKGVYDLERLLSRIALGRANPRDLAALRDSLAALPELKELLAELDSPLLAELAE- 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 403 aelhaQLATPDAALDLLCRAILPEPAALIRDGGVIAKGFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRV 482
Cdd:COG0249   401 -----ALDPLEDLAELLERAIVDEPPLLIRDGGVIREGYDAELDELRELSENGKEWLAELEARERERTGIKSLKVGYNKV 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 483 HGFYIEVSHANATRVPDDYRRRQTLKNAERYLTPELKAFEDKALSAQERGLAREKLLYEGLLATLQDDLPQLQQIAQAVA 562
Cdd:COG0249   476 FGYYIEVTKANADKVPDDYIRKQTLKNAERYITPELKELEDKILSAEERALALEYELFEELREEVAAHIERLQALARALA 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 563 GIDLLSGFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVEEQIGGgESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTA 642
Cdd:COG0249   556 ELDVLASLAEVAVENNYVRPELDDSPGIEIEGGRHPVVEQALPG-EPFVPNDCDLDPDRRILLITGPNMAGKSTYMRQVA 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 643 LIALLAHVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALA 722
Cdd:COG0249   635 LIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIA 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 723 FAICRHLLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKA 802
Cdd:COG0249   715 WAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSYGIHVAKLAGLPASVIER 794
                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234294342 803 ARRQLREFEQRASIN-----PLQPDLFATAlanaaeaqEHPTPPAIERLRSIDPDRLTPREALDALYELKSLL 870
Cdd:COG0249   795 AREILAELEKGEAAAagkaaPDQLSLFAAA--------DPEPSPVLEELKALDPDELTPREALNLLYELKKLL 859
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
15-868 0e+00

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


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 995.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  15 HTPMMQQYLRIKAEHPGILLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGQPIKMAGVPYHAVEQYLAKLVRLGES 94
Cdd:TIGR01070   1 LTPMMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQSADEPIPMAGIPYHAVEAYLEKLVKQGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  95 VVICEQIGDPATSKGPVERAVARIVTPGTLTDAALLDEKRNTLLLSLCASKQFAGLAWINLASGDFRVCEVAP-SKLAAT 173
Cdd:TIGR01070  81 VAICEQIEDPKTAKGPVEREVVQLITPGTVSDEALLPERQDNLLAAIAQESNGFGLATLDLTTGEFKVTELADkETLYAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 174 LDRIRPAEIIVPESLGltftpevALTRQPDWHFDVEAARRELCTHFATRSLAGFGADALRPAIAAAGALLRYAKATQTRA 253
Cdd:TIGR01070 161 LQRLNPAEVLLAEDLS-------EMEAIELREFRKDTAVMSLEAQFGTEDLGGLGLRNAPLGLTAAGCLLQYAKRTQRTA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 254 LPHLRALIVERDATFLGLDTATRRNLELTETLRGQPAPTLCSLLDNCVTAMGARLLRHALHHPWRDPTIPAARHAAIAML 333
Cdd:TIGR01070 234 LPHLQPVRLYELQDFMQLDAATRRNLELTENLRGGKQNTLFSVLDETKTAMGSRLLKRWLHRPLRDREVLEARQDTVEVL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 334 LDDDGRTlHALRQALRGFADIERIAGRIALCSARPRDLSSLRDSLQRLHELRAPLAAMLSIAAAAAPLlaelhaQLATPD 413
Cdd:TIGR01070 314 LRHFFLR-EGLRPLLKEVGDLERLAARVALGNARPRDLARLRTSLEQLPELRALLEELEGPTLQALAA------QIDDFS 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 414 AALDLLCRAILPEPAALIRDGGVIAKGFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRVHGFYIEVSHAN 493
Cdd:TIGR01070 387 ELLELLEAALIENPPLVVRDGGLIREGYDEELDELRAASREGTDYLARLEARERERTGIPTLKVGYNAVFGYYIEVTRGQ 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 494 ATRVPDDYRRRQTLKNAERYLTPELKAFEDKALSAQERGLAREKLLYEGLLATLQDDLPQLQQIAQAVAGIDLLSGFADT 573
Cdd:TIGR01070 467 LHLVPAHYRRRQTLKNAERYITPELKEKEDKVLEAEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAEV 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 574 AQRRNYCRPLFSSEAGLLIEDGRHPVVEEQIGggESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSY 653
Cdd:TIGR01070 547 AETLHYTRPRFGDDPQLRIREGRHPVVEQVLR--TPFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQTALIALLAQIGSF 624
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 654 VPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKN 733
Cdd:TIGR01070 625 VPAESAELPLFDRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHI 704
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 734 RCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAARRQLREFEQR 813
Cdd:TIGR01070 705 RAKTLFATHYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEAR 784
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2234294342 814 ASINPL-QPDLFATALANAAEAQEHPTPPAIERLRSIDPDRLTPREALDALYELKS 868
Cdd:TIGR01070 785 STESEApQRKAQTSAPEQISLFDEAETHPLLEELAKLDPDDLTPLQALNLLYELKK 840
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
591-807 8.71e-123

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: 369.29  E-value: 8.71e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 591 LIEDGRHPVVEEQIGGGEsFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFTR 670
Cdd:cd03284     1 EIEGGRHPVVEQVLDNEP-FVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 671 IGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTLLA 750
Cdd:cd03284    80 IGASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTELE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2234294342 751 NEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAARRQL 807
Cdd:cd03284   160 GKLPRVKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERAREIL 216
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
624-811 6.31e-112

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: 339.94  E-value: 6.31e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 624 LLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHSL 703
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 704 VLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQ 783
Cdd:pfam00488  81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAADK 160
                         170       180
                  ....*....|....*....|....*...
gi 2234294342 784 SYGIQVAALAGIPSAVLKAARRQLREFE 811
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERAREILAELE 188
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
623-807 3.15e-97

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 301.40  E-value: 3.15e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  623 LLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEHS 702
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  703 LVLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTLLANEYPDLANVHLDAIEHGERIVFLHAVEEGPAN 782
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVAG 160
                          170       180
                   ....*....|....*....|....*
gi 2234294342  783 QSYGIQVAALAGIPSAVLKAARRQL 807
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
591-811 2.89e-85

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: 271.56  E-value: 2.89e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 591 LIEDGRHPVVEEQIGGgeSFIANDTRLG-DERRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFT 669
Cdd:cd03285     1 VLKEARHPCVEAQDDV--AFIPNDVTLTrGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 670 RIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTLL 749
Cdd:cd03285    79 RVGASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQIKCFCLFATHFHELTAL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2234294342 750 ANEYPDLANVHLDAI--EHGERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAARRQLREFE 811
Cdd:cd03285   159 ADEVPNVKNLHVTALtdDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQKALELE 222
MutS_III pfam05192
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair ...
274-571 6.77e-83

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: 267.73  E-value: 6.77e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 274 ATRRNLELTETLRGQPAPTLCSLLDNCVTAMGARLLRHALHHPWRDPTIPAARHAAIAMLLDDDGrTLHALRQALRGFAD 353
Cdd:pfam05192   1 ATLRNLELTENLRGGKEGSLLGLLDRTKTPMGSRLLRQWLLQPLTDLEEINERLDAVEELLENSE-LREDLRELLRRLPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 354 IERIAGRIALCSARPRDLSSLRDSLQRLHELRAPLAAMLSIaaaaapllaelhaQLATPDAALDLLCRAILPEPAALIRD 433
Cdd:pfam05192  80 LERLLSRIALGKATPRDLLALLDSLEKLPLLKELLLEEKSA-------------LLGELASLAELLEEAIDEEPPALLRD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 434 GGVIAKGFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRVHG-------FYIEVSHANATRVPDDYRRRQT 506
Cdd:pfam05192 147 GGVIRDGYDEELDELRDLLLDGKRLLAKLEARERERTGIKSLKVLYNKVFGyylllveYYIEVSKSQKDKVPDDYIRIQT 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234294342 507 LKNAERYLTPELKAFEDKALSAQERGLAREKLLYEGLLATLQDDLPQLQQIAQAVAGIDLLSGFA 571
Cdd:pfam05192 227 TKNAERYITPELKELERKILQAEERLLALEKELFEELLEEVLEYIEVLRRAAEALAELDVLLSLA 291
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
592-795 7.26e-83

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: 264.50  E-value: 7.26e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 592 IEDGRHPVVEeQIGGGESFIANDTRLGDeRRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFTRI 671
Cdd:cd03243     2 IKGGRHPVLL-ALTKGETFVPNDINLGS-GRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 672 GAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKnRCLTLFATHYFELTLLAN 751
Cdd:cd03243    80 GAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEK-GCRTLFATHFHELADLPE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2234294342 752 EYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGI 795
Cdd:cd03243   159 QVPGVKNLHMEELITTGGLTFTYKLIDGICDPSYALQIAELAGL 202
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
291-603 2.54e-79

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 258.77  E-value: 2.54e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  291 PTLCSLLDNCVTAMGARLLRHALHHPWRDPTIPAARHAAIAMLLDDDGRTLHaLRQALRGFADIERIAGRIALCSARPRD 370
Cdd:smart00533   2 GSLFELLNHTKTPMGKRLLRRWLLQPLLDLKEINERLDAVEELVENPELRQK-LRQLLKRIPDLERLLSRIERGRASPRD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  371 LSSLRDSLQRLHELRAPLAAMLSIAAAAAPLlaelhaQLATPDAAL-DLLCRAILPEPAALIRDGGVIAKGFDADLDELR 449
Cdd:smart00533  81 LLRLYDSLEGLKEIRQLLESLDGPLLGLLLK------VILEPLLELlELLLELLNDDDPLEVNDGGLIKDGFDPELDELR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  450 ALNDHCGTFLLELEARERERTGIGNLKVEYNRVHGFYIEVSHANATRVPDDYRRRQTLKNAERYLTPELKAFEDKALSAQ 529
Cdd:smart00533 155 EKLEELEEELEELLKKEREELGIDSLKLGYNKVHGYYIEVTKSEAKKVPKDFIRRSSLKNTERFTTPELKELENELLEAK 234
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2234294342  530 ERGLAREKLLYEGLLATLQDDLPQLQQIAQAVAGIDLLSGFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVEEQ 603
Cdd:smart00533 235 EEIERLEKEILRELLEKVLEYLEELRALAEALAELDVLLSLATLAAEGNYVRPEFVDSGELEIKNGRHPVLELQ 308
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
591-803 1.54e-77

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: 250.81  E-value: 1.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 591 LIEDGRHPVVEEQigGGESFIANDTRLGDER-RLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFT 669
Cdd:cd03286     1 CFEELRHPCLNAS--TASSFVPNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 670 RIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTLL 749
Cdd:cd03286    79 RIGARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKCLTLFSTHYHSLCDE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 750 ANEYPDLANVHLDAIEHGE------RIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAA 803
Cdd:cd03286   159 FHEHGGVRLGHMACAVKNEsdptirDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
590-803 6.56e-71

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: 233.15  E-value: 6.56e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 590 LLIEDGRHPVVEEQIGggESFIANDTRL-GDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIF 668
Cdd:cd03287     1 ILIKEGRHPMIESLLD--KSFVPNDIHLsAEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 669 TRIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKNRCLTLFATHYFELTL 748
Cdd:cd03287    79 TRMGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEKKCLVLFVTHYPSLGE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2234294342 749 LANEYPD-LANVHLDAIEH--------GERIVFLHAVEEGPANQSYGIQVAALAGIPSAVLKAA 803
Cdd:cd03287   159 ILRRFEGsIRNYHMSYLESqkdfetsdSQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
592-795 3.23e-55

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: 189.82  E-value: 3.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 592 IEDGRHPVVEEQIgggESFIANDTRL-GDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFTR 670
Cdd:cd03281     2 IQGGRHPLLELFV---DSFVPNDTEIgGGGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 671 IGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEK--NRCLTLFATHYFELTL 748
Cdd:cd03281    79 MSSRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRgpECPRVIVSTHFHELFN 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2234294342 749 LANEYPDLANVHL--------DAIEHGERIVFLHAVEEGPANQSYGIQVAALAGI 795
Cdd:cd03281   159 RSLLPERLKIKFLtmevllnpTSTSPNEDITYLYRLVPGLADTSFAIHCAKLAGI 213
MutS_I pfam01624
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ...
16-126 9.61e-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: 184.71  E-value: 9.61e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342  16 TPMMQQYLRIKAEHPGILLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGQPIKMAGVPYHAVEQYLAKLVRLGESV 95
Cdd:pfam01624   1 TPMMRQYLELKSKYPDAVLFFRVGDFYELFGEDAEIAARELGITLTVRKGGSGKRIPMAGVPEHAFERYARRLVNKGYKV 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2234294342  96 VICEQIGDPATSKGPVERAVARIVTPGTLTD 126
Cdd:pfam01624  81 AICEQTETPAEAKGVVKREVVRVVTPGTLTD 111
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
591-793 1.92e-48

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: 170.65  E-value: 1.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 591 LIEDGRHPVVEeqiGGGESFIANDTRL-GDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPLDQIFT 669
Cdd:cd03282     1 IIRDSRHPILD---RDKKNFIPNDIYLtRGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 670 RIGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKnRCLTLFATHYFELTLL 749
Cdd:cd03282    78 RLSNDDSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKK-ESTVFFATHFRDIAAI 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2234294342 750 ANEYPDLANVHLDA--IEHGErIVFLHAVEEGPANQ-SYGIQVAALA 793
Cdd:cd03282   157 LGNKSCVVHLHMKAqsINSNG-IEMAYKLVLGLYRIvDDGIRFVRVL 202
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
592-795 1.54e-36

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: 136.66  E-value: 1.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 592 IEDGRHPVVEEqigggESFIANDTRLGDeRRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLgPLDQIFTRI 671
Cdd:cd03283     2 AKNLGHPLIGR-----EKRVANDIDMEK-KNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFEL-PPVKIFTSI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 672 GAADDLAAGRSTFMVEMIESAAILHHA--TEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKNrCLTLFATHYFELTLL 749
Cdd:cd03283    75 RVSDDLRDGISYFYAELRRLKEIVEKAkkGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKN-TIGIISTHDLELADL 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2234294342 750 ANEYPDLANVHLDAIEHGERIVFLHAVEEGPANQSYGIQVAALAGI 795
Cdd:cd03283   154 LDLDSAVRNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIGI 199
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
592-758 1.23e-34

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: 131.22  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 592 IEDGRHPVVEEQiggGESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPL-DQIFTR 670
Cdd:cd03280     2 LREARHPLLPLQ---GEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAEGSSLPVfENIFAD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 671 IGAADDLAAGRSTFMVEMIESAAILHHATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKNrCLTLFATHYFELTLLA 750
Cdd:cd03280    79 IGDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERG-ALVIATTHYGELKAYA 157

                  ....*...
gi 2234294342 751 NEYPDLAN 758
Cdd:cd03280   158 YKREGVEN 165
MutS_IV pfam05190
MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch ...
440-531 1.65e-34

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: 126.57  E-value: 1.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 440 GFDADLDELRALNDHCGTFLLELEARERERTGIGNLKVEYNRVHGFYIEVSHANATRVPDDYRRRQTLKNAERYLTPELK 519
Cdd:pfam05190   1 GFDEELDELRDLLDELEKELEELEKKEREKLGIKSLKVGYNKVFGYYIEVTRSEAKKVPSNYIRRQTLKNGVRFTTPELK 80
                          90
                  ....*....|..
gi 2234294342 520 AFEDKALSAQER 531
Cdd:pfam05190  81 KLEDELLEAEEE 92
mutS2 TIGR01069
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ...
543-810 2.10e-33

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: 138.03  E-value: 2.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 543 LLATLQDDLPQLQQIAQAVAGIDLLSGFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVEEQigggeSFIANDTRLGDERR 622
Cdd:TIGR01069 249 LSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMPSFTGKIILENARHPLLKEP-----KVVPFTLNLKFEKR 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 623 LLLITGPNMGGKSTYMRQTALIALLAHVGSYVPATRAVLGPL-DQIFTRIGAADDLAAGRSTFMVEMIESAAILHHATEH 701
Cdd:TIGR01069 324 VLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEHSEIPYfEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTEN 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 702 SLVLMDEVGRGTSTFDGMALAFAICRHLLEKNrCLTLFATHYFELTLLA--NEYPDLANVHLDAiehgERIVFLHAVEEG 779
Cdd:TIGR01069 404 SLVLFDELGAGTDPDEGSALAISILEYLLKQN-AQVLITTHYKELKALMynNEGVENASVLFDE----ETLSPTYKLLKG 478
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2234294342 780 PANQSYGIQVAALAGIPSAVLKAARRQLREF 810
Cdd:TIGR01069 479 IPGESYAFEIAQRYGIPHFIIEQAKTFYGEF 509
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
524-758 5.55e-33

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 136.81  E-value: 5.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 524 KALSAQERglaRE--KLLYEgLLATLQDDLPQLQQIAQAVAGIDLLSGFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVE 601
Cdd:COG1193   235 RELEAEER---REieRILRE-LSALVREYAEELLENLEILAELDFIFAKARYALELKAVKPELNDEGYIKLKKARHPLLD 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 602 EqigggESFIANDTRLGDERRLLLITGPNMGGKSTYMRQTALIALLAHVGSYVPAT-RAVLGPLDQIFTRIGAADDLAAG 680
Cdd:COG1193   311 L-----KKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAeGSELPVFDNIFADIGDEQSIEQS 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 681 RSTF---MVEMIEsaaILHHATEHSLVLMDEVGRGTstfD---GMALAFAICRHLLEKNrCLTLFATHYFELTLLANEYP 754
Cdd:COG1193   386 LSTFsshMTNIVE---ILEKADENSLVLLDELGAGT---DpqeGAALAIAILEELLERG-ARVVATTHYSELKAYAYNTE 458

                  ....
gi 2234294342 755 DLAN 758
Cdd:COG1193   459 GVEN 462
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
475-751 1.71e-27

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 119.55  E-value: 1.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 475 LKVEYNR-----VHG-------FYIEvshanatrvPDDYrrrQTLKNAERyltpELKAFEDkalsaQERglarEKLLYEg 542
Cdd:PRK00409  200 VKAEYKHaikgiVHDqsssgatLYIE---------PQSV---VELNNEIR----ELRNKEE-----QEI----ERILKE- 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 543 LLATLQDDLPQLQQIAQAVAGIDLLSGFADTAQRRNYCRPLFSSEAGLLIEDGRHPVVEEqigggESFIANDTRLGDERR 622
Cdd:PRK00409  254 LSAKVAKNLDFLKFLNKIFDELDFIFARARYAKALKATFPLFNDEGKIDLRQARHPLLDG-----EKVVPKDISLGFDKT 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 623 LLLITGPNMGGKSTYMRQTALIALLAHVGSYVPA-TRAVLGPLDQIFTRIG----AADDLaagrSTFMVEMIESAAILHH 697
Cdd:PRK00409  329 VLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPAnEPSEIPVFKEIFADIGdeqsIEQSL----STFSGHMTNIVRILEK 404
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2234294342 698 ATEHSLVLMDEVGRGTSTFDGMALAFAICRHLLEKNrCLTLFATHYFEL-TLLAN 751
Cdd:PRK00409  405 ADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRG-AKIIATTHYKELkALMYN 458
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
592-751 1.22e-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: 106.68  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 592 IEDGRHPVVeeqigggesFIANDTRLGDERrLLLITGPNMGGKSTYMRQTALIALLA----------HVGSYVPATRAVL 661
Cdd:cd03227     2 IVLGRFPSY---------FVPNDVTFGEGS-LTIITGPNGSGKSTILDAIGLALGGAqsatrrrsgvKAGCIVAAVSAEL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 662 gpldqIFTRIGaaddLAAGrstfMVEMIESAAILHHAT--EHSLVLMDEVGRGTSTFDGMALAFAICRHLleKNRCLTLF 739
Cdd:cd03227    72 -----IFTRLQ----LSGG----EKELSALALILALASlkPRPLYILDEIDRGLDPRDGQALAEAILEHL--VKGAQVIV 136
                         170
                  ....*....|..
gi 2234294342 740 ATHYFELTLLAN 751
Cdd:cd03227   137 ITHLPELAELAD 148
MutS_II pfam05188
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair ...
149-258 4.83e-25

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: 101.27  E-value: 4.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 149 GLAWINLASGDFRVCEVAP-SKLAATLDRIRPAEIIVPESLGLTFTPEVA--------LTRQPDWHFDVEAARRELCTHF 219
Cdd:pfam05188  15 GLAFLDLSTGEFGVSEFEDfEELLAELSRLSPKELLLPESLSSSTVAESQkllelrlrVGRRPTWLFELEHAYEDLNEDF 94
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2234294342 220 ATRSLAGFGADALRPAIAAAGALLRYAKATQTRALPHLR 258
Cdd:pfam05188  95 GVEDLDGFGLEELPLALCAAGALISYLKETQKENLPHIQ 133
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
592-750 2.59e-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: 59.57  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 592 IEDGRHPvveeqIGGGESFIANDTRLgDERRLLLITGPNMGGKSTYMRqtaLIALLAHVGS---YVPATRAVLGPLDQIF 668
Cdd:cd00267     2 IENLSFR-----YGGRTALDNVSLTL-KAGEIVALVGPNGSGKSTLLR---AIAGLLKPTSgeiLIDGKDIAKLPLEELR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234294342 669 TRIGAADDLAAGrstfMVEMIESAAILHHATehSLVLMDEVGRGTSTFDGMALAfAICRHLLEKNRcLTLFATHYFELTL 748
Cdd:cd00267    73 RRIGYVPQLSGG----QRQRVALARALLLNP--DLLLLDEPTSGLDPASRERLL-ELLRELAEEGR-TVIIVTHDPELAE 144

                  ..
gi 2234294342 749 LA 750
Cdd:cd00267   145 LA 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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