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Conserved domains on  [gi|1005261254|ref|NP_001307980|]
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PMS1 protein homolog 1 isoform h [Homo sapiens]

Protein Classification

DNA mismatch repair MutL family protein( domain architecture ID 1001378)

DNA mismatch repair MutL family protein is required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage, or recombination events

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mutl super family cl36694
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-140 3.85e-68

DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00585:

Pssm-ID: 273155 [Multi-domain]  Cd Length: 312  Bit Score: 209.03  E-value: 3.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   1 MKQLPAATVRLLSSSQIITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINS 80
Cdd:TIGR00585   3 IKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005261254  81 HEDLENLTTYGFRGEALGSICCIAEVLITTRT-AADNFSTQYVLDGsGHILSQKPSHLGQG 140
Cdd:TIGR00585  83 FEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEG-GMIESIKPAPRPVG 142
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-140 3.85e-68

DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273155 [Multi-domain]  Cd Length: 312  Bit Score: 209.03  E-value: 3.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   1 MKQLPAATVRLLSSSQIITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINS 80
Cdd:TIGR00585   3 IKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005261254  81 HEDLENLTTYGFRGEALGSICCIAEVLITTRT-AADNFSTQYVLDGsGHILSQKPSHLGQG 140
Cdd:TIGR00585  83 FEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEG-GMIESIKPAPRPVG 142
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 8-140 5.22e-65

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 196.89  E-value: 5.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   8 TVRLLSSSQIITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINSHEDLENL 87
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1005261254  88 TTYGFRGEALGSICCIAEVLITTRTAADNFSTQYVLDGSGHILSQKPSHLGQG 140
Cdd:cd16926    81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVG 133
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
2-140 3.80e-44

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 152.12  E-value: 3.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   2 KQLPAATVrllssSQI-----ITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPvMA-MKYYT 75
Cdd:COG0323     5 RLLPDELA-----NQIaagevVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLP-LAfERHAT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005261254  76 SKINSHEDLENLTTYGFRGEALGSICCIAEVLITTRTAADNFSTQYVLDGsGHILSQKPSHLGQG 140
Cdd:COG0323    79 SKIRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEG-GKVVEVEPAAAPKG 142
mutL PRK00095
DNA mismatch repair endonuclease MutL;
2-141 4.39e-41

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 144.97  E-value: 4.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   2 KQLPAATVrllssSQI-----ITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTS 76
Cdd:PRK00095    4 QLLPPQLA-----NQIaagevVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATS 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005261254  77 KINSHEDLENLTTYGFRGEALGSICCIAEVLITTRTAADNFSTQYVLDGsGHILSQKPSHLGQGS 141
Cdd:PRK00095   79 KIASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEG-GEIVEVKPAAHPVGT 142
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 24-82 6.78e-07

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 45.44  E-value: 6.78e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005261254  24 VVKELIENSLD--AGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINSHE 82
Cdd:pfam02518   9 VLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG 69
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 24-82 4.05e-04

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 38.01  E-value: 4.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005261254   24 VVKELIENSLDAGATS--VDVKLENYGFD-KIEVRDNGEGIKAVDAPVMAMKYYTSKINSHE 82
Cdd:smart00387   9 VLSNLLDNAIKYTPEGgrITVTLERDGDHvEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK 70
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 1-140 3.85e-68

DNA mismatch repair protein MutL; All proteins in this family for which the functions are known are involved in the process of generalized mismatch repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273155 [Multi-domain]  Cd Length: 312  Bit Score: 209.03  E-value: 3.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   1 MKQLPAATVRLLSSSQIITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINS 80
Cdd:TIGR00585   3 IKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLACERHATSKIQS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005261254  81 HEDLENLTTYGFRGEALGSICCIAEVLITTRT-AADNFSTQYVLDGsGHILSQKPSHLGQG 140
Cdd:TIGR00585  83 FEDLERIETLGFRGEALASISSVSRLTITTKTsAADGLAYQALLEG-GMIESIKPAPRPVG 142
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 8-140 5.22e-65

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 196.89  E-value: 5.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   8 TVRLLSSSQIITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINSHEDLENL 87
Cdd:cd16926     1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAFERHATSKISSFEDLFSI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1005261254  88 TTYGFRGEALGSICCIAEVLITTRTAADNFSTQYVLDGSGHILSQKPSHLGQG 140
Cdd:cd16926    81 TTLGFRGEALASIASVSRLTITTRTADDDVGTRLVVDGGGIIEEVKPAAAPVG 133
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
2-140 3.80e-44

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 152.12  E-value: 3.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   2 KQLPAATVrllssSQI-----ITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPvMA-MKYYT 75
Cdd:COG0323     5 RLLPDELA-----NQIaagevVERPASVVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPEDLP-LAfERHAT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005261254  76 SKINSHEDLENLTTYGFRGEALGSICCIAEVLITTRTAADNFSTQYVLDGsGHILSQKPSHLGQG 140
Cdd:COG0323    79 SKIRSAEDLFRIRTLGFRGEALASIASVSRLTLTTRTAGAELGTRIEVEG-GKVVEVEPAAAPKG 142
mutL PRK00095
DNA mismatch repair endonuclease MutL;
2-141 4.39e-41

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 144.97  E-value: 4.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   2 KQLPAATVrllssSQI-----ITSVVSVVKELIENSLDAGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTS 76
Cdd:PRK00095    4 QLLPPQLA-----NQIaagevVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKEDLALALARHATS 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005261254  77 KINSHEDLENLTTYGFRGEALGSICCIAEVLITTRTAADNFSTQYVLDGsGHILSQKPSHLGQGS 141
Cdd:PRK00095   79 KIASLDDLEAIRTLGFRGEALPSIASVSRLTLTSRTADAAEGWQIVYEG-GEIVEVKPAAHPVGT 142
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 24-82 6.78e-07

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 45.44  E-value: 6.78e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005261254  24 VVKELIENSLD--AGATSVDVKLENYGFDKIEVRDNGEGIKAVDAPVMAMKYYTSKINSHE 82
Cdd:pfam02518   9 VLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGG 69
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 23-112 1.41e-05

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 42.32  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254  23 SVVKELIENSLDAGATSVDVKLENY--GFDKIEVRDNGEGIKAVDApVMAMKYYTSKINSHEDLENLTTYGFrGEALGSI 100
Cdd:pfam13589   3 GALAELIDNSIDADATNIKIEVNKNrgGGTEIVIEDDGHGMSPEEL-INALRLATSAKEAKRGSTDLGRYGI-GLKLASL 80

                          90
                  ....*....|..
gi 1005261254 101 CCIAEVLITTRT 112
Cdd:pfam13589  81 SLGAKLTVTSKK 92
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
 20-77 9.07e-05

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 41.42  E-value: 9.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261254  20 SVVSVVKELIENSLDAGATS-------VDVKLENYGFD--KIEVRDNGEGI-KAVDAPVMAMKYYTSK 77
Cdd:PRK04184   36 ALYTTVKELVDNSLDACEEAgilpdikIEIKRVDEGKDhyRVTVEDNGPGIpPEEIPKVFGKLLYGSK 103
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
 18-77 1.55e-04

Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.


Pssm-ID: 340410 [Multi-domain]  Cd Length: 203  Bit Score: 40.41  E-value: 1.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261254  18 ITSVVSVVKELIENSLDAGATS-------VDVKLENYGFDKIEVRDNGEGIKAVDAP-VMAMKYYTSK 77
Cdd:cd16933    17 IRSLYTTVRELVENSLDATEEAgilpdikVEIEEIGKDHYKVIVEDNGPGIPEEQIPkVFGKVLYGSK 84
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 24-82 4.05e-04

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 38.01  E-value: 4.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005261254   24 VVKELIENSLDAGATS--VDVKLENYGFD-KIEVRDNGEGIKAVDAPVMAMKYYTSKINSHE 82
Cdd:smart00387   9 VLSNLLDNAIKYTPEGgrITVTLERDGDHvEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRK 70
HATPase_GyrB-like cd16928
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ...
 25-61 6.75e-04

Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes histidine kinase-like ATPase domain of the B subunit of DNA gyrase. Bacterial DNA gyrase is a type II topoisomerase (type II as it transiently cleaves both strands of DNA) which catalyzes the introduction of negative supercoils into DNA, possibly by a mechanism in which one segment of the double-stranded DNA substrate is passed through a transient break in a second segment. It consists of GyrA and GyrB subunits in an A2B2 stoichiometry; GyrA subunits catalyze strand-breakage and reunion reactions, and GyrB subunits hydrolyze ATP. DNA gyrase is found in bacteria, plants and archaea, but as it is absent in humans it is a possible drug target for the treatment of bacterial and parasite infections.


Pssm-ID: 340405 [Multi-domain]  Cd Length: 180  Bit Score: 38.29  E-value: 6.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1005261254  25 VKELIENSLD---AG-ATSVDVKLENYGFdkIEVRDNGEGI 61
Cdd:cd16928     5 VWEIVDNSIDealAGyATEIEVTLHEDNS--ITVEDNGRGI 43
PRK14867 PRK14867
DNA topoisomerase VI subunit B; Provisional
 11-61 9.28e-04

DNA topoisomerase VI subunit B; Provisional


Pssm-ID: 237841 [Multi-domain]  Cd Length: 659  Bit Score: 38.64  E-value: 9.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261254  11 LLSSSQIITSVVSVVKELIENSLDAGATS-----VDVKLENYGFD--KIEVRDNGEGI 61
Cdd:PRK14867   27 MLGYSGKLRSMTTIIHELVTNSLDACEEAeilpdIKVEIEKLGSDhyKVAVEDNGPGI 84
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 21-81 1.26e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 36.50  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261254  21 VVSVVKELIENSLDAGATS------VDVKLENYGFD-KIEVRDNGEGIKAVDAPVMAMKYYTSKINSH 81
Cdd:cd16915     1 LITIVGNLIDNALDALAATgapnkqVEVFLRDEGDDlVIEVRDTGPGIAPELRDKVFERGVSTKGQGE 68
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 21-81 1.37e-03

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 37.91  E-value: 1.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005261254  21 VVSVVKELIENSLDAGATS------VDVKLENYGFD-KIEVRDNGEGIKAVDAPVMAMKYYTSKINSH 81
Cdd:COG3290   282 LVTILGNLLDNAIEAVEKLpeeerrVELSIRDDGDElVIEVEDSGPGIPEELLEKIFERGFSTKLGEG 349
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 3-77 3.78e-03

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 36.81  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261254   3 QLPAAtvrllSSSQIITSVVSVVKELIENSLDA------GATSVDVKLENyGFDKIEVRDNGEGIKAVDAPVMAMKYYTS 76
Cdd:PRK11086  421 QLPDS-----GDEDQVHELITILGNLIENALEAvggeegGEISVSLHYRN-GWLHCEVSDDGPGIAPDEIDAIFDKGYST 494


                  .
gi 1005261254  77 K 77
Cdd:PRK11086  495 K 495
 
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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