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Conserved domains on  [gi|6678938|ref|NP_032654|]
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DNA mismatch repair protein Msh2 [Mus musculus]

Protein Classification

DNA mismatch repair protein MutS( domain architecture ID 11415631)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MutS super family cl33816
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
152-853 7.49e-162

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


The actual alignment was detected with superfamily member COG0249:

Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 495.74  E-value: 7.49e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  152 MAVVDGQRHVGVGYVD-STQRkLGLCEFPENDQfsnLEALLIQIGPKECVLPggETTGDMGKLRQVIQRGGILITERKRA 230
Cdd:COG0249 131 AAVARDKGRYGLAWLDiSTGE-FLVTELDGEEA---LLDELARLAPAEILVP--EDLPDPEELLELLRERGAAVTRLPDW 204
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  231 DFSTKDIYQDLNRLLKGKkgeqiNSAALPEMENQVAVSSLSAVIKFLEllsdDSNFGQFE----LATFDFSQYMKLDMAA 306
Cdd:COG0249 205 AFDPDAARRRLLEQFGVA-----SLDGFGLEDLPAAIAAAGALLAYLE----ETQKGALPhlrrLRRYEEDDYLILDAAT 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  307 VRALNLFQGSVEDTTGSqsLAALLNKCKTAQGQRLVNQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQEdLLRRFPD 386
Cdd:COG0249 276 RRNLELTETLRGGRKGS--LLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEARLDAVEELLEDPLLREELRE-LLKGVYD 352
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  387 LNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALEKYEGRHQALLLAVFvTPLIDLRsdfskfqEMIETTLdmdqVENH 466
Cdd:COG0249 353 LERLLSRIALGRANPRDLAALRDSLAALPELKELLAELDSPLLAELAEAL-DPLEDLA-------ELLERAI----VDEP 420
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  467 EFLV------KPSFDPNLSELREVMDG-------LEKKMQ-----STLinaarglgldpgkqiKLDSSAQFGYYFRVTck 528
Cdd:COG0249 421 PLLIrdggviREGYDAELDELRELSENgkewlaeLEARERertgiKSL---------------KVGYNKVFGYYIEVT-- 483
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  529 eekvlrnNKNFSTVD-----IQ--KNGVKFTNSELSslneeytknkgEYEE----AQDAIV-------KEIVNISSGYVE 590
Cdd:COG0249 484 -------KANADKVPddyirKQtlKNAERYITPELK-----------ELEDkilsAEERALaleyelfEELREEVAAHIE 545
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  591 PMQTLNDVLAHLDAIVSFAHVS---NaapvpYVRPVILEKGkgRIILKASRHACVE-VQDEVAFIPNDVHFEKDKQMfHI 666
Cdd:COG0249 546 RLQALARALAELDVLASLAEVAvenN-----YVRPELDDSP--GIEIEGGRHPVVEqALPGEPFVPNDCDLDPDRRI-LL 617
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  667 ITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLII 746
Cdd:COG0249 618 ITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVL 697
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  747 IDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSF 826
Cdd:COG0249 698 LDEIGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSY 777
                       730       740
                ....*....|....*....|....*..
gi 6678938  827 GIHVAELANFPRHVIACAKQKALELEE 853
Cdd:COG0249 778 GIHVAKLAGLPASVIERAREILAELEK 804
MutS_I pfam01624
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ...
18-132 2.50e-29

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: 112.68  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     18 GFVRFFEGMPEKPSTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYmgpAGSKTLQSVVLSKMNFESFVKDLLLvRQ 97
Cdd:pfam01624   2 PMMRQYLELKSKYPDAVLFFRVGDFYELFGEDAEIAARELGITLTVRKG---GSGKRIPMAGVPEHAFERYARRLVN-KG 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 6678938     98 YRVEVYKNKAGNKASK-ENEWYLAFKASPGNLSQFE 132
Cdd:pfam01624  78 YKVAICEQTETPAEAKgVVKREVVRVVTPGTLTDDE 113
 
Name Accession Description Interval E-value
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
152-853 7.49e-162

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 495.74  E-value: 7.49e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  152 MAVVDGQRHVGVGYVD-STQRkLGLCEFPENDQfsnLEALLIQIGPKECVLPggETTGDMGKLRQVIQRGGILITERKRA 230
Cdd:COG0249 131 AAVARDKGRYGLAWLDiSTGE-FLVTELDGEEA---LLDELARLAPAEILVP--EDLPDPEELLELLRERGAAVTRLPDW 204
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  231 DFSTKDIYQDLNRLLKGKkgeqiNSAALPEMENQVAVSSLSAVIKFLEllsdDSNFGQFE----LATFDFSQYMKLDMAA 306
Cdd:COG0249 205 AFDPDAARRRLLEQFGVA-----SLDGFGLEDLPAAIAAAGALLAYLE----ETQKGALPhlrrLRRYEEDDYLILDAAT 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  307 VRALNLFQGSVEDTTGSqsLAALLNKCKTAQGQRLVNQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQEdLLRRFPD 386
Cdd:COG0249 276 RRNLELTETLRGGRKGS--LLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEARLDAVEELLEDPLLREELRE-LLKGVYD 352
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  387 LNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALEKYEGRHQALLLAVFvTPLIDLRsdfskfqEMIETTLdmdqVENH 466
Cdd:COG0249 353 LERLLSRIALGRANPRDLAALRDSLAALPELKELLAELDSPLLAELAEAL-DPLEDLA-------ELLERAI----VDEP 420
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  467 EFLV------KPSFDPNLSELREVMDG-------LEKKMQ-----STLinaarglgldpgkqiKLDSSAQFGYYFRVTck 528
Cdd:COG0249 421 PLLIrdggviREGYDAELDELRELSENgkewlaeLEARERertgiKSL---------------KVGYNKVFGYYIEVT-- 483
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  529 eekvlrnNKNFSTVD-----IQ--KNGVKFTNSELSslneeytknkgEYEE----AQDAIV-------KEIVNISSGYVE 590
Cdd:COG0249 484 -------KANADKVPddyirKQtlKNAERYITPELK-----------ELEDkilsAEERALaleyelfEELREEVAAHIE 545
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  591 PMQTLNDVLAHLDAIVSFAHVS---NaapvpYVRPVILEKGkgRIILKASRHACVE-VQDEVAFIPNDVHFEKDKQMfHI 666
Cdd:COG0249 546 RLQALARALAELDVLASLAEVAvenN-----YVRPELDDSP--GIEIEGGRHPVVEqALPGEPFVPNDCDLDPDRRI-LL 617
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  667 ITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLII 746
Cdd:COG0249 618 ITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVL 697
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  747 IDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSF 826
Cdd:COG0249 698 LDEIGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSY 777
                       730       740
                ....*....|....*....|....*..
gi 6678938  827 GIHVAELANFPRHVIACAKQKALELEE 853
Cdd:COG0249 778 GIHVAKLAGLPASVIERAREILAELEK 804
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
152-853 3.82e-159

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 488.84  E-value: 3.82e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   152 MAVVDGQRHVGVGYVDSTQRKLGLCEFPENDqfsnLEALLIQIGPKECVLPGGETTGDMGKLRQVIQRggiliteRKRAD 231
Cdd:PRK05399 132 AAIAQDGGGYGLAYLDLSTGEFRVTELDEEE----LLAELARLNPAEILVPEDFSEDELLLLRRGLRR-------RPPWE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   232 FSTKDIYQDLNRLLKGK--KGEQINSAAlpemenqvAVSSLSAVIKFLEllsdDSNFGQFE----LATFDFSQYMKLDMA 305
Cdd:PRK05399 201 FDLDTAEKRLLEQFGVAslDGFGVDLPL--------AIRAAGALLQYLK----ETQKRSLPhlrsPKRYEESDYLILDAA 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   306 AVRALNLFQgSVEDTTgSQSLAALLNKCKTAQGQRLVNQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQEdLLRRFP 385
Cdd:PRK05399 269 TRRNLELTE-NLRGGR-KNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLDAVEELLEDPLLREDLRE-LLKGVY 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   386 DLNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALEKyegrHQALLLAVFVTPLidlrSDFSKFQEMIETTLdmdqVEN 465
Cdd:PRK05399 346 DLERLLSRIALGRANPRDLAALRDSLEALPELKELLAE----LDSPLLAELAEQL----DPLEELADLLERAI----VEE 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   466 HEFLV------KPSFDPNLSELREVMDG-------LEKK-MQSTLINAarglgldpgkqIKLDSSAQFGYYFRVTckeek 531
Cdd:PRK05399 414 PPLLIrdggviADGYDAELDELRALSDNgkdwlaeLEAReRERTGISS-----------LKVGYNKVFGYYIEVT----- 477
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   532 vlrnNKNFSTVD-----IQ--KNGVKFTNSELSslneeytknkgEYEE----AQDAIV-------KEIVNISSGYVEPMQ 593
Cdd:PRK05399 478 ----KANLDKVPedyirRQtlKNAERYITPELK-----------ELEDkilsAEEKALaleyelfEELREEVAEHIERLQ 542
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   594 TLNDVLAHLDAIVSFAHVS---NaapvpYVRPVILEKGkgRIILKASRHACVE-VQDEVAFIPNDVHFEKDKQMfHIITG 669
Cdd:PRK05399 543 KLAKALAELDVLASLAEVAeenN-----YVRPEFTDDP--GIDIEEGRHPVVEqVLGGEPFVPNDCDLDEERRL-LLITG 614
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   670 PNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDE 749
Cdd:PRK05399 615 PNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDE 694
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   750 LGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIH 829
Cdd:PRK05399 695 IGRGTSTYDGLSIAWAVAEYLHDKIGAKTLFATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIH 774
                        730       740
                 ....*....|....*....|....
gi 6678938   830 VAELANFPRHVIACAKQKALELEE 853
Cdd:PRK05399 775 VAKLAGLPASVIKRAREILAQLES 798
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
633-852 1.79e-149

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: 440.66  E-value: 1.79e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  633 ILKASRHACVEVQDEVAFIPNDVHFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARV 712
Cdd:cd03285   1 VLKEARHPCVEAQDDVAFIPNDVTLTRGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILARV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  713 GAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALAN 792
Cdd:cd03285  81 GASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQIKCFCLFATHFHELTALAD 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678938  793 QIPTVNNLHV--TALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPRHVIACAKQKALELE 852
Cdd:cd03285 161 EVPNVKNLHVtaLTDDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQKALELE 222
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
36-910 1.43e-131

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


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 416.09  E-value: 1.43e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     36 LFDRGDFYTAHGEDALLAAREVFKTqgVIKYMGPAGsktlQSVVLSKMNFESFVK--DLLLVRQYRVEVYKNKAGNKASK 113
Cdd:TIGR01070  21 FFRMGDFYELFYEDAKKAAQLLDIS--LTSRGQSAD----EPIPMAGIPYHAVEAylEKLVKQGESVAICEQIEDPKTAK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    114 ---ENEwyLAFKASPGNLSQFEDILFGNNDMSAsvgvmgikmAVVDGQRHVGVGYVDSTQRKLGLCEFPEndqFSNLEAL 190
Cdd:TIGR01070  95 gpvERE--VVQLITPGTVSDEALLPERQDNLLA---------AIAQESNGFGLATLDLTTGEFKVTELAD---KETLYAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    191 LIQIGPKECVLPGGETTGDMGKLRQVIQRGGILITERKradFSTKDIyqdlnRLLKGKKGEQINSAALPEM----ENQ-V 265
Cdd:TIGR01070 161 LQRLNPAEVLLAEDLSEMEAIELREFRKDTAVMSLEAQ---FGTEDL-----GGLGLRNAPLGLTAAGCLLqyakRTQrT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    266 AVSSLSAVIKFlellsddsnfgqfelatfDFSQYMKLDMAAVRALNLFQ---GSVEDTtgsqsLAALLNKCKTAQGQRLV 342
Cdd:TIGR01070 233 ALPHLQPVRLY------------------ELQDFMQLDAATRRNLELTEnlrGGKQNT-----LFSVLDETKTAMGSRLL 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    343 NQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQeDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALE 422
Cdd:TIGR01070 290 KRWLHRPLRDREVLEARQDTVEVLLRHFFLREGLR-PLLKEVGDLERLAARVALGNARPRDLARLRTSLEQLPELRALLE 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    423 KYEGRHqalllavfVTPLIDLRSDFSKFQEMIETTLdmdqVENHEFLV------KPSFDPNLSELREVMDG-------LE 489
Cdd:TIGR01070 369 ELEGPT--------LQALAAQIDDFSELLELLEAAL----IENPPLVVrdggliREGYDEELDELRAASREgtdylarLE 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    490 KK-MQSTlinaarglGLDpgkQIKLDSSAQFGYYFRVT-CKEEKVlrnNKNFSTVDIQKNGVKFTNSELSSLNEEYTKNK 567
Cdd:TIGR01070 437 AReRERT--------GIP---TLKVGYNAVFGYYIEVTrGQLHLV---PAHYRRRQTLKNAERYITPELKEKEDKVLEAE 502
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    568 GEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAHLDAIVSFAHVsnAAPVPYVRPVILEKGKGRIilKASRHACVEVQDE 647
Cdd:TIGR01070 503 GKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAEV--AETLHYTRPRFGDDPQLRI--REGRHPVVEQVLR 578
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    648 VAFIPNDVHFEKDKQMFhIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMA 727
Cdd:TIGR01070 579 TPFVPNDLEMAHNRRML-LITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMV 657
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    728 EMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTT 807
Cdd:TIGR01070 658 EMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRAKTLFATHYFELTALEESLPGLKNVHVAALEH 737
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    808 EETLTMLYQVKKGVCDQSFGIHVAELANFPRHVIACAKQKALELEEFQNIGTSLGCDEAEPAAKRRCLEREQGEKIILEF 887
Cdd:TIGR01070 738 NGTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEARSTESEAPQRKAQTSAPEQISLFDEAETHPLLEE 817
                         890       900
                  ....*....|....*....|...
gi 6678938    888 LSKVKQVPFTAMSEESISAKLKQ 910
Cdd:TIGR01070 818 LAKLDPDDLTPLQALNLLYELKK 840
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
665-852 3.91e-111

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: 339.55  E-value: 3.91e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    665 HIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSL 744
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    745 IIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQ 824
Cdd:pfam00488  81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAADK 160
                         170       180
                  ....*....|....*....|....*...
gi 6678938    825 SFGIHVAELANFPRHVIACAKQKALELE 852
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERAREILAELE 188
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
664-848 4.52e-104

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 321.04  E-value: 4.52e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     664 FHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDS 743
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     744 LIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCD 823
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVAG 160
                          170       180
                   ....*....|....*....|....*
gi 6678938     824 QSFGIHVAELANFPRHVIACAKQKA 848
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
MutS_I pfam01624
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ...
18-132 2.50e-29

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: 112.68  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     18 GFVRFFEGMPEKPSTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYmgpAGSKTLQSVVLSKMNFESFVKDLLLvRQ 97
Cdd:pfam01624   2 PMMRQYLELKSKYPDAVLFFRVGDFYELFGEDAEIAARELGITLTVRKG---GSGKRIPMAGVPEHAFERYARRLVN-KG 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 6678938     98 YRVEVYKNKAGNKASK-ENEWYLAFKASPGNLSQFE 132
Cdd:pfam01624  78 YKVAICEQTETPAEAKgVVKREVVRVVTPGTLTDDE 113
 
Name Accession Description Interval E-value
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
152-853 7.49e-162

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 495.74  E-value: 7.49e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  152 MAVVDGQRHVGVGYVD-STQRkLGLCEFPENDQfsnLEALLIQIGPKECVLPggETTGDMGKLRQVIQRGGILITERKRA 230
Cdd:COG0249 131 AAVARDKGRYGLAWLDiSTGE-FLVTELDGEEA---LLDELARLAPAEILVP--EDLPDPEELLELLRERGAAVTRLPDW 204
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  231 DFSTKDIYQDLNRLLKGKkgeqiNSAALPEMENQVAVSSLSAVIKFLEllsdDSNFGQFE----LATFDFSQYMKLDMAA 306
Cdd:COG0249 205 AFDPDAARRRLLEQFGVA-----SLDGFGLEDLPAAIAAAGALLAYLE----ETQKGALPhlrrLRRYEEDDYLILDAAT 275
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  307 VRALNLFQGSVEDTTGSqsLAALLNKCKTAQGQRLVNQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQEdLLRRFPD 386
Cdd:COG0249 276 RRNLELTETLRGGRKGS--LLSVLDRTVTAMGSRLLRRWLLRPLRDRAAIEARLDAVEELLEDPLLREELRE-LLKGVYD 352
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  387 LNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALEKYEGRHQALLLAVFvTPLIDLRsdfskfqEMIETTLdmdqVENH 466
Cdd:COG0249 353 LERLLSRIALGRANPRDLAALRDSLAALPELKELLAELDSPLLAELAEAL-DPLEDLA-------ELLERAI----VDEP 420
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  467 EFLV------KPSFDPNLSELREVMDG-------LEKKMQ-----STLinaarglgldpgkqiKLDSSAQFGYYFRVTck 528
Cdd:COG0249 421 PLLIrdggviREGYDAELDELRELSENgkewlaeLEARERertgiKSL---------------KVGYNKVFGYYIEVT-- 483
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  529 eekvlrnNKNFSTVD-----IQ--KNGVKFTNSELSslneeytknkgEYEE----AQDAIV-------KEIVNISSGYVE 590
Cdd:COG0249 484 -------KANADKVPddyirKQtlKNAERYITPELK-----------ELEDkilsAEERALaleyelfEELREEVAAHIE 545
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  591 PMQTLNDVLAHLDAIVSFAHVS---NaapvpYVRPVILEKGkgRIILKASRHACVE-VQDEVAFIPNDVHFEKDKQMfHI 666
Cdd:COG0249 546 RLQALARALAELDVLASLAEVAvenN-----YVRPELDDSP--GIEIEGGRHPVVEqALPGEPFVPNDCDLDPDRRI-LL 617
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  667 ITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLII 746
Cdd:COG0249 618 ITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRVGASDDLARGQSTFMVEMTETANILNNATERSLVL 697
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  747 IDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSF 826
Cdd:COG0249 698 LDEIGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELTELAEKLPGVKNYHVAVKEWGGDIVFLHKVVPGPADRSY 777
                       730       740
                ....*....|....*....|....*..
gi 6678938  827 GIHVAELANFPRHVIACAKQKALELEE 853
Cdd:COG0249 778 GIHVAKLAGLPASVIERAREILAELEK 804
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
152-853 3.82e-159

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 488.84  E-value: 3.82e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   152 MAVVDGQRHVGVGYVDSTQRKLGLCEFPENDqfsnLEALLIQIGPKECVLPGGETTGDMGKLRQVIQRggiliteRKRAD 231
Cdd:PRK05399 132 AAIAQDGGGYGLAYLDLSTGEFRVTELDEEE----LLAELARLNPAEILVPEDFSEDELLLLRRGLRR-------RPPWE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   232 FSTKDIYQDLNRLLKGK--KGEQINSAAlpemenqvAVSSLSAVIKFLEllsdDSNFGQFE----LATFDFSQYMKLDMA 305
Cdd:PRK05399 201 FDLDTAEKRLLEQFGVAslDGFGVDLPL--------AIRAAGALLQYLK----ETQKRSLPhlrsPKRYEESDYLILDAA 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   306 AVRALNLFQgSVEDTTgSQSLAALLNKCKTAQGQRLVNQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQEdLLRRFP 385
Cdd:PRK05399 269 TRRNLELTE-NLRGGR-KNSLLSVLDRTVTAMGGRLLRRWLHRPLRDREAIEARLDAVEELLEDPLLREDLRE-LLKGVY 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   386 DLNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALEKyegrHQALLLAVFVTPLidlrSDFSKFQEMIETTLdmdqVEN 465
Cdd:PRK05399 346 DLERLLSRIALGRANPRDLAALRDSLEALPELKELLAE----LDSPLLAELAEQL----DPLEELADLLERAI----VEE 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   466 HEFLV------KPSFDPNLSELREVMDG-------LEKK-MQSTLINAarglgldpgkqIKLDSSAQFGYYFRVTckeek 531
Cdd:PRK05399 414 PPLLIrdggviADGYDAELDELRALSDNgkdwlaeLEAReRERTGISS-----------LKVGYNKVFGYYIEVT----- 477
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   532 vlrnNKNFSTVD-----IQ--KNGVKFTNSELSslneeytknkgEYEE----AQDAIV-------KEIVNISSGYVEPMQ 593
Cdd:PRK05399 478 ----KANLDKVPedyirRQtlKNAERYITPELK-----------ELEDkilsAEEKALaleyelfEELREEVAEHIERLQ 542
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   594 TLNDVLAHLDAIVSFAHVS---NaapvpYVRPVILEKGkgRIILKASRHACVE-VQDEVAFIPNDVHFEKDKQMfHIITG 669
Cdd:PRK05399 543 KLAKALAELDVLASLAEVAeenN-----YVRPEFTDDP--GIDIEEGRHPVVEqVLGGEPFVPNDCDLDEERRL-LLITG 614
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   670 PNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDE 749
Cdd:PRK05399 615 PNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDE 694
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   750 LGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIH 829
Cdd:PRK05399 695 IGRGTSTYDGLSIAWAVAEYLHDKIGAKTLFATHYHELTELEEKLPGVKNVHVAVKEHGGDIVFLHKVVPGAADKSYGIH 774
                        730       740
                 ....*....|....*....|....
gi 6678938   830 VAELANFPRHVIACAKQKALELEE 853
Cdd:PRK05399 775 VAKLAGLPASVIKRAREILAQLES 798
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
633-852 1.79e-149

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: 440.66  E-value: 1.79e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  633 ILKASRHACVEVQDEVAFIPNDVHFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARV 712
Cdd:cd03285   1 VLKEARHPCVEAQDDVAFIPNDVTLTRGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILARV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  713 GAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALAN 792
Cdd:cd03285  81 GASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQIKCFCLFATHFHELTALAD 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678938  793 QIPTVNNLHV--TALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPRHVIACAKQKALELE 852
Cdd:cd03285 161 EVPNVKNLHVtaLTDDASRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQKALELE 222
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
36-910 1.43e-131

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


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 416.09  E-value: 1.43e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     36 LFDRGDFYTAHGEDALLAAREVFKTqgVIKYMGPAGsktlQSVVLSKMNFESFVK--DLLLVRQYRVEVYKNKAGNKASK 113
Cdd:TIGR01070  21 FFRMGDFYELFYEDAKKAAQLLDIS--LTSRGQSAD----EPIPMAGIPYHAVEAylEKLVKQGESVAICEQIEDPKTAK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    114 ---ENEwyLAFKASPGNLSQFEDILFGNNDMSAsvgvmgikmAVVDGQRHVGVGYVDSTQRKLGLCEFPEndqFSNLEAL 190
Cdd:TIGR01070  95 gpvERE--VVQLITPGTVSDEALLPERQDNLLA---------AIAQESNGFGLATLDLTTGEFKVTELAD---KETLYAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    191 LIQIGPKECVLPGGETTGDMGKLRQVIQRGGILITERKradFSTKDIyqdlnRLLKGKKGEQINSAALPEM----ENQ-V 265
Cdd:TIGR01070 161 LQRLNPAEVLLAEDLSEMEAIELREFRKDTAVMSLEAQ---FGTEDL-----GGLGLRNAPLGLTAAGCLLqyakRTQrT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    266 AVSSLSAVIKFlellsddsnfgqfelatfDFSQYMKLDMAAVRALNLFQ---GSVEDTtgsqsLAALLNKCKTAQGQRLV 342
Cdd:TIGR01070 233 ALPHLQPVRLY------------------ELQDFMQLDAATRRNLELTEnlrGGKQNT-----LFSVLDETKTAMGSRLL 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    343 NQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQeDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALE 422
Cdd:TIGR01070 290 KRWLHRPLRDREVLEARQDTVEVLLRHFFLREGLR-PLLKEVGDLERLAARVALGNARPRDLARLRTSLEQLPELRALLE 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    423 KYEGRHqalllavfVTPLIDLRSDFSKFQEMIETTLdmdqVENHEFLV------KPSFDPNLSELREVMDG-------LE 489
Cdd:TIGR01070 369 ELEGPT--------LQALAAQIDDFSELLELLEAAL----IENPPLVVrdggliREGYDEELDELRAASREgtdylarLE 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    490 KK-MQSTlinaarglGLDpgkQIKLDSSAQFGYYFRVT-CKEEKVlrnNKNFSTVDIQKNGVKFTNSELSSLNEEYTKNK 567
Cdd:TIGR01070 437 AReRERT--------GIP---TLKVGYNAVFGYYIEVTrGQLHLV---PAHYRRRQTLKNAERYITPELKEKEDKVLEAE 502
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    568 GEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAHLDAIVSFAHVsnAAPVPYVRPVILEKGKGRIilKASRHACVEVQDE 647
Cdd:TIGR01070 503 GKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAEV--AETLHYTRPRFGDDPQLRI--REGRHPVVEQVLR 578
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    648 VAFIPNDVHFEKDKQMFhIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMA 727
Cdd:TIGR01070 579 TPFVPNDLEMAHNRRML-LITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASDDLASGRSTFMV 657
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    728 EMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTT 807
Cdd:TIGR01070 658 EMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRAKTLFATHYFELTALEESLPGLKNVHVAALEH 737
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    808 EETLTMLYQVKKGVCDQSFGIHVAELANFPRHVIACAKQKALELEEFQNIGTSLGCDEAEPAAKRRCLEREQGEKIILEF 887
Cdd:TIGR01070 738 NGTIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEARSTESEAPQRKAQTSAPEQISLFDEAETHPLLEE 817
                         890       900
                  ....*....|....*....|...
gi 6678938    888 LSKVKQVPFTAMSEESISAKLKQ 910
Cdd:TIGR01070 818 LAKLDPDDLTPLQALNLLYELKK 840
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
665-852 3.91e-111

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: 339.55  E-value: 3.91e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    665 HIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSL 744
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    745 IIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQ 824
Cdd:pfam00488  81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAADK 160
                         170       180
                  ....*....|....*....|....*...
gi 6678938    825 SFGIHVAELANFPRHVIACAKQKALELE 852
Cdd:pfam00488 161 SYGIHVAELAGLPESVVERAREILAELE 188
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
664-848 4.52e-104

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 321.04  E-value: 4.52e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     664 FHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDS 743
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     744 LIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCD 823
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVAG 160
                          170       180
                   ....*....|....*....|....*
gi 6678938     824 QSFGIHVAELANFPRHVIACAKQKA 848
Cdd:smart00534 161 KSYGIEVAKLAGLPKEVIERAKRIL 185
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
323-645 2.53e-99

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 313.47  E-value: 2.53e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     323 SQSLAALLNKCKTAQGQRLVNQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQEdLLRRFPDLNRLAKKFQRQAANLQ 402
Cdd:smart00533   1 KGSLFELLNHTKTPMGKRLLRRWLLQPLLDLKEINERLDAVEELVENPELRQKLRQ-LLKRIPDLERLLSRIERGRASPR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     403 DCYRLYQGINQLPSVIQALEKYEGRHQALLLAVFVTPLIdlrsdfSKFQEMIETTLDMDQVE-NHEFLVKPSFDPNLSEL 481
Cdd:smart00533  80 DLLRLYDSLEGLKEIRQLLESLDGPLLGLLLKVILEPLL------ELLELLLELLNDDDPLEvNDGGLIKDGFDPELDEL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     482 REVMDGLEKKMQSTLINAARGLGLDpgkQIKLDSSAQFGYYFRVTCKEEKVLRnnKNFSTVDIQKNGVKFTNSELSSLNE 561
Cdd:smart00533 154 REKLEELEEELEELLKKEREELGID---SLKLGYNKVHGYYIEVTKSEAKKVP--KDFIRRSSLKNTERFTTPELKELEN 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     562 EYTKNKGEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAHLDAIVSFAHVsnAAPVPYVRPVILEkgKGRIILKASRHAC 641
Cdd:smart00533 229 ELLEAKEEIERLEKEILRELLEKVLEYLEELRALAEALAELDVLLSLATL--AAEGNYVRPEFVD--SGELEIKNGRHPV 304

                   ....
gi 6678938     642 VEVQ 645
Cdd:smart00533 305 LELQ 308
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
633-846 2.80e-96

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: 301.49  E-value: 2.80e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  633 ILKASRHACVE-VQDEVAFIPNDVHFEKDKQMfHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILAR 711
Cdd:cd03284   1 EIEGGRHPVVEqVLDNEPFVPNDTELDPERQI-LLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  712 VGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALA 791
Cdd:cd03284  80 IGASDDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELTELE 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6678938  792 NQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPRHVIACAKQ 846
Cdd:cd03284 160 GKLPRVKNFHVAVKEKGGGVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERARE 214
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
634-836 5.59e-80

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: 257.56  E-value: 5.59e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  634 LKASRHACVEVQ-DEVAFIPNDVHFEKDKqmFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARV 712
Cdd:cd03243   2 IKGGRHPVLLALtKGETFVPNDINLGSGR--LLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  713 GAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKiGAFCMFATHFHELTALAN 792
Cdd:cd03243  80 GAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEK-GCRTLFATHFHELADLPE 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 6678938  793 QIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANF 836
Cdd:cd03243 159 QVPGVKNLHMEELITTGGLTFTYKLIDGICDPSYALQIAELAGL 202
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
632-844 4.49e-69

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: 228.91  E-value: 4.49e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  632 IILKASRHACVEVQDEVAFIPNDVHFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILAR 711
Cdd:cd03287   1 ILIKEGRHPMIESLLDKSFVPNDIHLSAEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVLTR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  712 VGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALA 791
Cdd:cd03287  81 MGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEKKCLVLFVTHYPSLGEIL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678938  792 NQIP-TVNNLHV--------TALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPRHVIACA 844
Cdd:cd03287 161 RRFEgSIRNYHMsylesqkdFETSDSQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
633-844 7.25e-63

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: 211.90  E-value: 7.25e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  633 ILKASRHACVEVQDEVAFIPNDVHFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARV 712
Cdd:cd03286   1 CFEELRHPCLNASTASSFVPNDVDLGATSPRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFTRI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  713 GAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKIGAFCMFATHFHELTALAN 792
Cdd:cd03286  81 GARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKCLTLFSTHYHSLCDEFH 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6678938  793 QIPTVNNLHV------TALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPRHVIACA 844
Cdd:cd03286 161 EHGGVRLGHMacavknESDPTIRDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
637-801 1.40e-51

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: 179.89  E-value: 1.40e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  637 SRHACVEVQDEVaFIPNDVHFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGD 716
Cdd:cd03282   5 SRHPILDRDKKN-FIPNDIYLTRGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLSRLSNDD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  717 SQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIaTKIGAFCMFATHFHELTALANQIPT 796
Cdd:cd03282  84 SMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECL-IKKESTVFFATHFRDIAAILGNKSC 162

                ....*
gi 6678938  797 VNNLH 801
Cdd:cd03282 163 VVHLH 167
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
633-834 1.90e-50

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: 176.72  E-value: 1.90e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  633 ILKASRHACVEvQDEVAFIPNDVHFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARV 712
Cdd:cd03281   1 EIQGGRHPLLE-LFVDSFVPNDTEIGGGGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFTRM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  713 GAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATKiGAFC---MFATHFHELTa 789
Cdd:cd03281  80 SSRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKR-GPECprvIVSTHFHELF- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6678938  790 laNQIPTVNNLHVT-----------ALTTEETLTMLYQVKKGVCDQSFGIHVAELA 834
Cdd:cd03281 158 --NRSLLPERLKIKfltmevllnptSTSPNEDITYLYRLVPGLADTSFAIHCAKLA 211
MutS_III pfam05192
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair ...
305-609 3.60e-49

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: 176.06  E-value: 3.60e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    305 AAVRALNLFQGSveDTTGSQSLAALLNKCKTAQGQRLVNQWIKQPLMDRNRIEERLNLVEAFVEDSELRQSLQEdLLRRF 384
Cdd:pfam05192   1 ATLRNLELTENL--RGGKEGSLLGLLDRTKTPMGSRLLRQWLLQPLTDLEEINERLDAVEELLENSELREDLRE-LLRRL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    385 PDLNRLAKKFQRQAANLQDCYRLYQGINQLPSVIQALEKYEgrhqalllavfvtplIDLRSDFSKFQEMIETTLDMDQVE 464
Cdd:pfam05192  78 PDLERLLSRIALGKATPRDLLALLDSLEKLPLLKELLLEEK---------------SALLGELASLAELLEEAIDEEPPA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    465 NHEFLVKPSFDPNLsELREVMDGLEKKMQSTLINAARGLGLDPGKQIKLDSSAQFGYYFRVTC-----KEEKVLRNNKNF 539
Cdd:pfam05192 143 LLRDGGVIRDGYDE-ELDELRDLLLDGKRLLAKLEARERERTGIKSLKVLYNKVFGYYLLLVEyyievSKSQKDKVPDDY 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    540 STVDIQKNGVKFTNSELSSLNEEYTKNKGEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAHLDAIVSFA 609
Cdd:pfam05192 222 IRIQTTKNAERYITPELKELERKILQAEERLLALEKELFEELLEEVLEYIEVLRRAAEALAELDVLLSLA 291
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
326-793 3.16e-32

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 134.88  E-value: 3.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  326 LAALLNKCKTAQGQRLVNQWikQPLMDRNRIEERLNLVEAFVEDSELRQSLQedlLRRFPDLNRLAKKFQRQAA-NLQDC 404
Cdd:COG1193  15 LELLAEYAVSELGKELARKL--RPSTDLEEVERLLAETAEARRLLRLEGGLP---LGGIPDIRPLLKRAEEGGVlSPEEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  405 YRLYQGINQLPSVIQALEKYEGRHQALllavfvTPLIDLRSDFSKFQEMIETTLDmdqvENHEflVKPSFDPNLSELREV 484
Cdd:COG1193  90 LDIARTLRAARRLKRFLEELEEEYPAL------KELAERLPPLPELEKEIDRAID----EDGE--VKDSASPELRRIRRE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  485 MDGLEKKMQStlinaarglgldpgkqiKLDS---SAQFGYYFR---VTCKEEK----VLRNNKN---------------- 538
Cdd:COG1193 158 IRSLEQRIRE-----------------KLESilrSASYQKYLQdaiITIRNGRyvipVKAEYKGkipgivhdqsasgqtl 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  539 ----FSTVDIqkngvkftNSELSSLneeytknkgEYEEAQ--DAIVKEIVNISSGYVEPMQTLNDVLAHLD---AIVSFA 609
Cdd:COG1193 221 fiepMAVVEL--------NNELREL---------EAEERReiERILRELSALVREYAEELLENLEILAELDfifAKARYA 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  610 HVSNAapvpyVRPVILEKGkgRIILKASRHACVeVQDEVafIPNDVHFEKDKQMFhIITGPNMGGKSTYIRQTGVIVLMA 689
Cdd:COG1193 284 LELKA-----VKPELNDEG--YIKLKKARHPLL-DLKKV--VPIDIELGEDFRTL-VITGPNTGGKTVTLKTVGLLTLMA 352
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  690 QIGCFVPC-ESAEVSIVDCILARVGagDSQ-----LkgvSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLA 763
Cdd:COG1193 353 QSGLPIPAaEGSELPVFDNIFADIG--DEQsieqsL---STFSSHMTNIVEILEKADENSLVLLDELGAGTDPQEGAALA 427
                       490       500       510
                ....*....|....*....|....*....|
gi 6678938  764 WAISDYIATKiGAFCMFATHFHELTALANQ 793
Cdd:COG1193 428 IAILEELLER-GARVVATTHYSELKAYAYN 456
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
634-832 1.33e-30

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: 119.66  E-value: 1.33e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  634 LKASRHACVEVQDEvAFIPNDVHFEKDKQMFhIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPC-ESAEVSIVDCILARV 712
Cdd:cd03280   2 LREARHPLLPLQGE-KVVPLDIQLGENKRVL-VITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAaEGSSLPVFENIFADI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  713 GAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIAtKIGAFCMFATHFHELTALAN 792
Cdd:cd03280  80 GDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELL-ERGALVIATTHYGELKAYAY 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6678938  793 QIPTVNNLHVTALTTEETLtmLYQVKKGVCDQSFGIHVAE 832
Cdd:cd03280 159 KREGVENASMEFDPETLKP--TYRLLIGVPGRSNALEIAR 196
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
647-794 3.49e-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: 117.08  E-value: 3.49e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  647 EVAFIPNDVHFekDKQMFHIITGPNMGGKSTYIRQTGVIVLMA----------QIGCFVPCESAEVSIVdcilarvgagd 716
Cdd:cd03227   8 PSYFVPNDVTF--GEGSLTIITGPNGSGKSTILDAIGLALGGAqsatrrrsgvKAGCIVAAVSAELIFT----------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  717 sqLKGVSTFMAEMLETASILRSATK--DSLIIIDELGRGTSTYDGFGLAWAISDYiaTKIGAFCMFATHFHELTALANQI 794
Cdd:cd03227  75 --RLQLSGGEKELSALALILALASLkpRPLYILDEIDRGLDPRDGQALAEAILEH--LVKGAQVIVITHLPELAELADKL 150
MutS_I pfam01624
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ...
18-132 2.50e-29

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: 112.68  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938     18 GFVRFFEGMPEKPSTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYmgpAGSKTLQSVVLSKMNFESFVKDLLLvRQ 97
Cdd:pfam01624   2 PMMRQYLELKSKYPDAVLFFRVGDFYELFGEDAEIAARELGITLTVRKG---GSGKRIPMAGVPEHAFERYARRLVN-KG 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 6678938     98 YRVEVYKNKAGNKASK-ENEWYLAFKASPGNLSQFE 132
Cdd:pfam01624  78 YKVAICEQTETPAEAKgVVKREVVRVVTPGTLTDDE 113
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
634-834 6.45e-28

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: 112.01  E-value: 6.45e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  634 LKASRHACVEVQDEVAfipNDVHFEKDKQMfhIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDcILARVG 713
Cdd:cd03283   2 AKNLGHPLIGREKRVA---NDIDMEKKNGI--LITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVK-IFTSIR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  714 AGDSQLKGVSTFMAEMLETASILRSATKD--SLIIIDELGRGTSTYDGFGLAWAISDYIATKiGAFCMFATHFHELTALA 791
Cdd:cd03283  76 VSDDLRDGISYFYAELRRLKEIVEKAKKGepVLFLLDEIFKGTNSRERQAASAAVLKFLKNK-NTIGIISTHDLELADLL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6678938  792 NQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELA 834
Cdd:cd03283 155 DLDSAVRNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKI 197
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
553-802 8.10e-26

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 114.54  E-value: 8.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   553 NSELSSLneeytKNKGEYEEaqDAIVKEIVNISSGYVEPMQTLNDVLAHLDAIvsFAHVSNAAPVPYVRPviLEKGKGRI 632
Cdd:PRK00409 233 NNEIREL-----RNKEEQEI--ERILKELSAKVAKNLDFLKFLNKIFDELDFI--FARARYAKALKATFP--LFNDEGKI 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   633 ILKASRHACVeVQDEVafIPNDVHFEKDKQMFhIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPC-ESAEVSIVDCILAR 711
Cdd:PRK00409 302 DLRQARHPLL-DGEKV--VPKDISLGFDKTVL-VITGPNTGGKTVTLKTLGLAALMAKSGLPIPAnEPSEIPVFKEIFAD 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938   712 VgaGDSQ-LK-GVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIAtKIGAFCMFATHFHELTA 789
Cdd:PRK00409 378 I--GDEQsIEqSLSTFSGHMTNIVRILEKADKNSLVLFDELGAGTDPDEGAALAISILEYLR-KRGAKIIATTHYKELKA 454
                        250
                 ....*....|...
gi 6678938   790 LANQIPTVNNLHV 802
Cdd:PRK00409 455 LMYNREGVENASV 467
mutS2 TIGR01069
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ...
559-931 3.35e-24

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: 109.14  E-value: 3.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    559 LNEEYTKNKGEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAHLDAIvsFAHVSNAAPVPYVRPVILEKGKgrIILKASR 638
Cdd:TIGR01069 227 LNNKLAQLKNEEECEIEKILRTLSEKVQEYLLELKFLFKEFDFLDSL--QARARYAKAVKGEFPMPSFTGK--IILENAR 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    639 HAcveVQDEVAFIPNDVHFEKDKQMFhIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPC-ESAEVSIVDCILARVGAGDS 717
Cdd:TIGR01069 303 HP---LLKEPKVVPFTLNLKFEKRVL-AITGPNTGGKTVTLKTLGLLALMFQSGIPIPAnEHSEIPYFEEIFADIGDEQS 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    718 QLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISDYIAtKIGAFCMFATHFHELTALANQIPTV 797
Cdd:TIGR01069 379 IEQNLSTFSGHMKNISAILSKTTENSLVLFDELGAGTDPDEGSALAISILEYLL-KQNAQVLITTHYKELKALMYNNEGV 457
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    798 NNLHVTALTTEETLtmLYQVKKGVCDQSFGIHVAELANFPRHVIACAKQKALEL-EEFQNIGTSLgcdeaEPAAKRRCLE 876
Cdd:TIGR01069 458 ENASVLFDEETLSP--TYKLLKGIPGESYAFEIAQRYGIPHFIIEQAKTFYGEFkEEINVLIEKL-----SALEKELEQK 530
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6678938    877 REQGEKIILEFLSKVKQVPFTAMSEESISAKLK----QLKAEVVAKNNSFVNEIISRIK 931
Cdd:TIGR01069 531 NEHLEKLLKEQEKLKKELEQEMEELKERERNKKleleKEAQEALKALKKEVESIIRELK 589
MutS_IV pfam05190
MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch ...
473-569 1.59e-19

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: 84.20  E-value: 1.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    473 SFDPNLSELREVMDGLEKKMQSTLINAARGLGLdpgKQIKLDSSAQFGYYFRVTCKEEKVLRnnKNFSTVDIQKNGVKFT 552
Cdd:pfam05190   1 GFDEELDELRDLLDELEKELEELEKKEREKLGI---KSLKVGYNKVFGYYIEVTRSEAKKVP--SNYIRRQTLKNGVRFT 75
                          90
                  ....*....|....*..
gi 6678938    553 NSELSSLNEEYTKNKGE 569
Cdd:pfam05190  76 TPELKKLEDELLEAEEE 92
MutS_II pfam05188
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair ...
152-284 3.15e-19

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: 84.71  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938    152 MAVVDG-QRHVGVGYVDSTQRKLGLCEFPEndqFSNLEALLIQIGPKECVLPGGETTGDMGKLrQVIQRGGILITERKRA 230
Cdd:pfam05188   4 AAISRGdGNRYGLAFLDLSTGEFGVSEFED---FEELLAELSRLSPKELLLPESLSSSTVAES-QKLLELRLRVGRRPTW 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6678938    231 DFSTKDIYQDLNRLLKGKKGEQINSaalpeMENQVAVSSLSAVIKFLELLSDDS 284
Cdd:pfam05188  80 LFELEHAYEDLNEDFGVEDLDGFGL-----EELPLALCAAGALISYLKETQKEN 128
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
638-793 3.97e-09

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 56.48  E-value: 3.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678938  638 RHACVEVQDEVAFIPNDVHFEKDKqmFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAgDS 717
Cdd:cd00267   3 ENLSFRYGGRTALDNVSLTLKAGE--IVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY-VP 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678938  718 QLkgvSTFMAEMLETASILrsATKDSLIIIDELGRGTSTYDGFGLAWAISDYIATkiGAFCMFATHFHELTALANQ 793
Cdd:cd00267  80 QL---SGGQRQRVALARAL--LLNPDLLLLDEPTSGLDPASRERLLELLRELAEE--GRTVIIVTHDPELAELAAD 148
 
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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