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Conserved domains on  [gi|334184730|ref|NP_181194|]
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haloacid dehalogenase-like hydrolase family protein [Arabidopsis thaliana]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
33-110 2.56e-05

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member pfam03031:

Pssm-ID: 473868  Cd Length: 160  Bit Score: 41.45  E-value: 2.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334184730   33 DKPLFFKDLSKVfqcfkGFSASNTIFIEEEPYKALLNPDNtGVFPLSYDPSDTKDNLLDPegefCSYLDGLANSSDVQ 110
Cdd:pfam03031  93 EDGVYVKDLSLL-----GRDLSRVVIVDNSPDSFLLQPDN-GIPIPPFFGDPDDNELLKL----LPFLEGLAGVDDVR 160
 
Name Accession Description Interval E-value
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
33-110 2.56e-05

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 41.45  E-value: 2.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334184730   33 DKPLFFKDLSKVfqcfkGFSASNTIFIEEEPYKALLNPDNtGVFPLSYDPSDTKDNLLDPegefCSYLDGLANSSDVQ 110
Cdd:pfam03031  93 EDGVYVKDLSLL-----GRDLSRVVIVDNSPDSFLLQPDN-GIPIPPFFGDPDDNELLKL----LPFLEGLAGVDDVR 160
 
Name Accession Description Interval E-value
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
33-110 2.56e-05

NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain.


Pssm-ID: 397254  Cd Length: 160  Bit Score: 41.45  E-value: 2.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334184730   33 DKPLFFKDLSKVfqcfkGFSASNTIFIEEEPYKALLNPDNtGVFPLSYDPSDTKDNLLDPegefCSYLDGLANSSDVQ 110
Cdd:pfam03031  93 EDGVYVKDLSLL-----GRDLSRVVIVDNSPDSFLLQPDN-GIPIPPFFGDPDDNELLKL----LPFLEGLAGVDDVR 160
 
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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