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Conserved domains on  [gi|2470626058|ref|XP_054558260|]
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magnesium-dependent_phosphatase-1 [Candidozyma auris]

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 ...
3-167 1.37e-58

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 pfam12689:

Pssm-ID: 473868  Cd Length: 169  Bit Score: 180.50  E-value: 1.37e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058   3 PKAIVLDLDYTIWPCWCDTHLSLPLSKASKT-GIEDGRGFKLYLFDDVSSIVKLLSNSGVILIAASRTARPDIAEKLLTL 81
Cdd:pfam12689   3 PKLIVFDLDYTLWPFWVDTHVSPPFKKVSNGsRVVDRRGEELSLYPDVPSILQELKTRGVTLAAASRTDAPDWARELLKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058  82 FHIDDKP-----LISFFRSLQWGQGSKINHVEKaaceLHIEEELRRGDVILFDDEARNRDVE-EVNCYFFKINQneGLTF 155
Cdd:pfam12689  83 LHINDGPgdtvpAIDYFDDLEIYPGSKTKHFTK----ILKKSGIPYSDMLFFDDESRNIDVVsRLGVTFVLVPD--GLTR 156
                         170
                  ....*....|..
gi 2470626058 156 PVFNEALEVWRK 167
Cdd:pfam12689 157 EEFERGLRKWRK 168
 
Name Accession Description Interval E-value
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
3-167 1.37e-58

Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase.


Pssm-ID: 372256  Cd Length: 169  Bit Score: 180.50  E-value: 1.37e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058   3 PKAIVLDLDYTIWPCWCDTHLSLPLSKASKT-GIEDGRGFKLYLFDDVSSIVKLLSNSGVILIAASRTARPDIAEKLLTL 81
Cdd:pfam12689   3 PKLIVFDLDYTLWPFWVDTHVSPPFKKVSNGsRVVDRRGEELSLYPDVPSILQELKTRGVTLAAASRTDAPDWARELLKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058  82 FHIDDKP-----LISFFRSLQWGQGSKINHVEKaaceLHIEEELRRGDVILFDDEARNRDVE-EVNCYFFKINQneGLTF 155
Cdd:pfam12689  83 LHINDGPgdtvpAIDYFDDLEIYPGSKTKHFTK----ILKKSGIPYSDMLFFDDESRNIDVVsRLGVTFVLVPD--GLTR 156
                         170
                  ....*....|..
gi 2470626058 156 PVFNEALEVWRK 167
Cdd:pfam12689 157 EEFERGLRKWRK 168
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
3-141 3.12e-28

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. This family belongs 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 101.65  E-value: 3.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058   3 PKAIVLDLDYTIWPCWCDTHLSLPlskasktgIEDGRGFKLYLFDDVSSIVKLLSNSGVILIAASRTARPDIAEKLLTLF 82
Cdd:cd07501     1 PKCLVFDLDYTLWPGVVDEHGIPP--------FKDRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDHANEVLEKL 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2470626058  83 hiddkPLISFFRSLQWGQGSKINHVEKAACELHIEEElrrgDVILFDDEARNRDVEEVN 141
Cdd:cd07501    73 -----DLKELFDAFEIYPGSKSSHFRKIAKELGIGFD----SMVFFDDEPRNREEVSEG 122
MDP-1 TIGR01685
magnesium-dependent phosphatase-1; This model represents two closely related clades of ...
3-166 3.45e-25

magnesium-dependent phosphatase-1; This model represents two closely related clades of sequences from eukaryotes and archaea. The mouse enzyme has been characterized as a phosphatase and has been positively identified as a member of the haloacid dehalogenase (HAD) superfamily by site-directed mutagenesis of the active site residues.


Pssm-ID: 273756  Cd Length: 174  Bit Score: 95.30  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058   3 PKAIVLDLDYTIWPCWCDTHLSLP--LSKASKTGIEDGRGFKLYLFDDVSSIVKLLSNSGVILIAASRTARPDIAEKLLT 80
Cdd:TIGR01685   2 PRVIVFDLDGTLWDHYMISLLGGPfkPVKQNNSIIIDKSGTEVTLIKEVRDVLQTLKDAGTYLATASWNDVPEWAYEILG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058  81 LFHID----DKPLISFFRSLQWG-QGSKINHVEKAACELHIEE--ELRRGDVILFDDEARNrdVEEVNCYFFKINQNE-G 152
Cdd:TIGR01685  82 TFEITyagkTVPMHSLFDDRIEIyKPNKAKQLEMILQKVNKVDpsVLKPAQILFFDDRTDN--VREVWGYGVTSCYCPsG 159
                         170
                  ....*....|....
gi 2470626058 153 LTFPVFNEALEVWR 166
Cdd:TIGR01685 160 MDKGTFKKILEMWR 173
 
Name Accession Description Interval E-value
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
3-167 1.37e-58

Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase.


Pssm-ID: 372256  Cd Length: 169  Bit Score: 180.50  E-value: 1.37e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058   3 PKAIVLDLDYTIWPCWCDTHLSLPLSKASKT-GIEDGRGFKLYLFDDVSSIVKLLSNSGVILIAASRTARPDIAEKLLTL 81
Cdd:pfam12689   3 PKLIVFDLDYTLWPFWVDTHVSPPFKKVSNGsRVVDRRGEELSLYPDVPSILQELKTRGVTLAAASRTDAPDWARELLKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058  82 FHIDDKP-----LISFFRSLQWGQGSKINHVEKaaceLHIEEELRRGDVILFDDEARNRDVE-EVNCYFFKINQneGLTF 155
Cdd:pfam12689  83 LHINDGPgdtvpAIDYFDDLEIYPGSKTKHFTK----ILKKSGIPYSDMLFFDDESRNIDVVsRLGVTFVLVPD--GLTR 156
                         170
                  ....*....|..
gi 2470626058 156 PVFNEALEVWRK 167
Cdd:pfam12689 157 EEFERGLRKWRK 168
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
3-141 3.12e-28

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. This family belongs 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 101.65  E-value: 3.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058   3 PKAIVLDLDYTIWPCWCDTHLSLPlskasktgIEDGRGFKLYLFDDVSSIVKLLSNSGVILIAASRTARPDIAEKLLTLF 82
Cdd:cd07501     1 PKCLVFDLDYTLWPGVVDEHGIPP--------FKDRGGKEVSLYPDAQEILKELKERGILLAVASRNNEFDHANEVLEKL 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2470626058  83 hiddkPLISFFRSLQWGQGSKINHVEKAACELHIEEElrrgDVILFDDEARNRDVEEVN 141
Cdd:cd07501    73 -----DLKELFDAFEIYPGSKSSHFRKIAKELGIGFD----SMVFFDDEPRNREEVSEG 122
MDP-1 TIGR01685
magnesium-dependent phosphatase-1; This model represents two closely related clades of ...
3-166 3.45e-25

magnesium-dependent phosphatase-1; This model represents two closely related clades of sequences from eukaryotes and archaea. The mouse enzyme has been characterized as a phosphatase and has been positively identified as a member of the haloacid dehalogenase (HAD) superfamily by site-directed mutagenesis of the active site residues.


Pssm-ID: 273756  Cd Length: 174  Bit Score: 95.30  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058   3 PKAIVLDLDYTIWPCWCDTHLSLP--LSKASKTGIEDGRGFKLYLFDDVSSIVKLLSNSGVILIAASRTARPDIAEKLLT 80
Cdd:TIGR01685   2 PRVIVFDLDGTLWDHYMISLLGGPfkPVKQNNSIIIDKSGTEVTLIKEVRDVLQTLKDAGTYLATASWNDVPEWAYEILG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058  81 LFHID----DKPLISFFRSLQWG-QGSKINHVEKAACELHIEE--ELRRGDVILFDDEARNrdVEEVNCYFFKINQNE-G 152
Cdd:TIGR01685  82 TFEITyagkTVPMHSLFDDRIEIyKPNKAKQLEMILQKVNKVDpsVLKPAQILFFDDRTDN--VREVWGYGVTSCYCPsG 159
                         170
                  ....*....|....
gi 2470626058 153 LTFPVFNEALEVWR 166
Cdd:TIGR01685 160 MDKGTFKKILEMWR 173
HAD-SF-IIIC TIGR01681
HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the ...
4-136 5.04e-13

HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. Subfamily III (also including IIIA - TIGR01662 and IIIB - pfam03767) contains sequences which do not contain either of the insert domains (between the 1st and 2nd conserved catalytic motifs, subfamily I - TIGR01493, TIGR01509, TIGR01549, TIGR01488, TIGR01494, TIGR01658, TIGR01544 and TIGR01545, or between the 2nd and 3rd, subfamily II - TIGR01460 and TIGR01484). Subfamily IIIC contains five relatively distantly related clades: a family of viral proteins (TIGR01684), a family of eukaryotic proteins called MDP-1 and a family of archaeal proteins most closely related to MDP-1 (TIGR01685), a family of bacteria including the Streptomyces FkbH protein (TIGR01686), and a small clade including the Pasteurella BcbF and EcbF proteins. The overall lack of species overlap among these clades may indicate a conserved function, but the degree of divergence between the clades and the differences in archetecture outside of the domain in some clades warns against such a conclusion. No member of this subfamily is characterized with respect to function, however the MDP-1 protein is a characterized phosphatase. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC.


Pssm-ID: 273752 [Multi-domain]  Cd Length: 128  Bit Score: 62.45  E-value: 5.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470626058   4 KAIVLDLDYTIWPCWCDTHlslplskasktgIEDGRGFKLYLFDDVSSIVKLLSNSGVILIAASRTARPDIAEKLLTLFH 83
Cdd:TIGR01681   1 KVIVFDLDNTLWTGENIVV------------GEDPIIDLEVTIKEIRDKLQTLKKNGFLLALASYNDDPHVAYELLKIFE 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2470626058  84 IDDK--PLISFFRSLQWGQ-GSKINHVEKAACELHIEEELrrGDVILFDDEARNRD 136
Cdd:TIGR01681  69 DFGIifPLAEYFDPLTIGYwLPKSPRLVEIALKLNGVLKP--KSILFVDDRPDNNE 122
 
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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