NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568964139|ref|XP_006512326|]
View 

CTD small phosphatase-like protein isoform X2 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-108 3.97e-60

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 TIGR02251:

Pssm-ID: 473868  Cd Length: 162  Bit Score: 181.72  E-value: 3.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139    1 MGQLFECVLFTASLAKYADPVADLLDRWG-VFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:TIGR02251  54 VSKWYELVIFTASLEEYADPVLDILDRGGkVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAI 133

                          90       100
                  ....*....|....*....|....*....
gi 568964139   80 PVQSWFDDMTDTELLDLIPFFEGLSREDD 108
Cdd:TIGR02251 134 PIKSWFSDPNDTELLNLIPFLEGLRFEDD 162
 
Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 1-108 3.97e-60

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


Pssm-ID: 274055  Cd Length: 162  Bit Score: 181.72  E-value: 3.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139    1 MGQLFECVLFTASLAKYADPVADLLDRWG-VFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:TIGR02251  54 VSKWYELVIFTASLEEYADPVLDILDRGGkVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAI 133

                          90       100
                  ....*....|....*....|....*....
gi 568964139   80 PVQSWFDDMTDTELLDLIPFFEGLSREDD 108
Cdd:TIGR02251 134 PIKSWFSDPNDTELLNLIPFLEGLRFEDD 162
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 1-109 1.01e-47

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: 150.08  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139    1 MGQLFECVLFTASLAKYADPVADLLDRWGV-FRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:pfam03031  50 LSKYYEIVIFTASSKEYADPVLDILDPNGKlFSHRLYRESCKFEDGVYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGI 129

                          90       100       110
                  ....*....|....*....|....*....|
gi 568964139   80 PVQSWFDDMTDTELLDLIPFFEGLSREDDV 109
Cdd:pfam03031 130 PIPPFFGDPDDNELLKLLPFLEGLAGVDDV 159
CPDc smart00577
catalytic domain of ctd-like phosphatases;
1-91 4.20e-43

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 138.13  E-value: 4.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139     1 MGQLFECVLFTASLAKYADPVADLLDR-WGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:smart00577  57 ASELFELVVFTAGLRMYADPVLDLLDPkKYFGYRRLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLI 136

                           90
                   ....*....|..
gi 568964139    80 PVQSWFDDMTDT 91
Cdd:smart00577 137 PIKPWFGDPDDT 148
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 1-81 2.08e-40

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 130.79  E-value: 2.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139   1 MGQLFECVLFTASLAKYADPVADLLDRWG-VFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:cd07521   53 LSKLYEIVIFTAGTRAYADPVADKLDPNGlFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAI 132


                 ..
gi 568964139  80 PV 81
Cdd:cd07521  133 PI 134
 
Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 1-108 3.97e-60

Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031.


Pssm-ID: 274055  Cd Length: 162  Bit Score: 181.72  E-value: 3.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139    1 MGQLFECVLFTASLAKYADPVADLLDRWG-VFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:TIGR02251  54 VSKWYELVIFTASLEEYADPVLDILDRGGkVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAI 133

                          90       100
                  ....*....|....*....|....*....
gi 568964139   80 PVQSWFDDMTDTELLDLIPFFEGLSREDD 108
Cdd:TIGR02251 134 PIKSWFSDPNDTELLNLIPFLEGLRFEDD 162
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 1-109 1.01e-47

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: 150.08  E-value: 1.01e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139    1 MGQLFECVLFTASLAKYADPVADLLDRWGV-FRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:pfam03031  50 LSKYYEIVIFTASSKEYADPVLDILDPNGKlFSHRLYRESCKFEDGVYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGI 129

                          90       100       110
                  ....*....|....*....|....*....|
gi 568964139   80 PVQSWFDDMTDTELLDLIPFFEGLSREDDV 109
Cdd:pfam03031 130 PIPPFFGDPDDNELLKLLPFLEGLAGVDDV 159
CPDc smart00577
catalytic domain of ctd-like phosphatases;
1-91 4.20e-43

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 138.13  E-value: 4.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139     1 MGQLFECVLFTASLAKYADPVADLLDR-WGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:smart00577  57 ASELFELVVFTAGLRMYADPVLDLLDPkKYFGYRRLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLI 136

                           90
                   ....*....|..
gi 568964139    80 PVQSWFDDMTDT 91
Cdd:smart00577 137 PIKPWFGDPDDT 148
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 1-81 2.08e-40

human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319823  Cd Length: 134  Bit Score: 130.79  E-value: 2.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964139   1 MGQLFECVLFTASLAKYADPVADLLDRWG-VFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAV 79
Cdd:cd07521   53 LSKLYEIVIFTAGTRAYADPVADKLDPNGlFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAI 132


                 ..
gi 568964139  80 PV 81
Cdd:cd07521  133 PI 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH