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Conserved domains on  [gi|502729652|ref|WP_012964636|]
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DNA mismatch repair protein MutS [Ferroglobus placidus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 349-526 8.00e-37

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member smart00534:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 185  Bit Score: 134.61  E-value: 8.00e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652   349 ILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELFFFKRKKMSYGSG--AFENTIKSFARAISSKG-RKLI 425
Cdd:smart00534   3 IITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGlsTFMVEMKETANILKNATkNSLV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652   426 LVDEFEAITEPGAAVKILKKILE-LIHSAGDYAIVVSHLGeELSKL--DFVRVDGIEAVGLDENFRLIVNRQPIFGKIGR 502
Cdd:smart00534  83 LLDELGRGTSTYDGLAIAAAILEyLLEKIGARTLFATHYH-ELTKLadNHPGVRNLHMSALEETENITFLYKLKPGVAGK 161

                          170       180
                   ....*....|....*....|....
gi 502729652   503 StPELIVEKLRrtskGREKEVYEK 526
Cdd:smart00534 162 S-YGIEVAKLA----GLPKEVIER 180
 
Name Accession Description Interval E-value
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
349-526 8.00e-37

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 134.61  E-value: 8.00e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652   349 ILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELFFFKRKKMSYGSG--AFENTIKSFARAISSKG-RKLI 425
Cdd:smart00534   3 IITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGlsTFMVEMKETANILKNATkNSLV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652   426 LVDEFEAITEPGAAVKILKKILE-LIHSAGDYAIVVSHLGeELSKL--DFVRVDGIEAVGLDENFRLIVNRQPIFGKIGR 502
Cdd:smart00534  83 LLDELGRGTSTYDGLAIAAAILEyLLEKIGARTLFATHYH-ELTKLadNHPGVRNLHMSALEETENITFLYKLKPGVAGK 161

                          170       180
                   ....*....|....*....|....
gi 502729652   503 StPELIVEKLRrtskGREKEVYEK 526
Cdd:smart00534 162 S-YGIEVAKLA----GLPKEVIER 180
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
 333-475 5.50e-23

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: 96.55  E-value: 5.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 333 NPQPIDYYLDErNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF--FFKRKKMSYGSGAFENTI 410
Cdd:cd03243   18 TFVPNDINLGS-GRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFtrIGAEDSISDGRSTFMAEL 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502729652 411 KSFARAIS-SKGRKLILVDEFEAITEPGAAVKILKKILELIHSAGDYAIVVSHLGEELSKLDFVRV 475
Cdd:cd03243   97 LELKEILSlATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQVPG 162
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
255-465 2.49e-10

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 63.24  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 255 IEVNEEkLRELKkkLEERHAIdfyfacRRIvekydLKGLNEKIKKYRS--LALYKVLQ--DFAF-------------PEI 317
Cdd:COG1193  228 VELNNE-LRELE--AEERREI------ERI-----LRELSALVREYAEelLENLEILAelDFIFakaryalelkavkPEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 318 GEG--LRIFKGKN--LFIDNPQPIDYYLDERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNA-ERAEVRVFDELF 392
Cdd:COG1193  294 NDEgyIKLKKARHplLDLKKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAaEGSELPVFDNIF 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 393 ---------------FfkrkkmsygSGAFENtIKSFARAISSkgRKLILVDEFEAITEP--GAAVKIlkKILELIHSAGD 455
Cdd:COG1193  374 adigdeqsieqslstF---------SSHMTN-IVEILEKADE--NSLVLLDELGAGTDPqeGAALAI--AILEELLERGA 439

                        250
                 ....*....|
gi 502729652 456 YAIVVSHLGE 465
Cdd:COG1193  440 RVVATTHYSE 449
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 330-392 2.09e-08

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 57.03  E-value: 2.09e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502729652 330 FIDNpqpiDYYLDERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:PRK05399 596 FVPN----DCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIF 654
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 349-392 1.20e-07

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: 51.81  E-value: 1.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 502729652  349 ILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:pfam00488   2 IITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIF 45
 
Name Accession Description Interval E-value
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
349-526 8.00e-37

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 134.61  E-value: 8.00e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652   349 ILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELFFFKRKKMSYGSG--AFENTIKSFARAISSKG-RKLI 425
Cdd:smart00534   3 IITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGlsTFMVEMKETANILKNATkNSLV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652   426 LVDEFEAITEPGAAVKILKKILE-LIHSAGDYAIVVSHLGeELSKL--DFVRVDGIEAVGLDENFRLIVNRQPIFGKIGR 502
Cdd:smart00534  83 LLDELGRGTSTYDGLAIAAAILEyLLEKIGARTLFATHYH-ELTKLadNHPGVRNLHMSALEETENITFLYKLKPGVAGK 161

                          170       180
                   ....*....|....*....|....
gi 502729652   503 StPELIVEKLRrtskGREKEVYEK 526
Cdd:smart00534 162 S-YGIEVAKLA----GLPKEVIER 180
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
 333-475 5.50e-23

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: 96.55  E-value: 5.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 333 NPQPIDYYLDErNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF--FFKRKKMSYGSGAFENTI 410
Cdd:cd03243   18 TFVPNDINLGS-GRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFtrIGAEDSISDGRSTFMAEL 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502729652 411 KSFARAIS-SKGRKLILVDEFEAITEPGAAVKILKKILELIHSAGDYAIVVSHLGEELSKLDFVRV 475
Cdd:cd03243   97 LELKEILSlATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQVPG 162
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
 332-465 2.07e-15

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: 74.98  E-value: 2.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 332 DNPQPIDYYLDERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNA-ERAEVRVFDELFFF--KRKKMSYGSGAFEN 408
Cdd:cd03280   15 EKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAaEGSSLPVFENIFADigDEQSIEQSLSTFSS 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 409 TIKSFARAISSKGRK-LILVDEFEAITEP--GAAVKIlkKILELIHSAGDYAIVVSHLGE 465
Cdd:cd03280   95 HMKNIARILQHADPDsLVLLDELGSGTDPveGAALAI--AILEELLERGALVIATTHYGE 152
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
 329-440 1.12e-14

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: 73.10  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 329 LFIDNPQPIDYYLDERN-RIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF--FFKRKKMSYGSGA 405
Cdd:cd03281   12 LFVDSFVPNDTEIGGGGpSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFtrMSSRESVSSGQSA 91

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 502729652 406 FENTIKSFARAIS-SKGRKLILVDEF--EAITEPGAAV 440
Cdd:cd03281   92 FMIDLYQVSKALRlATRRSLVLIDEFgkGTDTEDGAGL 129
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
 329-465 1.48e-11

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: 63.95  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 329 LFIDNPQPI-----------DYYLD-ERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF--FF 394
Cdd:cd03282    1 IIRDSRHPIldrdkknfipnDIYLTrGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLsrLS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502729652 395 KRKKMSYGSGAFENTIKSFARAIS-SKGRKLILVDEFEAITEPGAAVKILKKILELIHSAGDYAIVVSHLGE 465
Cdd:cd03282   81 NDDSMERNLSTFASEMSETAYILDyADGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRD 152
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
 336-392 9.72e-11

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: 61.67  E-value: 9.72e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502729652 336 PIDYYLDERN-RIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:cd03286   20 PNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIF 77
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
255-465 2.49e-10

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 63.24  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 255 IEVNEEkLRELKkkLEERHAIdfyfacRRIvekydLKGLNEKIKKYRS--LALYKVLQ--DFAF-------------PEI 317
Cdd:COG1193  228 VELNNE-LRELE--AEERREI------ERI-----LRELSALVREYAEelLENLEILAelDFIFakaryalelkavkPEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 318 GEG--LRIFKGKN--LFIDNPQPIDYYLDERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNA-ERAEVRVFDELF 392
Cdd:COG1193  294 NDEgyIKLKKARHplLDLKKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAaEGSELPVFDNIF 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 393 ---------------FfkrkkmsygSGAFENtIKSFARAISSkgRKLILVDEFEAITEP--GAAVKIlkKILELIHSAGD 455
Cdd:COG1193  374 adigdeqsieqslstF---------SSHMTN-IVEILEKADE--NSLVLLDELGAGTDPqeGAALAI--AILEELLERGA 439

                        250
                 ....*....|
gi 502729652 456 YAIVVSHLGE 465
Cdd:COG1193  440 RVVATTHYSE 449
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
 330-392 1.23e-08

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: 55.35  E-value: 1.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502729652 330 FIDNpqpiDYYLDERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:cd03284   19 FVPN----DTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIF 77
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
330-392 1.72e-08

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 57.38  E-value: 1.72e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502729652 330 FIDNpqpiDYYLDERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:COG0249  602 FVPN----DCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIF 660
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 330-392 2.09e-08

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 57.03  E-value: 2.09e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502729652 330 FIDNpqpiDYYLDERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:PRK05399 596 FVPN----DCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIF 654
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 349-392 1.20e-07

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: 51.81  E-value: 1.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 502729652  349 ILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:pfam00488   2 IITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIF 45
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
 343-472 6.25e-06

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: 46.91  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 343 ERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVF---------DELfffkRKKMSYgsgaFENTIKSF 413
Cdd:cd03283   23 EKKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVkiftsirvsDDL----RDGISY----FYAELRRL 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502729652 414 ARAIS--SKGRK-LILVDEFEAITEPGAAVKILKKILELIHSAGDYAIVVSHLGEELSKLDF 472
Cdd:cd03283   95 KEIVEkaKKGEPvLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDL 156
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
 330-392 2.41e-05

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: 45.83  E-value: 2.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502729652 330 FIDNpqpiDYYLD-ERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:cd03285   18 FIPN----DVTLTrGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCIL 77
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 333-470 2.94e-04

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: 41.58  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 333 NPQPIDYYLDErNRIAILTGANSGGKTSLLELVCQIVILA--HMGLPVNAERAEVRVFDELFF-FKRKKMSYGSGAFENT 409
Cdd:cd03227   10 YFVPNDVTFGE-GSLTIITGPNGSGKSTILDAIGLALGGAqsATRRRSGVKAGCIVAAVSAELiFTRLQLSGGEKELSAL 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502729652 410 IKSFARAiSSKGRKLILVDEFEAITEPGAAVKILKKILELIHSaGDYAIVVSHLgEELSKL 470
Cdd:cd03227   89 ALILALA-SLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHL-PELAEL 146
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 336-465 5.36e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502729652 336 PIDYYLDERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNA-ERAEVRVFDELFffkrkkmsygsgA--------- 405
Cdd:PRK00409 318 PKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPAnEPSEIPVFKEIF------------Adigdeqsie 385

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502729652 406 -----FENTIKSFARAISSKGRK-LILVDEFEAITEP--GAAVKIlkKILELIHSAGDYAIVVSHLGE 465
Cdd:PRK00409 386 qslstFSGHMTNIVRILEKADKNsLVLFDELGAGTDPdeGAALAI--SILEYLRKRGAKIIATTHYKE 451
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
 329-392 1.76e-03

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: 40.16  E-value: 1.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502729652 329 LFIDNPQPIDYYLD-ERNRIAILTGANSGGKTSLLELVCQIVILAHMGLPVNAERAEVRVFDELF 392
Cdd:cd03287   14 LLDKSFVPNDIHLSaEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVL 78
 
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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