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Conserved domains on  [gi|489565927|ref|WP_003470432|]
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MULTISPECIES: DNA mismatch repair protein MutS [Bacillota]

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 ...
 344-531 1.35e-64

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: 209.46  E-value: 1.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 344 ELENLYHPLV--KNPIKNSISI--KNNIIFTGSNASGKSTFIKGIALNCILAQSLNTALCSKYKCKFSKVVTSMAIRDNI 419
Cdd:cd03283    1 EAKNLGHPLIgrEKRVANDIDMekKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVKIFTSIRVSDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 420 LLGESYFIAEIKSLKRLLDSLNGEIRVLAFIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIELTEMITD---Y 496
Cdd:cd03283   81 RDGISYFYAELRRLKEIVEKAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDLdsaV 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489565927 497 ENFHFSEIVTDDEVTFDYKLKLGPSKTRNALKLLK 531
Cdd:cd03283  161 RNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMK 195
 
Name Accession Description Interval E-value
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
 344-531 1.35e-64

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: 209.46  E-value: 1.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 344 ELENLYHPLV--KNPIKNSISI--KNNIIFTGSNASGKSTFIKGIALNCILAQSLNTALCSKYKCKFSKVVTSMAIRDNI 419
Cdd:cd03283    1 EAKNLGHPLIgrEKRVANDIDMekKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVKIFTSIRVSDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 420 LLGESYFIAEIKSLKRLLDSLNGEIRVLAFIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIELTEMITD---Y 496
Cdd:cd03283   81 RDGISYFYAELRRLKEIVEKAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDLdsaV 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489565927 497 ENFHFSEIVTDDEVTFDYKLKLGPSKTRNALKLLK 531
Cdd:cd03283  161 RNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMK 195
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
367-547 1.53e-26

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 106.49  E-value: 1.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927   367 IIFTGSNASGKSTFIKGIALNCILAQSLNTALCSKYKCK-FSKVVTSMAIRDNILLGESYFIAEIKSLKRLLDSLNGeiR 445
Cdd:smart00534   2 VIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPvFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATK--N 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927   446 VLAFIDEILKGTNTLERISSSASILKY-AKNTKAKLFVATHDIELTEMITD---YENFHFSEIVTDDEVTFDYKLKLGPS 521
Cdd:smart00534  80 SLVLLDELGRGTSTYDGLAIAAAILEYlLEKIGARTLFATHYHELTKLADNhpgVRNLHMSALEETENITFLYKLKPGVA 159

                          170       180
                   ....*....|....*....|....*.
gi 489565927   522 KTRNALKLLKTFDFENEVICLANSIY 547
Cdd:smart00534 160 GKSYGIEVAKLAGLPKEVIERAKRIL 185
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 367-550 7.00e-25

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: 101.89  E-value: 7.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927  367 IIFTGSNASGKSTFIKGIALNCILAQS-----LNTALCSKYKCKFSKVVTSmairDNILLGESYFIAEIKSLKRLLDSLN 441
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIgsfvpAESAEIGIVDRIFTRIGAS----DDLAKGRSTFMVEMLETANILHNAT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927  442 GEIRVLafIDEILKGTNTLERISSSASILKY-AKNTKAKLFVATHDIELTEM---ITDYENFHFSEIVTDDEVTFDYKLK 517
Cdd:pfam00488  77 DKSLVI--LDELGRGTSTYDGLAIAWAVAEHlAEKIKARTLFATHYHELTKLaekLPAVKNLHMAAVEDDDDIVFLYKVQ 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489565927  518 LGPSKTRNALKLLKTFDFENEVICLANSIYNDF 550
Cdd:pfam00488 155 PGAADKSYGIHVAELAGLPESVVERAREILAEL 187
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 311-521 4.21e-16

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 81.68  E-value: 4.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 311 DIVAKLDFAMSLTfYRKSIDEYTIPEFTESEDIELENLYHP-----LVKNP-IKNSISIKNN---IIFTGSNASGKSTFI 381
Cdd:PRK05399 546 KALAELDVLASLA-EVAEENNYVRPEFTDDPGIDIEEGRHPvveqvLGGEPfVPNDCDLDEErrlLLITGPNMAGKSTYM 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 382 KGIALNCILAQ------------SLntalcskykckFSKVVTSMAIRDNILLGESYFIAEIKSLKRLL-----DSLngei 444
Cdd:PRK05399 625 RQVALIVLLAQigsfvpaesariGI-----------VDRIFTRIGASDDLASGRSTFMVEMTETANILnnateRSL---- 689

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 445 rVLafIDEILKGTNTLERISSSASILKY-AKNTKAK-LFvATHDIELTEMITDYE---NFHFSEIVTDDEVTFDYKLKLG 519
Cdd:PRK05399 690 -VL--LDEIGRGTSTYDGLSIAWAVAEYlHDKIGAKtLF-ATHYHELTELEEKLPgvkNVHVAVKEHGGDIVFLHKVVPG 765


                 ..
gi 489565927 520 PS 521
Cdd:PRK05399 766 AA 767
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
311-521 2.65e-15

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 79.33  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 311 DIVAKLDFAMSLTfYRKSIDEYTIPEFTESEDIELENLYHPLV-----KNP-IKNSISIKNN---IIFTGSNASGKSTFI 381
Cdd:COG0249  552 RALAELDVLASLA-EVAVENNYVRPELDDSPGIEIEGGRHPVVeqalpGEPfVPNDCDLDPDrriLLITGPNMAGKSTYM 630

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 382 KGIALNCILAQ--------SLNTALCSKYkckFSKVVTSmairDNILLGESYF------IAEI------KSLkrlldsln 441
Cdd:COG0249  631 RQVALIVLLAQigsfvpaeSARIGIVDRI---FTRVGAS----DDLARGQSTFmvemteTANIlnnateRSL-------- 695

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 442 geirVLafIDEILKGTNTLERISSSASILKY-AKNTKAK-LFvATHDIELTEMITDYE---NFHFSEIVTDDEVTFDYKL 516
Cdd:COG0249  696 ----VL--LDEIGRGTSTYDGLSIAWAVAEYlHDKIRARtLF-ATHYHELTELAEKLPgvkNYHVAVKEWGGDIVFLHKV 768


                 ....*
gi 489565927 517 KLGPS 521
Cdd:COG0249  769 VPGPA 773
 
Name Accession Description Interval E-value
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
 344-531 1.35e-64

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: 209.46  E-value: 1.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 344 ELENLYHPLV--KNPIKNSISI--KNNIIFTGSNASGKSTFIKGIALNCILAQSLNTALCSKYKCKFSKVVTSMAIRDNI 419
Cdd:cd03283    1 EAKNLGHPLIgrEKRVANDIDMekKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELPPVKIFTSIRVSDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 420 LLGESYFIAEIKSLKRLLDSLNGEIRVLAFIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIELTEMITD---Y 496
Cdd:cd03283   81 RDGISYFYAELRRLKEIVEKAKKGEPVLFLLDEIFKGTNSRERQAASAAVLKFLKNKNTIGIISTHDLELADLLDLdsaV 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489565927 497 ENFHFSEIVTDDEVTFDYKLKLGPSKTRNALKLLK 531
Cdd:cd03283  161 RNYHFREDIDDNKLIFDYKLKPGVSPTRNALRLMK 195
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
 344-531 2.39e-30

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: 117.74  E-value: 2.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 344 ELENLYHPLV------KNPIKNSISIKNN--IIFTGSNASGKSTFIKGIALNCILAQSLNTALCSKYK-CKFSKVVTSMA 414
Cdd:cd03243    1 EIKGGRHPVLlaltkgETFVPNDINLGSGrlLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASiPLVDRIFTRIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 415 IRDNILLGESYFIAEIKSLKRLLDSLNGEIRVLafIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIELTEMIT 494
Cdd:cd03243   81 AEDSISDGRSTFMAELLELKEILSLATPRSLVL--IDELGRGTSTAEGLAIAYAVLEHLLEKGCRTLFATHFHELADLPE 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489565927 495 DYE---NFHFSEIVTDDEVTFDYKLKLGPSKTRNALKLLK 531
Cdd:cd03243  159 QVPgvkNLHMEELITTGGLTFTYKLIDGICDPSYALQIAE 198
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
367-547 1.53e-26

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 106.49  E-value: 1.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927   367 IIFTGSNASGKSTFIKGIALNCILAQSLNTALCSKYKCK-FSKVVTSMAIRDNILLGESYFIAEIKSLKRLLDSLNGeiR 445
Cdd:smart00534   2 VIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPvFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATK--N 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927   446 VLAFIDEILKGTNTLERISSSASILKY-AKNTKAKLFVATHDIELTEMITD---YENFHFSEIVTDDEVTFDYKLKLGPS 521
Cdd:smart00534  80 SLVLLDELGRGTSTYDGLAIAAAILEYlLEKIGARTLFATHYHELTKLADNhpgVRNLHMSALEETENITFLYKLKPGVA 159

                          170       180
                   ....*....|....*....|....*.
gi 489565927   522 KTRNALKLLKTFDFENEVICLANSIY 547
Cdd:smart00534 160 GKSYGIEVAKLAGLPKEVIERAKRIL 185
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
 367-550 7.00e-25

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: 101.89  E-value: 7.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927  367 IIFTGSNASGKSTFIKGIALNCILAQS-----LNTALCSKYKCKFSKVVTSmairDNILLGESYFIAEIKSLKRLLDSLN 441
Cdd:pfam00488   1 LIITGPNMGGKSTYLRQVALIVLMAQIgsfvpAESAEIGIVDRIFTRIGAS----DDLAKGRSTFMVEMLETANILHNAT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927  442 GEIRVLafIDEILKGTNTLERISSSASILKY-AKNTKAKLFVATHDIELTEM---ITDYENFHFSEIVTDDEVTFDYKLK 517
Cdd:pfam00488  77 DKSLVI--LDELGRGTSTYDGLAIAWAVAEHlAEKIKARTLFATHYHELTKLaekLPAVKNLHMAAVEDDDDIVFLYKVQ 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 489565927  518 LGPSKTRNALKLLKTFDFENEVICLANSIYNDF 550
Cdd:pfam00488 155 PGAADKSYGIHVAELAGLPESVVERAREILAEL 187
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
 350-521 4.22e-21

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: 91.94  E-value: 4.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 350 HPLVKNPIKNSISIKNN---------IIFTGSNASGKSTFIKGIALNCILAQSLNTALCSKYK-CKFSKVVTSMAIRDNI 419
Cdd:cd03284    7 HPVVEQVLDNEPFVPNDteldperqiLLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEiGVVDRIFTRIGASDDL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 420 LLGESYFIAEIKSLKRLLdsLNGEIRVLAFIDEILKGTNTLERISSSASILKY-AKNTKAKLFVATHDIELTEM---ITD 495
Cdd:cd03284   87 AGGRSTFMVEMVETANIL--NNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYlHEKIGAKTLFATHYHELTELegkLPR 164

                        170       180
                 ....*....|....*....|....*.
gi 489565927 496 YENFHFSEIVTDDEVTFDYKLKLGPS 521
Cdd:cd03284  165 VKNFHVAVKEKGGGVVFLHKIVEGAA 190
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
 344-528 8.52e-18

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: 82.35  E-value: 8.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 344 ELENLYHPL----VKNPIKNSISIKNN----IIFTGSNASGKSTFIKGIALNCILAQslntalCSKYKCK-------FSK 408
Cdd:cd03281    1 EIQGGRHPLlelfVDSFVPNDTEIGGGgpsiMVITGPNSSGKSVYLKQVALIVFLAH------IGSFVPAdsatiglVDK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 409 VVTSMAIRDNILLGESYFIAEIKSLKRLLDSLNGeiRVLAFIDEILKGTNTLERISSSASILKYAKNTKA---KLFVATH 485
Cdd:cd03281   75 IFTRMSSRESVSSGQSAFMIDLYQVSKALRLATR--RSLVLIDEFGKGTDTEDGAGLLIATIEHLLKRGPecpRVIVSTH 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489565927 486 DIELTEMITDYEN-----FHF------SEIVTDDEVTFDYKLKLGPSKTRNALK 528
Cdd:cd03281  153 FHELFNRSLLPERlkikfLTMevllnpTSTSPNEDITYLYRLVPGLADTSFAIH 206
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
 345-543 2.02e-17

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: 81.27  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 345 LENLYHPLVK-----NPIKNSISIKNNI----IFTGSNASGKSTFIKGIALNCILAQ-----SLNTALCSKYKCKFSKVV 410
Cdd:cd03285    2 LKEARHPCVEaqddvAFIPNDVTLTRGKsrflIITGPNMGGKSTYIRQIGVIVLMAQigcfvPCDSADIPIVDCILARVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 411 TSmairDNILLGESYFIAEIKSLKRLLDSlnGEIRVLAFIDEILKGTNTLERISSSASILKY-AKNTKAKLFVATHDIEL 489
Cdd:cd03285   82 AS----DSQLKGVSTFMAEMLETAAILKS--ATENSLIIIDELGRGTSTYDGFGLAWAIAEYiATQIKCFCLFATHFHEL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489565927 490 TEM---ITDYENFHFSEIVTD--DEVTFDYKLKLGPSKTRNALKLLKTFDFENEVICLA 543
Cdd:cd03285  156 TALadeVPNVKNLHVTALTDDasRTLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMA 214
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
 350-520 1.18e-16

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: 78.58  E-value: 1.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 350 HPLVKNPIKNSIsiKNNI----------IFTGSNASGKSTFIKGIALNCILAQsLNTALCSKYKCK--FSKVVTSMAIRD 417
Cdd:cd03282    7 HPILDRDKKNFI--PNDIyltrgssrfhIITGPNMSGKSTYLKQIALLAIMAQ-IGCFVPAEYATLpiFNRLLSRLSNDD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 418 NILLGESYFIAEIKSLKRLLDSLNGEIRVLafIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIELTEMITDYE 497
Cdd:cd03282   84 SMERNLSTFASEMSETAYILDYADGDSLVL--IDELGRGTSSADGFAISLAILECLIKKESTVFFATHFRDIAAILGNKS 161

                        170       180
                 ....*....|....*....|....*..
gi 489565927 498 ---NFHFS-EIVTDDEVTFDYKLKLGP 520
Cdd:cd03282  162 cvvHLHMKaQSINSNGIEMAYKLVLGL 188
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
 311-521 4.21e-16

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 81.68  E-value: 4.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 311 DIVAKLDFAMSLTfYRKSIDEYTIPEFTESEDIELENLYHP-----LVKNP-IKNSISIKNN---IIFTGSNASGKSTFI 381
Cdd:PRK05399 546 KALAELDVLASLA-EVAEENNYVRPEFTDDPGIDIEEGRHPvveqvLGGEPfVPNDCDLDEErrlLLITGPNMAGKSTYM 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 382 KGIALNCILAQ------------SLntalcskykckFSKVVTSMAIRDNILLGESYFIAEIKSLKRLL-----DSLngei 444
Cdd:PRK05399 625 RQVALIVLLAQigsfvpaesariGI-----------VDRIFTRIGASDDLASGRSTFMVEMTETANILnnateRSL---- 689

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 445 rVLafIDEILKGTNTLERISSSASILKY-AKNTKAK-LFvATHDIELTEMITDYE---NFHFSEIVTDDEVTFDYKLKLG 519
Cdd:PRK05399 690 -VL--LDEIGRGTSTYDGLSIAWAVAEYlHDKIGAKtLF-ATHYHELTELEEKLPgvkNVHVAVKEHGGDIVFLHKVVPG 765


                 ..
gi 489565927 520 PS 521
Cdd:PRK05399 766 AA 767
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
311-521 2.65e-15

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


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 79.33  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 311 DIVAKLDFAMSLTfYRKSIDEYTIPEFTESEDIELENLYHPLV-----KNP-IKNSISIKNN---IIFTGSNASGKSTFI 381
Cdd:COG0249  552 RALAELDVLASLA-EVAVENNYVRPELDDSPGIEIEGGRHPVVeqalpGEPfVPNDCDLDPDrriLLITGPNMAGKSTYM 630

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 382 KGIALNCILAQ--------SLNTALCSKYkckFSKVVTSmairDNILLGESYF------IAEI------KSLkrlldsln 441
Cdd:COG0249  631 RQVALIVLLAQigsfvpaeSARIGIVDRI---FTRVGAS----DDLARGQSTFmvemteTANIlnnateRSL-------- 695

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 442 geirVLafIDEILKGTNTLERISSSASILKY-AKNTKAK-LFvATHDIELTEMITDYE---NFHFSEIVTDDEVTFDYKL 516
Cdd:COG0249  696 ----VL--LDEIGRGTSTYDGLSIAWAVAEYlHDKIRARtLF-ATHYHELTELAEKLPgvkNYHVAVKEWGGDIVFLHKV 768


                 ....*
gi 489565927 517 KLGPS 521
Cdd:COG0249  769 VPGPA 773
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
 345-519 2.26e-14

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: 72.46  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 345 LENLYHPLVK-----NPIKNSI----SIKNNIIFTGSNASGKSTFIKGIALNCILAQsLNTALCSKyKCKFS---KVVTS 412
Cdd:cd03286    2 FEELRHPCLNastasSFVPNDVdlgaTSPRILVLTGPNMGGKSTLLRTVCLAVIMAQ-MGMDVPAK-SMRLSlvdRIFTR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 413 MAIRDNILLGESYFIAEIKSLKRLLDslNGEIRVLAFIDEILKGTNTLERISSSASILKY-AKNTKAKLFVATHDIELTE 491
Cdd:cd03286   80 IGARDDIMKGESTFMVELSETANILR--HATPDSLVILDELGRGTSTHDGYAIAHAVLEYlVKKVKCLTLFSTHYHSLCD 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489565927 492 MITDYENF---HFSEIV------TDDEVTFDYKLKLG 519
Cdd:cd03286  158 EFHEHGGVrlgHMACAVknesdpTIRDITFLYKLVAG 194
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
 368-519 2.59e-13

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: 69.44  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 368 IFTGSNASGKSTFIKGIALNCILAQSLNTALCSKYKCK-FSKVVTSMAIRDNILLGESYFIAEIKSLKRLLDSLNGeiRV 446
Cdd:cd03287   35 IITGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSiFDSVLTRMGASDSIQHGMSTFMVELSETSHILSNCTS--RS 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 447 LAFIDEILKGTNTLERISSSASILKY-AKNTKAKLFVATHDIELTEMITDYE----NFHFS--------EIVTDDEVTFD 513
Cdd:cd03287  113 LVILDELGRGTSTHDGIAIAYATLHYlLEEKKCLVLFVTHYPSLGEILRRFEgsirNYHMSylesqkdfETSDSQSITFL 192


                 ....*.
gi 489565927 514 YKLKLG 519
Cdd:cd03287  193 YKLVRG 198
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 298-489 2.34e-11

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 66.77  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 298 ILEKNKQNLYKIYDIVAKLDFAMSLTFYRKSIDeYTIPEFTESEDIELENLYHPLVKNPIKNSISI-----KNNIIFTGS 372
Cdd:PRK00409 257 KVAKNLDFLKFLNKIFDELDFIFARARYAKALK-ATFPLFNDEGKIDLRQARHPLLDGEKVVPKDIslgfdKTVLVITGP 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 373 NASGKSTFIKGIALNCILAQSL-------NTALCSkykckFSKVVTSM----AIRDNIllgeSYFIAEIKSLKRLLDSLN 441
Cdd:PRK00409 336 NTGGKTVTLKTLGLAALMAKSGlpipanePSEIPV-----FKEIFADIgdeqSIEQSL----STFSGHMTNIVRILEKAD 406

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 489565927 442 GEIRVLafIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIEL 489
Cdd:PRK00409 407 KNSLVL--FDELGAGTDPDEGAALAISILEYLRKRGAKIIATTHYKEL 452
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
 344-489 9.37e-10

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: 58.41  E-value: 9.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 344 ELENLYHPL----VKNPIKNSISIKNN---IIFTGSNASGKSTFIKGIALNCILAQSlNTALCSKYKCK---FSKVVTSM 413
Cdd:cd03280    1 RLREARHPLlplqGEKVVPLDIQLGENkrvLVITGPNAGGKTVTLKTLGLLTLMAQS-GLPIPAAEGSSlpvFENIFADI 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489565927 414 AIRDNILLGESYFIAEIKSLKRLLDSLNGEIRVLafIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIEL 489
Cdd:cd03280   80 GDEQSIEQSLSTFSSHMKNIARILQHADPDSLVL--LDELGSGTDPVEGAALAIAILEELLERGALVIATTHYGEL 153
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
302-485 1.85e-09

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 60.54  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 302 NKQNLYKIYDIVAKLDFAMSLTFYRKSIDeYTIPEFTESEDIELENLYHPL--VKNPIKNSISIKNN---IIFTGSNASG 376
Cdd:COG1193  259 YAEELLENLEILAELDFIFAKARYALELK-AVKPELNDEGYIKLKKARHPLldLKKVVPIDIELGEDfrtLVITGPNTGG 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 377 KSTFIKGIALNCILAQSlntAL---CSKYkckfskvvTSMAIRDNIL--LGE--------SYFIAEIKSLKRLLDSLNGE 443
Cdd:COG1193  338 KTVTLKTVGLLTLMAQS---GLpipAAEG--------SELPVFDNIFadIGDeqsieqslSTFSSHMTNIVEILEKADEN 406

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 489565927 444 IRVLafIDEILKGTNTLErisSSA---SILKYAKNTKAKLFVATH 485
Cdd:COG1193  407 SLVL--LDELGAGTDPQE---GAAlaiAILEELLERGARVVATTH 446
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 355-492 4.52e-08

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: 52.75  E-value: 4.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 355 NPIKNSISIKN---NIIfTGSNASGKSTFIKGIALNCILAQSLNT----ALCSKYKCKFSkvVTSMAIRDNILLGESyfi 427
Cdd:cd03227   10 YFVPNDVTFGEgslTII-TGPNGSGKSTILDAIGLALGGAQSATRrrsgVKAGCIVAAVS--AELIFTRLQLSGGEK--- 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489565927 428 aEIKSLKRLLDSLNGEIRVLAFIDEILKGTNTLERISSSASILKYAKNtKAKLFVATHDIELTEM 492
Cdd:cd03227   84 -ELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAEL 146
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 367-495 1.86e-04

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 43.17  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 367 IIFTGSNASGKSTFIKgialncILAQSLN-------TALCS-KYKCKFSKVVTSMAIRD------NILLGESYFIAEI-K 431
Cdd:cd03237   28 IGILGPNGIGKTTFIK------MLAGVLKpdegdieIELDTvSYKPQYIKADYEGTVRDllssitKDFYTHPYFKTEIaK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 432 SLK--RLLDSL-----NGEI-RV-----------LAFIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIELTEM 492
Cdd:cd03237  102 PLQieQILDREvpelsGGELqRVaiaaclskdadIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDY 181


                 ...
gi 489565927 493 ITD 495
Cdd:cd03237  182 LAD 184
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
371-495 1.57e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 41.33  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 371 GSNASGKSTFIKgialncILA-------QSLNTALCSKYKCKFSKVVTSMAIRDNI-----LLGESYFIAEIK---SLKR 435
Cdd:PRK13409 372 GPNGIGKTTFAK------LLAgvlkpdeGEVDPELKISYKPQYIKPDYDGTVEDLLrsitdDLGSSYYKSEIIkplQLER 445

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489565927 436 LLDS-LN----GEI-RV-----------LAFIDEILKGTNTLERISSSASILKYAKNTKAKLFVATHDIELTEMITD 495
Cdd:PRK13409 446 LLDKnVKdlsgGELqRVaiaaclsrdadLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISD 522
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 371-495 1.69e-03

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 41.31  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 371 GSNASGKSTFIKgialncILA-------QSLNTALCSKYKCKFSKVVTSMAIRDNI------LLGESYFIAEIK---SLK 434
Cdd:COG1245  373 GPNGIGKTTFAK------ILAgvlkpdeGEVDEDLKISYKPQYISPDYDGTVEEFLrsantdDFGSSYYKTEIIkplGLE 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489565927 435 RLLDS----LNG----------------EIRVL----AFID-EilkgtntlERISSSASILKYAKNTKAKLFVATHDIEL 489
Cdd:COG1245  447 KLLDKnvkdLSGgelqrvaiaaclsrdaDLYLLdepsAHLDvE--------QRLAVAKAIRRFAENRGKTAMVVDHDIYL 518


                 ....*.
gi 489565927 490 TEMITD 495
Cdd:COG1245  519 IDYISD 524
 
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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