NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|665392739|ref|NP_001285516|]
View 

dullard, isoform C [Drosophila melanogaster]

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 ...
 60-167 1.61e-36

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: 124.33  E-value: 1.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739   60 RKTLVLDLDETLIHShhnamprNTVKPGTPHDFTVKVTIDRNPVRFFVHKRPHVDYFLD--------VIF---------- 121
Cdd:TIGR02251   1 KKTLVLDLDETLVHS-------TFKMPKVDADFKVPVLIDGKIIQVYVFKRPHVDEFLErvskwyelVIFtasleeyadp 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739  122 -------------------------------------------IIDNSPGAYRCFPNNAIPIKSWFSDPMDTALLSLLPM 158
Cdd:TIGR02251  74 vldildrggkvisrrlyrescvftngkyvkdlslvgkdlskviIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPF 153


                  ....*....
gi 665392739  159 LDALRFTND 167
Cdd:TIGR02251 154 LEGLRFEDD 162
 
Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 60-167 1.61e-36

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: 124.33  E-value: 1.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739   60 RKTLVLDLDETLIHShhnamprNTVKPGTPHDFTVKVTIDRNPVRFFVHKRPHVDYFLD--------VIF---------- 121
Cdd:TIGR02251   1 KKTLVLDLDETLVHS-------TFKMPKVDADFKVPVLIDGKIIQVYVFKRPHVDEFLErvskwyelVIFtasleeyadp 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739  122 -------------------------------------------IIDNSPGAYRCFPNNAIPIKSWFSDPMDTALLSLLPM 158
Cdd:TIGR02251  74 vldildrggkvisrrlyrescvftngkyvkdlslvgkdlskviIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPF 153


                  ....*....
gi 665392739  159 LDALRFTND 167
Cdd:TIGR02251 154 LEGLRFEDD 162
CPDc smart00577
catalytic domain of ctd-like phosphatases;
59-150 4.73e-26

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 96.91  E-value: 4.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739    59 QRKTLVLDLDETLIHSHHNamprnTVKPGTPHDFTVKVTIDRNPVRFFVHKRPHVDYFLD--------VIF--------- 121
Cdd:smart00577   1 KKKTLVLDLDETLVHSTHR-----SFKEWTNRDFIVPVLIDGHPHGVYVKKRPGVDEFLKraselfelVVFtaglrmyad 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665392739   122 --------------------------------------------IIDNSPGAYRCFPNNAIPIKSWFSDPMDT 150
Cdd:smart00577  76 pvldlldpkkyfgyrrlfrdecvfvkgkyvkdlsllnrdlskviIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 61-169 2.42e-23

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: 90.37  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739   61 KTLVLDLDETLIHShhnamprnTVKPGTPHDFTVKVtiDRNPVRFFVHKRPHVDYFLD--------VIF----------- 121
Cdd:pfam03031   1 KTLVLDLDETLVHS--------SFEPPLKSDFILPV--PGETHGGYVKKRPGLDEFLKelskyyeiVIFtasskeyadpv 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739  122 ------------------------------------------IIDNSPGAYRCFPNNAIPIKSWFSDPMDTALLSLLPML 159
Cdd:pfam03031  71 ldildpngklfshrlyresckfedgvyvkdlsllgrdlsrvvIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFL 150

                         170
                  ....*....|
gi 665392739  160 DALRFTNDVR 169
Cdd:pfam03031 151 EGLAGVDDVR 160
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 60-140 1.38e-15

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: 69.55  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739  60 RKTLVLDLDETLIHSHHnamprntvKPGTPHDFTVKVTIDRNPVRFFVHKRPHVDYFLD--------VIF---------- 121
Cdd:cd07521    1 KLTLVLDLDETLVHSTW--------KPVLSEDFKIPVLPDGREHGYYVKKRPGVDEFLErlsklyeiVIFtagtrayadp 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665392739 122 -------------------------------------------IIDNSPGAYRCFPNNAIPI 140
Cdd:cd07521   73 vadkldpnglfidrrlfrdscvyvdgnyvkdlsklfrdlskvvIIDDSPGSYWLQPENAIPI 134
 
Name Accession Description Interval E-value
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 60-167 1.61e-36

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: 124.33  E-value: 1.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739   60 RKTLVLDLDETLIHShhnamprNTVKPGTPHDFTVKVTIDRNPVRFFVHKRPHVDYFLD--------VIF---------- 121
Cdd:TIGR02251   1 KKTLVLDLDETLVHS-------TFKMPKVDADFKVPVLIDGKIIQVYVFKRPHVDEFLErvskwyelVIFtasleeyadp 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739  122 -------------------------------------------IIDNSPGAYRCFPNNAIPIKSWFSDPMDTALLSLLPM 158
Cdd:TIGR02251  74 vldildrggkvisrrlyrescvftngkyvkdlslvgkdlskviIIDNSPYSYSLQPDNAIPIKSWFSDPNDTELLNLIPF 153


                  ....*....
gi 665392739  159 LDALRFTND 167
Cdd:TIGR02251 154 LEGLRFEDD 162
CPDc smart00577
catalytic domain of ctd-like phosphatases;
59-150 4.73e-26

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 96.91  E-value: 4.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739    59 QRKTLVLDLDETLIHSHHNamprnTVKPGTPHDFTVKVTIDRNPVRFFVHKRPHVDYFLD--------VIF--------- 121
Cdd:smart00577   1 KKKTLVLDLDETLVHSTHR-----SFKEWTNRDFIVPVLIDGHPHGVYVKKRPGVDEFLKraselfelVVFtaglrmyad 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665392739   122 --------------------------------------------IIDNSPGAYRCFPNNAIPIKSWFSDPMDT 150
Cdd:smart00577  76 pvldlldpkkyfgyrrlfrdecvfvkgkyvkdlsllnrdlskviIIDDSPDSWPFHPENLIPIKPWFGDPDDT 148
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 61-169 2.42e-23

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: 90.37  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739   61 KTLVLDLDETLIHShhnamprnTVKPGTPHDFTVKVtiDRNPVRFFVHKRPHVDYFLD--------VIF----------- 121
Cdd:pfam03031   1 KTLVLDLDETLVHS--------SFEPPLKSDFILPV--PGETHGGYVKKRPGLDEFLKelskyyeiVIFtasskeyadpv 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739  122 ------------------------------------------IIDNSPGAYRCFPNNAIPIKSWFSDPMDTALLSLLPML 159
Cdd:pfam03031  71 ldildpngklfshrlyresckfedgvyvkdlsllgrdlsrvvIVDNSPDSFLLQPDNGIPIPPFFGDPDDNELLKLLPFL 150

                         170
                  ....*....|
gi 665392739  160 DALRFTNDVR 169
Cdd:pfam03031 151 EGLAGVDDVR 160
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 60-140 1.38e-15

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: 69.55  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665392739  60 RKTLVLDLDETLIHSHHnamprntvKPGTPHDFTVKVTIDRNPVRFFVHKRPHVDYFLD--------VIF---------- 121
Cdd:cd07521    1 KLTLVLDLDETLVHSTW--------KPVLSEDFKIPVLPDGREHGYYVKKRPGVDEFLErlsklyeiVIFtagtrayadp 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665392739 122 -------------------------------------------IIDNSPGAYRCFPNNAIPI 140
Cdd:cd07521   73 vadkldpnglfidrrlfrdscvyvdgnyvkdlsklfrdlskvvIIDDSPGSYWLQPENAIPI 134
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 57-117 3.96e-03

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: 36.10  E-value: 3.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665392739   57 LVQRK-TLVLDLDETLIHS--HHNAMPRNTVKPGTPHDFTVK--VTIDRNPVRFFVHKRPHVDYFL 117
Cdd:TIGR02250   2 LREKKlHLVLDLDQTLIHTtkDPTLSEWEKYDIEEPNSETRRdlRKFNLGTMWYLTKLRPFLHEFL 67
 
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