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Conserved domains on  [gi|119596965|gb|EAW76559|]
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hCG2023604, isoform CRA_a, partial [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 ...
 17-87 6.58e-31

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: 110.42  E-value: 6.58e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119596965   17 KAIKPIDRKSVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEENFEGL 87
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLA 71
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 17-87 6.58e-31

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: 110.42  E-value: 6.58e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119596965   17 KAIKPIDRKSVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEENFEGL 87
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLA 71
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 26-91 9.18e-27

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: 96.74  E-value: 9.18e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119596965  26 SVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEENFEGL------SKLT 91
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAferhatSKIS 72
mutL PRK00095
DNA mismatch repair endonuclease MutL;
18-82 5.59e-18

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 77.18  E-value: 5.59e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119596965  18 AIKPIDRKSVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEE 82
Cdd:PRK00095   2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKE 66
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
27-82 8.06e-17

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 73.54  E-value: 8.06e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119596965  27 VHQICSGPVV--PSlStAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEE 82
Cdd:COG0323   12 ANQIAAGEVVerPA-S-VVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPE 67
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 39-95 1.03e-04

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: 38.47  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119596965   39 LSTAVKELVENSLDAGATNIDLKLKDY--GVDLIEVSGNGCGVEEENFEGLSKLTFSNP 95
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNrgGGTEIVIEDDGHGMSPEELINALRLATSAK 59
 
Name Accession Description Interval E-value
mutl TIGR00585
DNA mismatch repair protein MutL; All proteins in this family for which the functions are ...
 17-87 6.58e-31

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: 110.42  E-value: 6.58e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119596965   17 KAIKPIDRKSVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEENFEGL 87
Cdd:TIGR00585   1 MTIKPLPPELVNKIAAGEVIERPASVVKELVENSLDAGATRIDVEIEEGGLKLIEVSDNGSGIDKEDLPLA 71
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 26-91 9.18e-27

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: 96.74  E-value: 9.18e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119596965  26 SVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEENFEGL------SKLT 91
Cdd:cd16926    1 VVNKIAAGEVIERPASVVKELVENSIDAGATRIDVEIEEGGLKLIRVTDNGSGISREDLELAferhatSKIS 72
mutL PRK00095
DNA mismatch repair endonuclease MutL;
18-82 5.59e-18

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 77.18  E-value: 5.59e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119596965  18 AIKPIDRKSVHQICSGPVVPSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEE 82
Cdd:PRK00095   2 PIQLLPPQLANQIAAGEVVERPASVVKELVENALDAGATRIDIEIEEGGLKLIRVRDNGCGISKE 66
MutL COG0323
DNA mismatch repair ATPase MutL [Replication, recombination and repair];
27-82 8.06e-17

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


Pssm-ID: 440092 [Multi-domain]  Cd Length: 515  Bit Score: 73.54  E-value: 8.06e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119596965  27 VHQICSGPVV--PSlStAVKELVENSLDAGATNIDLKLKDYGVDLIEVSGNGCGVEEE 82
Cdd:COG0323   12 ANQIAAGEVVerPA-S-VVKELVENAIDAGATRIEVEIEEGGKSLIRVTDNGCGMSPE 67
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 39-95 1.03e-04

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: 38.47  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119596965   39 LSTAVKELVENSLDAGATNIDLKLKDY--GVDLIEVSGNGCGVEEENFEGLSKLTFSNP 95
Cdd:pfam13589   1 LEGALAELIDNSIDADATNIKIEVNKNrgGGTEIVIEDDGHGMSPEELINALRLATSAK 59
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
 38-83 1.89e-04

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 38.33  E-value: 1.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119596965  38 SLSTAVKELVENSLDAGATN-------IDLKLKDYGVDL--IEVSGNGCGVEEEN 83
Cdd:PRK04184  36 ALYTTVKELVDNSLDACEEAgilpdikIEIKRVDEGKDHyrVTVEDNGPGIPPEE 90
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 39-87 7.82e-04

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: 35.81  E-value: 7.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119596965   39 LSTAVKELVENSLD--AGATNIDLKLKDYGVDLIEVSGNGCGVEEENFEGL 87
Cdd:pfam02518   6 LRQVLSNLLDNALKhaAKAGEITVTLSEGGELTLTVEDNGIGIPPEDLPRI 56
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
 38-82 4.07e-03

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: 34.63  E-value: 4.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119596965  38 SLSTAVKELVENSLDAGAT-----NIDLKLKDYGVD--LIEVSGNGCGVEEE 82
Cdd:cd16933   19 SLYTTVRELVENSLDATEEagilpDIKVEIEEIGKDhyKVIVEDNGPGIPEE 70
HATPase_MORC-like cd16931
Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger ...
 42-82 8.28e-03

Histidine kinase-like ATPase domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of human microrchidia (MORC) family CW-type zinc finger proteins MORC1-4, and related domains. In addition to the HATPase domain, MORC family proteins have a CW-type zinc finger domain containing four conserved cysteines and two conserved tryptophans, and coiled-coil domains at the carboxy-terminus. MORC1 has cross-species differential methylation in association with early life stress, and genome-wide association with major depressive disorder (MDD). MORC2 is involved in several nuclear processes, including transcription modulation and DNA damage repair, and exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY. MORC3 regulates p53, and is an antiviral factor which plays an important role during HSV-1 and HCMV infection, and is a positive regulator of influenza virus transcription. MORC4 is highly expressed in a subset of diffuse large B-cell lymphomas and has potential as a lymphoma biomarker.


Pssm-ID: 340408 [Multi-domain]  Cd Length: 118  Bit Score: 33.15  E-value: 8.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119596965  42 AVKELVENSLDAGATN----IDLKLKDYGVDLIEVSGNGCGVEEE 82
Cdd:cd16931   15 AVAELVDNARDADATRldifIDDINLLRGGFMLSFLDDGNGMTPE 59
 
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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