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Conserved domains on  [gi|1785918051|ref|WP_157183367|]
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MutS-related protein [Sciscionella marina]

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 ...
 331-515 5.45e-48

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 cd03243:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 202  Bit Score: 165.12  E-value: 5.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 331 NKTVVCNDLRLHDReRILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQD 410
Cdd:cd03243    16 GETFVPNDINLGSG-RLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRIGAEDSISDGRSTFMA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 411 DLLRMRSILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRLGKATVSM----VSVVDPE 486
Cdd:cd03243    95 ELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQVPGVknlhMEELITT 174

                         170       180
                  ....*....|....*....|....*....
gi 1785918051 487 DPAIRTYQLVRRPADgHSYAEAIAEKYGL 515
Cdd:cd03243   175 GGLTFTYKLIDGICD-PSYALQIAELAGL 202
 
Name Accession Description Interval E-value
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
 331-515 5.45e-48

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: 165.12  E-value: 5.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 331 NKTVVCNDLRLHDReRILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQD 410
Cdd:cd03243    16 GETFVPNDINLGSG-RLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRIGAEDSISDGRSTFMA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 411 DLLRMRSILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRLGKATVSM----VSVVDPE 486
Cdd:cd03243    95 ELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQVPGVknlhMEELITT 174

                         170       180
                  ....*....|....*....|....*....
gi 1785918051 487 DPAIRTYQLVRRPADgHSYAEAIAEKYGL 515
Cdd:cd03243   175 GGLTFTYKLIDGICD-PSYALQIAELAGL 202
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
347-526 8.38e-22

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 92.62  E-value: 8.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051  347 ILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQDDLLRMRSILDTATDRS 426
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051  427 IVILNELFTSTSMADASEMGTEILLRMIE-LGCLCVCVTFIDELSRLGK--ATVSMVSV-VDPEDPAIR-TYQLVRRPAD 501
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEkIGARTLFATHYHELTKLADnhPGVRNLHMsALEETENITfLYKLKPGVAG 160

                          170       180
                   ....*....|....*....|....*
gi 1785918051  502 GhSYAEAIAEKYGLtYDRIKERVLR 526
Cdd:smart00534 161 K-SYGIEVAKLAGL-PKEVIERAKR 183
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
332-515 7.07e-17

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 84.04  E-value: 7.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 332 KTVVCNDLRLHDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSE-ARVYLFDQLFThfehgeNLGDlRGKLQD 410
Cdd:COG1193   312 KKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEgSELPVFDNIFA------DIGD-EQSIEQ 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 411 DL-------LRMRSILDTATDRSIVILNELFTST--------SMAdasemgteILLRMIELGCLCVCVTFIDELSRLGKA 475
Cdd:COG1193   385 SLstfsshmTNIVEILEKADENSLVLLDELGAGTdpqegaalAIA--------ILEELLERGARVVATTHYSELKAYAYN 456

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1785918051 476 TVSMV--SVV-DPED--PairTYQL-VRRPadGHSYAEAIAEKYGL 515
Cdd:COG1193   457 TEGVEnaSVEfDVETlsP---TYRLlIGVP--GRSNAFEIARRLGL 497
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 348-515 4.18e-16

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: 76.46  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 348 LVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQDDLLRMRSILDTATDRSI 427
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 428 VILNEL--FTST----SMADASemgTEILLRmiELGCLCVCVTFIDELSRLGK-----ATVSMVSVVDPEDPAIrTYQLV 496
Cdd:pfam00488  81 VILDELgrGTSTydglAIAWAV---AEHLAE--KIKARTLFATHYHELTKLAEklpavKNLHMAAVEDDDDIVF-LYKVQ 154

                         170
                  ....*....|....*....
gi 1785918051 497 RRPADGhSYAEAIAEKYGL 515
Cdd:pfam00488 155 PGAADK-SYGIHVAELAGL 172
mutS2 TIGR01069
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ...
 272-515 1.79e-13

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: 73.32  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 272 ETISSFDREVHFYLAYLEFIDPLrQAGLRFCFpvvSTSGKEVEAGQTFDIAL---AHKLTQANKtVVCNDLRLHDRERIL 348
Cdd:TIGR01069 251 EKVQEYLLELKFLFKEFDFLDSL-QARARYAK---AVKGEFPMPSFTGKIILenaRHPLLKEPK-VVPFTLNLKFEKRVL 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 349 VITGPNQGGKTTMARTFAQVHYLAALGLLVPGSE-ARVYLFDQLFTHFEHGENLGDLRGKLQDDLLRMRSILDTATDRSI 427
Cdd:TIGR01069 326 AITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEhSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENSL 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 428 VILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRLG--KATVSMVSVVDPEDPAIRTYQLVRRpADGHSY 505
Cdd:TIGR01069 406 VLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMynNEGVENASVLFDEETLSPTYKLLKG-IPGESY 484

                         250
                  ....*....|
gi 1785918051 506 AEAIAEKYGL 515
Cdd:TIGR01069 485 AFEIAQRYGI 494
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 337-437 4.42e-12

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 68.97  E-value: 4.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 337 NDLRLHDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFThfehgenlgdlR-GKLqDDLLRM 415
Cdd:PRK05399  599 NDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFT-----------RiGAS-DDLASG 666

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1785918051 416 RS-----------ILDTATDRSIVILNELF--TST 437
Cdd:PRK05399  667 RStfmvemtetanILNNATERSLVLLDEIGrgTST 701
 
Name Accession Description Interval E-value
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
 331-515 5.45e-48

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: 165.12  E-value: 5.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 331 NKTVVCNDLRLHDReRILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQD 410
Cdd:cd03243    16 GETFVPNDINLGSG-RLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTRIGAEDSISDGRSTFMA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 411 DLLRMRSILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRLGKATVSM----VSVVDPE 486
Cdd:cd03243    95 ELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPEQVPGVknlhMEELITT 174

                         170       180
                  ....*....|....*....|....*....
gi 1785918051 487 DPAIRTYQLVRRPADgHSYAEAIAEKYGL 515
Cdd:cd03243   175 GGLTFTYKLIDGICD-PSYALQIAELAGL 202
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
347-526 8.38e-22

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 92.62  E-value: 8.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051  347 ILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQDDLLRMRSILDTATDRS 426
Cdd:smart00534   1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051  427 IVILNELFTSTSMADASEMGTEILLRMIE-LGCLCVCVTFIDELSRLGK--ATVSMVSV-VDPEDPAIR-TYQLVRRPAD 501
Cdd:smart00534  81 LVLLDELGRGTSTYDGLAIAAAILEYLLEkIGARTLFATHYHELTKLADnhPGVRNLHMsALEETENITfLYKLKPGVAG 160

                          170       180
                   ....*....|....*....|....*
gi 1785918051  502 GhSYAEAIAEKYGLtYDRIKERVLR 526
Cdd:smart00534 161 K-SYGIEVAKLAGL-PKEVIERAKR 183
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
 327-515 1.73e-21

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: 92.31  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 327 LTQANKTVVCNDLRLHDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSE-ARVYLFDQLFThfehgeNLGDLR 405
Cdd:cd03280    10 LPLQGEKVVPLDIQLGENKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAAEgSSLPVFENIFA------DIGDEQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 406 GKLQD------DLLRMRSILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRLGKATVSM 479
Cdd:cd03280    84 SIEQSlstfssHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGELKAYAYKREGV 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1785918051 480 V--SV-VDPED--PairTYQL-VRRPadGHSYAEAIAEKYGL 515
Cdd:cd03280   164 EnaSMeFDPETlkP---TYRLlIGVP--GRSNALEIARRLGL 200
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
 335-515 3.55e-19

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: 86.17  E-value: 3.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 335 VCNDLRLHDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQDDLLR 414
Cdd:cd03284    20 VPNDTELDPERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTRIGASDDLAGGRSTFMVEMVE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 415 MRSILDTATDRSIVILNELFTSTSMADasemGTEILLRMIE-----LGCLCVCVTFIDELSRLGK-----ATVSMvSVVD 484
Cdd:cd03284   100 TANILNNATERSLVLLDEIGRGTSTYD----GLSIAWAIVEylhekIGAKTLFATHYHELTELEGklprvKNFHV-AVKE 174

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1785918051 485 PEDPAIRTYQLVRRPADgHSYAEAIAEKYGL 515
Cdd:cd03284   175 KGGGVVFLHKIVEGAAD-KSYGIEVARLAGL 204
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
 332-464 5.53e-17

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: 79.84  E-value: 5.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 332 KTVVCNDLRLH-DRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQD 410
Cdd:cd03287    17 KSFVPNDIHLSaEGGYCQIITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVLTRMGASDSIQHGMSTFMV 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1785918051 411 DLLRMRSILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIEL-GCLCVCVT 464
Cdd:cd03287    97 ELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEkKCLVLFVT 151
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
332-515 7.07e-17

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 84.04  E-value: 7.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 332 KTVVCNDLRLHDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSE-ARVYLFDQLFThfehgeNLGDlRGKLQD 410
Cdd:COG1193   312 KKVVPIDIELGEDFRTLVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAAEgSELPVFDNIFA------DIGD-EQSIEQ 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 411 DL-------LRMRSILDTATDRSIVILNELFTST--------SMAdasemgteILLRMIELGCLCVCVTFIDELSRLGKA 475
Cdd:COG1193   385 SLstfsshmTNIVEILEKADENSLVLLDELGAGTdpqegaalAIA--------ILEELLERGARVVATTHYSELKAYAYN 456

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1785918051 476 TVSMV--SVV-DPED--PairTYQL-VRRPadGHSYAEAIAEKYGL 515
Cdd:COG1193   457 TEGVEnaSVEfDVETlsP---TYRLlIGVP--GRSNAFEIARRLGL 497
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 348-515 4.18e-16

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: 76.46  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 348 LVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQDDLLRMRSILDTATDRSI 427
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 428 VILNEL--FTST----SMADASemgTEILLRmiELGCLCVCVTFIDELSRLGK-----ATVSMVSVVDPEDPAIrTYQLV 496
Cdd:pfam00488  81 VILDELgrGTSTydglAIAWAV---AEHLAE--KIKARTLFATHYHELTKLAEklpavKNLHMAAVEDDDDIVF-LYKVQ 154

                         170
                  ....*....|....*....
gi 1785918051 497 RRPADGhSYAEAIAEKYGL 515
Cdd:pfam00488 155 PGAADK-SYGIHVAELAGL 172
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
 329-515 1.13e-15

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: 75.93  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 329 QANKTVVCNDLRLHDRE-RILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFThfehgenlgdlRGK 407
Cdd:cd03286    13 STASSFVPNDVDLGATSpRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFT-----------RIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 408 LQDDLLRMRS-----------ILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIE-LGCLCVCVT----FIDELSR 471
Cdd:cd03286    82 ARDDIMKGEStfmvelsetanILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKkVKCLTLFSThyhsLCDEFHE 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1785918051 472 LGKATVS-MVSVVDPE-DPAIRTYQLVRRPADGhsyaeAIAEKYGL 515
Cdd:cd03286   162 HGGVRLGhMACAVKNEsDPTIRDITFLYKLVAG-----ICPKSYGL 202
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
 325-511 7.94e-15

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: 73.56  E-value: 7.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 325 HKLTQANKTVVC--NDLRLH-DRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENL 401
Cdd:cd03285     7 HPCVEAQDDVAFipNDVTLTrGKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCILARVGASDSQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 402 gdLRG--KLQDDLLRMRSILDTATDRSIVILNELFTSTSMAD--------ASEMGTEIllrmielGCLCVCVTFIDELSR 471
Cdd:cd03285    87 --LKGvsTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDgfglawaiAEYIATQI-------KCFCLFATHFHELTA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1785918051 472 LGK--ATVSMVSVVDPEDPAIRT----YQLVRRPADgHSYAEAIAE 511
Cdd:cd03285   158 LADevPNVKNLHVTALTDDASRTltmlYKVEKGACD-QSFGIHVAE 202
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
 332-515 8.82e-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: 73.49  E-value: 8.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 332 KTVVCNDLRLHDRE-RILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLRGKLQD 410
Cdd:cd03281    15 DSFVPNDTEIGGGGpSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFTRMSSRESVSSGQSAFMI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 411 DLLRMRSILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIELGCLC----VCVTFID-----ELSRLGKATVSMVS 481
Cdd:cd03281    95 DLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRGPECprviVSTHFHElfnrsLLPERLKIKFLTME 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1785918051 482 V------VDPEDPAIRTYQLVRRPADgHSYAEAIAEKYGL 515
Cdd:cd03281   175 VllnptsTSPNEDITYLYRLVPGLAD-TSFAIHCAKLAGI 213
mutS2 TIGR01069
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ...
 272-515 1.79e-13

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: 73.32  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 272 ETISSFDREVHFYLAYLEFIDPLrQAGLRFCFpvvSTSGKEVEAGQTFDIAL---AHKLTQANKtVVCNDLRLHDRERIL 348
Cdd:TIGR01069 251 EKVQEYLLELKFLFKEFDFLDSL-QARARYAK---AVKGEFPMPSFTGKIILenaRHPLLKEPK-VVPFTLNLKFEKRVL 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 349 VITGPNQGGKTTMARTFAQVHYLAALGLLVPGSE-ARVYLFDQLFTHFEHGENLGDLRGKLQDDLLRMRSILDTATDRSI 427
Cdd:TIGR01069 326 AITGPNTGGKTVTLKTLGLLALMFQSGIPIPANEhSEIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENSL 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 428 VILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRLG--KATVSMVSVVDPEDPAIRTYQLVRRpADGHSY 505
Cdd:TIGR01069 406 VLFDELGAGTDPDEGSALAISILEYLLKQNAQVLITTHYKELKALMynNEGVENASVLFDEETLSPTYKLLKG-IPGESY 484

                         250
                  ....*....|
gi 1785918051 506 AEAIAEKYGL 515
Cdd:TIGR01069 485 AFEIAQRYGI 494
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
 327-512 1.42e-12

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: 66.64  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 327 LTQANKTVVCNDLRL-HDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFTHFEHGENLGDLR 405
Cdd:cd03282    10 LDRDKKNFIPNDIYLtRGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLSRLSNDDSMERNL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 406 GKLQDDLLRMRSILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRL-----GKATVSMV 480
Cdd:cd03282    90 STFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRDIAAIlgnksCVVHLHMK 169

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1785918051 481 SVVDPEDPAIRTYQLVRRPADGHSYAEAIAEK 512
Cdd:cd03282   170 AQSINSNGIEMAYKLVLGLYRIVDDGIRFVRV 201
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
335-437 1.43e-12

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 70.48  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 335 VCNDLRLHDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFThfehgenlgdlRGKLQDDLLR 414
Cdd:COG0249   603 VPNDCDLDPDRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFT-----------RVGASDDLAR 671

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1785918051 415 MRS-----------ILDTATDRSIVILNEL--FTST 437
Cdd:COG0249   672 GQStfmvemtetanILNNATERSLVLLDEIgrGTST 707
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 337-437 4.42e-12

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 68.97  E-value: 4.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 337 NDLRLHDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEARVYLFDQLFThfehgenlgdlR-GKLqDDLLRM 415
Cdd:PRK05399  599 NDCDLDEERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIFT-----------RiGAS-DDLASG 666

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1785918051 416 RS-----------ILDTATDRSIVILNELF--TST 437
Cdd:PRK05399  667 RStfmvemtetanILNNATERSLVLLDEIGrgTST 701
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
 322-495 3.25e-10

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: 59.62  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 322 ALAHKLTQANKTVVcNDLRLHDReRILVITGPNQGGKTTMARTFAQVHYLAALGLLVPGSEArVYLFDQLFTHFEHGENL 401
Cdd:cd03283     4 NLGHPLIGREKRVA-NDIDMEKK-NGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSF-ELPPVKIFTSIRVSDDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 402 GDLRGKLQDDLLRMRSILDTATDR--SIVILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRLGKatvsm 479
Cdd:cd03283    81 RDGISYFYAELRRLKEIVEKAKKGepVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLD----- 155

                         170
                  ....*....|....*.
gi 1785918051 480 vsvvdpEDPAIRTYQL 495
Cdd:cd03283   156 ------LDSAVRNYHF 165
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 332-515 6.24e-10

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 61.77  E-value: 6.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 332 KTVVCNDLRLHDRERILVITGPNQGGKTTMARTFAQVHYLAALGLLVP---GSEARVylFDQLFThfehgeNLGDLRgKL 408
Cdd:PRK00409  314 EKVVPKDISLGFDKTVLVITGPNTGGKTVTLKTLGLAALMAKSGLPIPanePSEIPV--FKEIFA------DIGDEQ-SI 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 409 QDDL-------LRMRSILDTATDRSIVILNELFTSTSMADASEMGTEILLRMIELGCLCVCVTFIDELSRLGKAT--VSM 479
Cdd:PRK00409  385 EQSLstfsghmTNIVRILEKADKNSLVLFDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKELKALMYNRegVEN 464

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1785918051 480 VSV---VDPEDPairTYQL---VrrPadGHSYAEAIAEKYGL 515
Cdd:PRK00409  465 ASVefdEETLRP---TYRLligI--P--GKSNAFEIAKRLGL 499
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 343-455 8.24e-06

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: 46.20  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 343 DRERILVITGPNQGGKTTMAR------TFAQVH----YLAALGLLVPGSEA-RVYLFDQLfthfEHGENlgdlrgklqdD 411
Cdd:cd03227    19 GEGSLTIITGPNGSGKSTILDaiglalGGAQSAtrrrSGVKAGCIVAAVSAeLIFTRLQL----SGGEK----------E 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1785918051 412 LLRMRSILDTAT--DRSIVILNELFTSTSMADAsemgtEILLRMIE 455
Cdd:cd03227    85 LSALALILALASlkPRPLYILDEIDRGLDPRDG-----QALAEAIL 125
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 331-473 1.01e-03

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: 39.92  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 331 NKTVVCNDLRLH-DRERILVITGPNQGGKTTMARtfaqvhylaALGLLVPGSEARVYLfdqlfthfeHGENLGDLRGKLQ 409
Cdd:cd00267    10 GGRTALDNVSLTlKAGEIVALVGPNGSGKSTLLR---------AIAGLLKPTSGEILI---------DGKDIAKLPLEEL 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785918051 410 DDLL----------RMRSILDTA--TDRSIVILNELFTSTSMADASEMgTEILLRMIELGCLCVCVT-FIDELSRLG 473
Cdd:cd00267    72 RRRIgyvpqlsggqRQRVALARAllLNPDLLLLDEPTSGLDPASRERL-LELLRELAEEGRTVIIVThDPELAELAA 147
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 331-479 4.32e-03

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 38.32  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 331 NKTVVCNDLRLH-DRERILVITGPNQGGKTTMARTFA--------QVHY----LAALGLLVPGSEARV-YLFDQ--LFTH 394
Cdd:cd03229    11 GQKTVLNDVSLNiEAGEIVALLGPSGSGKSTLLRCIAgleepdsgSILIdgedLTDLEDELPPLRRRIgMVFQDfaLFPH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785918051 395 FEHGENLG-DLRGKLQDDLLRMRSIldtATDRSIVILNELFTSTSMADASEMGTeiLLRMI--ELGCLCVCVTF-IDELS 470
Cdd:cd03229    91 LTVLENIAlGLSGGQQQRVALARAL---AMDPDVLLLDEPTSALDPITRREVRA--LLKSLqaQLGITVVLVTHdLDEAA 165


                  ....*....
gi 1785918051 471 RLGKATVSM 479
Cdd:cd03229   166 RLADRVVVL 174
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 346-370 6.34e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 463799 [Multi-domain]  Cd Length: 128  Bit Score: 36.80  E-value: 6.34e-03
                          10        20
                  ....*....|....*....|....*
gi 1785918051 346 RILVITGPNQGGKTTMARTFAQVHY 370
Cdd:pfam13173   3 KILVITGPRQVGKTTLLLQLIKELL 27
 
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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