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Conserved domains on  [gi|31873112|emb|CAD30428|]
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CTD small phosphatase-like protein 1 [Caenorhabditis elegans]

Protein Classification

dullard-like phosphatase domain-containing protein( domain architecture ID 10020532)

dullard-like phosphatase domain-containing protein similar to Homo sapiens CTD nuclear envelope phosphatase 1( also known as dullard), which functions as a serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 165-319 3.25e-79

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: 239.12  E-value: 3.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   165 KKCLVIDLDETLVHSSFKPVKN-PDFVIPVEIDGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADLLD- 242
Cdd:TIGR02251   1 KKTLVLDLDETLVHSTFKMPKVdADFKVPVLIDGKIIQVYVFKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDr 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31873112   243 KKRVFRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPVTTWFDDPSDTELLDILPSLEHL 319
Cdd:TIGR02251  81 GGKVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFLEGL 157
 
Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 165-319 3.25e-79

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: 239.12  E-value: 3.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   165 KKCLVIDLDETLVHSSFKPVKN-PDFVIPVEIDGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADLLD- 242
Cdd:TIGR02251   1 KKTLVLDLDETLVHSTFKMPKVdADFKVPVLIDGKIIQVYVFKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDr 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31873112   243 KKRVFRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPVTTWFDDPSDTELLDILPSLEHL 319
Cdd:TIGR02251  81 GGKVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFLEGL 157
CPDc smart00577
catalytic domain of ctd-like phosphatases;
164-307 3.05e-73

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 223.26  E-value: 3.05e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112    164 NKKCLVIDLDETLVHS---SFKPVKNPDFVIPVEIDGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADL 240
Cdd:smart00577   1 KKKTLVLDLDETLVHSthrSFKEWTNRDFIVPVLIDGHPHGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31873112    241 LD-KKRVFRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPVTTWFDDPSDT 307
Cdd:smart00577  81 LDpKKYFGYRRLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 166-325 7.11e-72

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: 220.19  E-value: 7.11e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   166 KCLVIDLDETLVHSSFKPVKNPDFVIPVEidGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADLLDKKR 245
Cdd:pfam03031   1 KTLVLDLDETLVHSSFEPPLKSDFILPVP--GETHGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILDPNG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   246 V-FRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPVTTWFDDPSDTELLDILPSLEHLNGFSS 324
Cdd:pfam03031  79 KlFSHRLYRESCKFEDGVYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFLEGLAGVDD 158


                  .
gi 31873112   325 I 325
Cdd:pfam03031 159 V 159
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 165-297 5.88e-70

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: 214.38  E-value: 5.88e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112 165 KKCLVIDLDETLVHSSFKPVKNPDFVIPVEIDGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADLLDKK 244
Cdd:cd07521   1 KLTLVLDLDETLVHSTWKPVLSEDFKIPVLPDGREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDPN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 31873112 245 R-VFRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPV 297
Cdd:cd07521  81 GlFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAIPI 134
 
Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 165-319 3.25e-79

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: 239.12  E-value: 3.25e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   165 KKCLVIDLDETLVHSSFKPVKN-PDFVIPVEIDGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADLLD- 242
Cdd:TIGR02251   1 KKTLVLDLDETLVHSTFKMPKVdADFKVPVLIDGKIIQVYVFKRPHVDEFLERVSKWYELVIFTASLEEYADPVLDILDr 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31873112   243 KKRVFRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPVTTWFDDPSDTELLDILPSLEHL 319
Cdd:TIGR02251  81 GGKVISRRLYRESCVFTNGKYVKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPFLEGL 157
CPDc smart00577
catalytic domain of ctd-like phosphatases;
164-307 3.05e-73

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 223.26  E-value: 3.05e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112    164 NKKCLVIDLDETLVHS---SFKPVKNPDFVIPVEIDGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADL 240
Cdd:smart00577   1 KKKTLVLDLDETLVHSthrSFKEWTNRDFIVPVLIDGHPHGVYVKKRPGVDEFLKRASELFELVVFTAGLRMYADPVLDL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31873112    241 LD-KKRVFRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPVTTWFDDPSDT 307
Cdd:smart00577  81 LDpKKYFGYRRLFRDECVFVKGKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 166-325 7.11e-72

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: 220.19  E-value: 7.11e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   166 KCLVIDLDETLVHSSFKPVKNPDFVIPVEidGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADLLDKKR 245
Cdd:pfam03031   1 KTLVLDLDETLVHSSFEPPLKSDFILPVP--GETHGGYVKKRPGLDEFLKELSKYYEIVIFTASSKEYADPVLDILDPNG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   246 V-FRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPVTTWFDDPSDTELLDILPSLEHLNGFSS 324
Cdd:pfam03031  79 KlFSHRLYRESCKFEDGVYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFLEGLAGVDD 158


                  .
gi 31873112   325 I 325
Cdd:pfam03031 159 V 159
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 165-297 5.88e-70

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: 214.38  E-value: 5.88e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112 165 KKCLVIDLDETLVHSSFKPVKNPDFVIPVEIDGVEHQVYVLKRPYVDEFLAKVGEHFECILFTASLAKYADPVADLLDKK 244
Cdd:cd07521   1 KLTLVLDLDETLVHSTWKPVLSEDFKIPVLPDGREHGYYVKKRPGVDEFLERLSKLYEIVIFTAGTRAYADPVADKLDPN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 31873112 245 R-VFRGRLFREACVFHKGNYVKDLSRLGRNLNQTLIIDNSPASYAFHPENAVPV 297
Cdd:cd07521  81 GlFIDRRLFRDSCVYVDGNYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAIPI 134
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 168-298 2.28e-10

FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. 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 (hhhhDDppphW). 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 the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031.


Pssm-ID: 131304  Cd Length: 156  Bit Score: 58.44  E-value: 2.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   168 LVIDLDETLVHSSFKPV---------KNPDFVIPVEIDGVEH---QVYVLKRPYVDEFLAKVGEHFECILFTASLAKYAD 235
Cdd:TIGR02250   9 LVLDLDQTLIHTTKDPTlsewekydiEEPNSETRRDLRKFNLgtmWYLTKLRPFLHEFLKEASKLYEMHVYTMGTRAYAQ 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31873112   236 PVADLLD-KKRVFRGR-LFREACvfhKGNYVKDLSRL-GRNLNQTLIIDNSPASYAFHPENAVPVT 298
Cdd:TIGR02250  89 AIAKLIDpDGKYFGDRiISRDES---GSPHTKSLLRLfPADESMVVIIDDREDVWPWHKRNLIQIE 151
HAD_IIID1 TIGR02245
HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to ...
 164-233 1.34e-03

HAD-superfamily subfamily IIID hydrolase, TIGR02245; This family of sequences appears to belong to the Haloacid Dehalogenase (HAD) superfamily of enzymes by virtue of the presence of three catalytic domains, in this case: LLVLD(ILV)D(YH)T, I(VMG)IWS, and (DN)(VC)K(PA)Lx{15-17}T(IL)(MH)(FV)DD(IL)(GRS)(RK)N. Since this family has no large "cap" domain between motifs 1 and 2 or between 2 and 3, it is formally a "class III" HAD.


Pssm-ID: 131299  Cd Length: 195  Bit Score: 39.42  E-value: 1.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31873112   164 NKKCLVIDLDETLVhssfkpvknpDFVIPVEiDGVEhqvyvLKRPYVDEFLAKVGEHFECILFTASLAKY 233
Cdd:TIGR02245  20 GKKLLVLDIDYTLF----------DHRSPAE-TGEE-----LMRPYLHEFLTSAYEDYDIVIWSATSMKW 73
 
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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