NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|495900518|ref|WP_008625097|]
View 

MutS-related protein, family 1 [Mariniradius saccharolyticus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 388-583 3.51e-72

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 cd03283:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 199  Bit Score: 229.88  E-value: 3.51e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 388 LKHPLILPNTAIGNDFHLGKEqKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAFGLFTSMRNTDNLGES 467
Cdd:cd03283    5 LGHPLIGREKRVANDIDMEKK-NGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVKIFTSIRVSDDLRDG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 468 VSSFYAELGRIKKLLDMAADGRPIFYLLDEILKGTNTIDRIMGSEALIRQLAASPCKGIISTHDIELSQLEDKLPYVINR 547
Cdd:cd03283   84 ISYFYAELRRLKEIVEKAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDLDSAVRNY 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495900518 548 SFHSQIFEDKILFDYTLKEGPCPSFNAHKLMELMGI 583
Cdd:cd03283  164 HFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIGI 199
 
Name Accession Description Interval E-value
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
 388-583 3.51e-72

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: 229.88  E-value: 3.51e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 388 LKHPLILPNTAIGNDFHLGKEqKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAFGLFTSMRNTDNLGES 467
Cdd:cd03283    5 LGHPLIGREKRVANDIDMEKK-NGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVKIFTSIRVSDDLRDG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 468 VSSFYAELGRIKKLLDMAADGRPIFYLLDEILKGTNTIDRIMGSEALIRQLAASPCKGIISTHDIELSQLEDKLPYVINR 547
Cdd:cd03283   84 ISYFYAELRRLKEIVEKAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDLDSAVRNY 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495900518 548 SFHSQIFEDKILFDYTLKEGPCPSFNAHKLMELMGI 583
Cdd:cd03283  164 HFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIGI 199
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
412-583 2.76e-27

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 108.80  E-value: 2.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518   412 VLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAF-GLFTSMRNTDNLGESVSSFYAELGRIKKLLDMAadGRP 490
Cdd:smart00534   2 VIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFdRIFTRIGASDSLAQGLSTFMVEMKETANILKNA--TKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518   491 IFYLLDEILKGTNTIDRIMGSEALIRQLAAS-PCKGIISTHDIELSQLEDKLPYVINRSFHSQIFEDKILFDYTLKEGPC 569
Cdd:smart00534  80 SLVLLDELGRGTSTYDGLAIAAAILEYLLEKiGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVA 159

                          170
                   ....*....|....
gi 495900518   570 PSFNAHKLMELMGI 583
Cdd:smart00534 160 GKSYGIEVAKLAGL 173
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
 353-568 4.60e-24

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


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 107.16  E-value: 4.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  353 LKEWQVLVSLASFAfeERLD-VLPTWNKSTEILAIDLKHPLI---LPNTAIGNDFHLGKEQKTVLLTGSNMSGKTTFMRT 428
Cdd:TIGR01070 534 LAELDVLANLAEVA--ETLHyTRPRFGDDPQLRIREGRHPVVeqvLRTPFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQ 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  429 LGINMVLANLGLGIFGKKFEIGAF-GLFTSMRNTDNLGESVSSFYAELGRIKKLLDMAADGRPIfyLLDEILKGTNTIDR 507
Cdd:TIGR01070 612 TALIALLAQIGSFVPAESAELPLFdRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLV--LFDEIGRGTSTYDG 689

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495900518  508 IMGSEALIRQLAAS-PCKGIISTHDIELSQLEDKLPYVINRSFHSQIFEDKILFDYTLKEGP 568
Cdd:TIGR01070 690 LALAWAIAEYLHEHiRAKTLFATHYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGP 751
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 412-570 3.77e-22

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: 94.18  E-value: 3.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  412 VLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAF-GLFTSMRNTDNLGESVSSFYAELGRIKKLLDMAADGRP 490
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVdRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  491 IfyLLDEILKGTNTIDRIMGSEALIRQLAAS-PCKGIISTHDIELSQLEDKLPYVINRSFHSQIFEDKILFDYTLKEGPC 569
Cdd:pfam00488  81 V--ILDELGRGTSTYDGLAIAWAVAEHLAEKiKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAA 158


                  .
gi 495900518  570 P 570
Cdd:pfam00488 159 D 159
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
358-568 7.56e-16

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 81.26  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 358 VLVSLASFAFEERLdVLPTWNKSTEILAIDLKHPLI---LPNTA-IGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGINM 433
Cdd:COG0249  559 VLASLAEVAVENNY-VRPELDDSPGIEIEGGRHPVVeqaLPGEPfVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIV 637

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 434 VLANLG---------LGIFGKKF-EIGAfglftsmrnTDNL--GEsvSSFY---AELGRI------KKLLdmaadgrpif 492
Cdd:COG0249  638 LLAQIGsfvpaesarIGIVDRIFtRVGA---------SDDLarGQ--STFMvemTETANIlnnateRSLV---------- 696

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 493 yLLDEILKGTNTIDrimG-------SEALIRQLAaspCKGIISTHDIELSQLEDKLPYVINrsFHSQIFE--DKILFDYT 563
Cdd:COG0249  697 -LLDEIGRGTSTYD---GlsiawavAEYLHDKIR---ARTLFATHYHELTELAEKLPGVKN--YHVAVKEwgGDIVFLHK 767


                 ....*
gi 495900518 564 LKEGP 568
Cdd:COG0249  768 VVPGP 772
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 358-568 1.20e-14

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 77.44  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 358 VLVSLASFAfeERLD-VLPTWNKSTEILAIDLKHPLI---LPNTA-IGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGIN 432
Cdd:PRK05399 553 VLASLAEVA--EENNyVRPEFTDDPGIDIEEGRHPVVeqvLGGEPfVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALI 630

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 433 MVLANLG---------LGIFGKKF-EIGAfglftsmrnTDNL--GEsvSSFYAElgrikkLLDMAAdgrpI--------F 492
Cdd:PRK05399 631 VLLAQIGsfvpaesarIGIVDRIFtRIGA---------SDDLasGR--STFMVE------MTETAN----IlnnatersL 689

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 493 YLLDEILKGTNTIDrimG-------SEALIRQLAaspCKGIISTHDIELSQLEDKLPYVINrsFHSQIFE--DKILFDYT 563
Cdd:PRK05399 690 VLLDEIGRGTSTYD---GlsiawavAEYLHDKIG---AKTLFATHYHELTELEEKLPGVKN--VHVAVKEhgGDIVFLHK 761


                 ....*
gi 495900518 564 LKEGP 568
Cdd:PRK05399 762 VVPGA 766
 
Name Accession Description Interval E-value
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
 388-583 3.51e-72

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: 229.88  E-value: 3.51e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 388 LKHPLILPNTAIGNDFHLGKEqKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAFGLFTSMRNTDNLGES 467
Cdd:cd03283    5 LGHPLIGREKRVANDIDMEKK-NGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVKIFTSIRVSDDLRDG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 468 VSSFYAELGRIKKLLDMAADGRPIFYLLDEILKGTNTIDRIMGSEALIRQLAASPCKGIISTHDIELSQLEDKLPYVINR 547
Cdd:cd03283   84 ISYFYAELRRLKEIVEKAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDLDSAVRNY 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495900518 548 SFHSQIFEDKILFDYTLKEGPCPSFNAHKLMELMGI 583
Cdd:cd03283  164 HFREDIDDNKLIFDYKLKPGVSPTRNALRLMKKIGI 199
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
 386-583 2.86e-41

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: 148.17  E-value: 2.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 386 IDLKHPLILP----NTAIGNDFHLGkEQKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIG-AFGLFTSMRN 460
Cdd:cd03243    3 KGGRHPVLLAltkgETFVPNDINLG-SGRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPlVDRIFTRIGA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 461 TDNLGESVSSFYAELGRIKKLLDMAadgRPI-FYLLDEILKGTNTIDRIMGSEALIRQLAASPCKGIISTHDIELSQLED 539
Cdd:cd03243   82 EDSISDGRSTFMAELLELKEILSLA---TPRsLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495900518 540 KLPYVINRSFHSQIFEDKILFDYTLKEGPCPSFNAHKLMELMGI 583
Cdd:cd03243  159 QVPGVKNLHMEELITTGGLTFTYKLIDGICDPSYALQIAELAGL 202
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
412-583 2.76e-27

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 108.80  E-value: 2.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518   412 VLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAF-GLFTSMRNTDNLGESVSSFYAELGRIKKLLDMAadGRP 490
Cdd:smart00534   2 VIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFdRIFTRIGASDSLAQGLSTFMVEMKETANILKNA--TKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518   491 IFYLLDEILKGTNTIDRIMGSEALIRQLAAS-PCKGIISTHDIELSQLEDKLPYVINRSFHSQIFEDKILFDYTLKEGPC 569
Cdd:smart00534  80 SLVLLDELGRGTSTYDGLAIAAAILEYLLEKiGARTLFATHYHELTKLADNHPGVRNLHMSALEETENITFLYKLKPGVA 159

                          170
                   ....*....|....
gi 495900518   570 PSFNAHKLMELMGI 583
Cdd:smart00534 160 GKSYGIEVAKLAGL 173
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
 353-568 4.60e-24

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


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 107.16  E-value: 4.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  353 LKEWQVLVSLASFAfeERLD-VLPTWNKSTEILAIDLKHPLI---LPNTAIGNDFHLGKEQKTVLLTGSNMSGKTTFMRT 428
Cdd:TIGR01070 534 LAELDVLANLAEVA--ETLHyTRPRFGDDPQLRIREGRHPVVeqvLRTPFVPNDLEMAHNRRMLLITGPNMGGKSTYMRQ 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  429 LGINMVLANLGLGIFGKKFEIGAF-GLFTSMRNTDNLGESVSSFYAELGRIKKLLDMAADGRPIfyLLDEILKGTNTIDR 507
Cdd:TIGR01070 612 TALIALLAQIGSFVPAESAELPLFdRIFTRIGASDDLASGRSTFMVEMTEAANILHNATENSLV--LFDEIGRGTSTYDG 689

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495900518  508 IMGSEALIRQLAAS-PCKGIISTHDIELSQLEDKLPYVINRSFHSQIFEDKILFDYTLKEGP 568
Cdd:TIGR01070 690 LALAWAIAEYLHEHiRAKTLFATHYFELTALEESLPGLKNVHVAALEHNGTIVFLHQVLPGP 751
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
 389-568 2.28e-23

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: 98.49  E-value: 2.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 389 KHPLI---LPNTA-IGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAF-GLFTSMRNTDN 463
Cdd:cd03284    6 RHPVVeqvLDNEPfVPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVdRIFTRIGASDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 464 LGESVSSFYAELGRIKKLLDMAADGRPIfyLLDEILKGTNTIDRIMGSEALIRQLA-ASPCKGIISTHDIELSQLEDKLP 542
Cdd:cd03284   86 LAGGRSTFMVEMVETANILNNATERSLV--LLDEIGRGTSTYDGLSIAWAIVEYLHeKIGAKTLFATHYHELTELEGKLP 163

                        170       180
                 ....*....|....*....|....*.
gi 495900518 543 YVINRSFHSQIFEDKILFDYTLKEGP 568
Cdd:cd03284  164 RVKNFHVAVKEKGGGVVFLHKIVEGA 189
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 412-570 3.77e-22

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: 94.18  E-value: 3.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  412 VLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAF-GLFTSMRNTDNLGESVSSFYAELGRIKKLLDMAADGRP 490
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVdRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  491 IfyLLDEILKGTNTIDRIMGSEALIRQLAAS-PCKGIISTHDIELSQLEDKLPYVINRSFHSQIFEDKILFDYTLKEGPC 569
Cdd:pfam00488  81 V--ILDELGRGTSTYDGLAIAWAVAEHLAEKiKARTLFATHYHELTKLAEKLPAVKNLHMAAVEDDDDIVFLYKVQPGAA 158


                  .
gi 495900518  570 P 570
Cdd:pfam00488 159 D 159
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
 388-583 2.29e-21

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: 92.88  E-value: 2.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 388 LKHPLILPNTA---IGNDFHLGKEQ-KTVLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAFG-LFTSMRNTD 462
Cdd:cd03286    5 LRHPCLNASTAssfVPNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDrIFTRIGARD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 463 NLGESVSSFYAELGRIKKLLDMAadGRPIFYLLDEILKGTNTIDRIMGSEALIRQLAAS-PCKGIISTHDIELSQLEDKL 541
Cdd:cd03286   85 DIMKGESTFMVELSETANILRHA--TPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKvKCLTLFSTHYHSLCDEFHEH 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495900518 542 PYVinRSFH--------SQIFEDKILFDYTLKEGPCPSFNAHKLMELMGI 583
Cdd:cd03286  163 GGV--RLGHmacavkneSDPTIRDITFLYKLVAGICPKSYGLYVALMAGI 210
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
 386-548 8.77e-18

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: 81.91  E-value: 8.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 386 IDLKHPLILPNTA--IGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGI-FGKKFEIGAF-GLFTSMRNT 461
Cdd:cd03280    3 REARHPLLPLQGEkvVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIpAAEGSSLPVFeNIFADIGDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 462 DNLGESVSSFYAELGRIKKLLDMAadGRPIFYLLDEILKGTNTIDRIMGSEALIRQLAASPCKGIISTHDIELSQLEDKL 541
Cdd:cd03280   83 QSIEQSLSTFSSHMKNIARILQHA--DPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAYAYKR 160


                 ....*..
gi 495900518 542 PYVINRS 548
Cdd:cd03280  161 EGVENAS 167
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
 386-575 1.35e-16

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: 78.96  E-value: 1.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 386 IDLKHPLI---LPNTAIGNDFHLGKEQKTVLL-TGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAF-GLFTSMRN 460
Cdd:cd03285    3 KEARHPCVeaqDDVAFIPNDVTLTRGKSRFLIiTGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVdCILARVGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 461 TDNLGESVSSFYAELGRIKKLLDMAADGRPIfyLLDEILKGTNTIDRIMGSEALIRQLAA---SPCkgIISTHDIELSQL 537
Cdd:cd03285   83 SDSQLKGVSTFMAEMLETAAILKSATENSLI--IIDELGRGTSTYDGFGLAWAIAEYIATqikCFC--LFATHFHELTAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 495900518 538 EDKLPYVINRSF--HSQIFEDKILFDYTLKEGPC-PSFNAH 575
Cdd:cd03285  159 ADEVPNVKNLHVtaLTDDASRTLTMLYKVEKGACdQSFGIH 199
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
 383-569 7.39e-16

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: 76.76  E-value: 7.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 383 ILAIDLKHPLI---LPNTAIGNDFHLGKE-QKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAF-GLFTS 457
Cdd:cd03287    1 ILIKEGRHPMIeslLDKSFVPNDIHLSAEgGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFdSVLTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 458 MRNTDNLGESVSSFYAELGRIKKLLDMAADGRPIfyLLDEILKGTNTIDRIMGSEALIRQLAASPCKGII-STHDIELSQ 536
Cdd:cd03287   81 MGASDSIQHGMSTFMVELSETSHILSNCTSRSLV--ILDELGRGTSTHDGIAIAYATLHYLLEEKKCLVLfVTHYPSLGE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495900518 537 LEDKLPYVInRSFHSQIFE----------DKILFDYTLKEGPC 569
Cdd:cd03287  159 ILRRFEGSI-RNYHMSYLEsqkdfetsdsQSITFLYKLVRGLA 200
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
358-568 7.56e-16

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 81.26  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 358 VLVSLASFAFEERLdVLPTWNKSTEILAIDLKHPLI---LPNTA-IGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGINM 433
Cdd:COG0249  559 VLASLAEVAVENNY-VRPELDDSPGIEIEGGRHPVVeqaLPGEPfVPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIV 637

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 434 VLANLG---------LGIFGKKF-EIGAfglftsmrnTDNL--GEsvSSFY---AELGRI------KKLLdmaadgrpif 492
Cdd:COG0249  638 LLAQIGsfvpaesarIGIVDRIFtRVGA---------SDDLarGQ--STFMvemTETANIlnnateRSLV---------- 696

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 493 yLLDEILKGTNTIDrimG-------SEALIRQLAaspCKGIISTHDIELSQLEDKLPYVINrsFHSQIFE--DKILFDYT 563
Cdd:COG0249  697 -LLDEIGRGTSTYD---GlsiawavAEYLHDKIR---ARTLFATHYHELTELAEKLPGVKN--YHVAVKEwgGDIVFLHK 767


                 ....*
gi 495900518 564 LKEGP 568
Cdd:COG0249  768 VVPGP 772
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
 386-576 6.24e-15

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: 73.87  E-value: 6.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 386 IDLKHPLILP--NTAIGNDFHL-GKEQKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAFG-LFTSMRNT 461
Cdd:cd03281    3 QGGRHPLLELfvDSFVPNDTEIgGGGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDkIFTRMSSR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 462 DNLGESVSSFYAELGRIKKLLDMAADGRPIfyLLDEILKGTNTIDRIMGSEALIR---QLAASPCKGIISTHDIELSQ-- 536
Cdd:cd03281   83 ESVSSGQSAFMIDLYQVSKALRLATRRSLV--LIDEFGKGTDTEDGAGLLIATIEhllKRGPECPRVIVSTHFHELFNrs 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495900518 537 -LEDKLPYV-----INRSFHSQIFEDKILFDYTLKEGPC-PSFNAHK 576
Cdd:cd03281  161 lLPERLKIKfltmeVLLNPTSTSPNEDITYLYRLVPGLAdTSFAIHC 207
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
373-546 7.94e-15

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 77.87  E-value: 7.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 373 VLPTWNKSTEILAIDLKHPLILPNTAIGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGINMVLANLGL----------GI 442
Cdd:COG1193  289 VKPELNDEGYIKLKKARHPLLDLKKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLpipaaegselPV 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 443 FGKKF-EIGafglftsmrntD--NLGESVSSFYAELGRIKKLLDmAADGRPIFyLLDEIlkGTNTiDRIMGS---EALIR 516
Cdd:COG1193  369 FDNIFaDIG-----------DeqSIEQSLSTFSSHMTNIVEILE-KADENSLV-LLDEL--GAGT-DPQEGAalaIAILE 432

                        170       180       190
                 ....*....|....*....|....*....|
gi 495900518 517 QLAASPCKGIISTHDIELSQLEDKLPYVIN 546
Cdd:COG1193  433 ELLERGARVVATTHYSELKAYAYNTEGVEN 462
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 358-568 1.20e-14

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 77.44  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 358 VLVSLASFAfeERLD-VLPTWNKSTEILAIDLKHPLI---LPNTA-IGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGIN 432
Cdd:PRK05399 553 VLASLAEVA--EENNyVRPEFTDDPGIDIEEGRHPVVeqvLGGEPfVPNDCDLDEERRLLLITGPNMAGKSTYMRQVALI 630

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 433 MVLANLG---------LGIFGKKF-EIGAfglftsmrnTDNL--GEsvSSFYAElgrikkLLDMAAdgrpI--------F 492
Cdd:PRK05399 631 VLLAQIGsfvpaesarIGIVDRIFtRIGA---------SDDLasGR--STFMVE------MTETAN----IlnnatersL 689

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 493 YLLDEILKGTNTIDrimG-------SEALIRQLAaspCKGIISTHDIELSQLEDKLPYVINrsFHSQIFE--DKILFDYT 563
Cdd:PRK05399 690 VLLDEIGRGTSTYD---GlsiawavAEYLHDKIG---AKTLFATHYHELTELEEKLPGVKN--VHVAVKEhgGDIVFLHK 761


                 ....*
gi 495900518 564 LKEGP 568
Cdd:PRK05399 762 VVPGA 766
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
 386-568 1.58e-13

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: 69.73  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 386 IDLKHPlILPNTA---IGNDFHLGKEQKTV-LLTGSNMSGKTTFMRTLGINMVLANLGLGIFGKKFEIGAF-GLFTSMRN 460
Cdd:cd03282    3 RDSRHP-ILDRDKknfIPNDIYLTRGSSRFhIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFnRLLSRLSN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 461 TDNLGESVSSFYAELGRIKKLLDMaADGRPIFyLLDEILKGTNTIDRIMGSEALIRQLAASPCKGIISTHDIELSQLEDK 540
Cdd:cd03282   82 DDSMERNLSTFASEMSETAYILDY-ADGDSLV-LIDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRDIAAILGN 159

                        170       180
                 ....*....|....*....|....*....
gi 495900518 541 LPYVINRSFHSQ-IFEDKILFDYTLKEGP 568
Cdd:cd03282  160 KSCVVHLHMKAQsINSNGIEMAYKLVLGL 188
mutS2 TIGR01069
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ...
 373-548 1.91e-12

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: 70.23  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  373 VLPTWNKSTEILAIDLKHPLILPNTAIGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGI-FGKKFEIGA 451
Cdd:TIGR01069 286 EFPMPSFTGKIILENARHPLLKEPKVVPFTLNLKFEKRVLAITGPNTGGKTVTLKTLGLLALMFQSGIPIpANEHSEIPY 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518  452 FG-LFTSMRNTDNLGESVSSFYAELGRIKKLLDmaADGRPIFYLLDEILKGTNTIDRIMGSEALIRQLAASPCKGIISTH 530
Cdd:TIGR01069 366 FEeIFADIGDEQSIEQNLSTFSGHMKNISAILS--KTTENSLVLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTH 443

                         170
                  ....*....|....*...
gi 495900518  531 DIELSQLEDKLPYVINRS 548
Cdd:TIGR01069 444 YKELKALMYNNEGVENAS 461
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 395-541 7.69e-11

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: 60.84  E-value: 7.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 395 PNTAIGNDFHLGKEQKTVLlTGSNMSGKTTFMRTLGINMVLANLGLGIfGKKFEIGAFG-------LFTSMRntdnlges 467
Cdd:cd03227    8 PSYFVPNDVTFGEGSLTII-TGPNGSGKSTILDAIGLALGGAQSATRR-RSGVKAGCIVaavsaelIFTRLQ-------- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495900518 468 VSSFYAELGRIKKLLDMAADGRPIFYLLDEILKGTNTIDRiMGSEALIRQLAASPCKGIISTHDIELSQLEDKL 541
Cdd:cd03227   78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDG-QALAEAILEHLVKGAQVIVITHLPELAELADKL 150
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 363-548 2.24e-10

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 63.69  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 363 ASFAFEERLdVLPTWNKSTEILAIDLKHPLILPNTAIGNDFHLGKEQKTVLLTGSNMSGKTTFMRTLGINMVLANLGLGI 442
Cdd:PRK00409 282 ARYAKALKA-TFPLFNDEGKIDLRQARHPLLDGEKVVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPI 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 443 FGK-KFEIGAF-GLFTSMRNTDNLGESVSSFYAELGRIKKLLDmaADGRPIFYLLDEILKGTntiDRIMGSE---ALIRQ 517
Cdd:PRK00409 361 PANePSEIPVFkEIFADIGDEQSIEQSLSTFSGHMTNIVRILE--KADKNSLVLFDELGAGT---DPDEGAAlaiSILEY 435

                        170       180       190
                 ....*....|....*....|....*....|.
gi 495900518 518 LAASPCKGIISTHDIELSQLEDKLPYVINRS 548
Cdd:PRK00409 436 LRKRGAKIIATTHYKELKALMYNREGVENAS 466
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 400-537 1.48e-04

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: 42.62  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495900518 400 GNDFHLGKEQKtVLLTGSNMSGKTTFMRTLginMVLANLGLG-IFGKKFEIGAFGLFTSMRNtdnlgesvSSFYAEL-GR 477
Cdd:cd00267   17 NVSLTLKAGEI-VALVGPNGSGKSTLLRAI---AGLLKPTSGeILIDGKDIAKLPLEELRRR--------IGYVPQLsGG 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495900518 478 IKKLLDMAAD--GRPIFYLLDEILKGTNTIDRImGSEALIRQLAASPCKGIISTHDIELSQL 537
Cdd:cd00267   85 QRQRVALARAllLNPDLLLLDEPTSGLDPASRE-RLLELLRELAEEGRTVIIVTHDPELAEL 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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