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Conserved domains on  [gi|19111973|ref|NP_595181|]
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thiamine-repressible acid phosphatase Pho4 [Schizosaccharomyces pombe]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10448333)

histidine phosphatase family protein contains a conserved His residue that is transiently phosphorylated during the catalytic cycle; similar to acid phosphatases and phytase A/B

CATH:  3.40.50.1240
EC:  3.1.3.-
Gene Ontology:  GO:0016791
PubMed:  18092946|31707654
SCOP:  3000781

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
60-405 4.33e-102

Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


:

Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 308.95  E-value: 4.33e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973    60 IKQVHLLQRHGSRNPTGDDTATDVSsaqyiDIFQNKLLNGSIPVNFSYPENPLYFVKHWTPVIkaenaDQLSSSGRIELF 139
Cdd:pfam00328   2 LEQVQVVSRHGDRTPTQKFKKSYES-----LIFKILSLAGSLEGKLSFPGDYRYFKLQYTLGW-----GGLTPSGRVQAE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   140 DLGRQVFERYY-ELFDT----DVYDINTAAQERVVDSAEWFSYGMFGDDMQ---------NKTNFIVLPEDDSAGANSLA 205
Cdd:pfam00328  72 NLGRYFRQRYVgGLLRDgynaKDIYIRASSEGRVIASAQAFAEGLFGPEGEdvdkdllddSNVAKVTIDEDKKALANNLT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   206 MYY-SCPVYEDNNIDENTTEAAHTSWRNVFLKPIANRLNKYFDSGYNLTVSDVRSLYYICVYEIALRDNSDFCSLFTPSE 284
Cdd:pfam00328 152 AGYcSCPAFEWPLQLLKQVDEALDYYLPVFLEPIAKRLEQLCPGETNLTADDVWALLFLCFFETNKADLSPFCDLFTEED 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   285 FLNFEYDSDLDYAY-WGGPASEWASTLGGAYVNNLANNLRKGVNNAS------DRKVFLAFTHDSQIIPVEAALGFFPDI 357
Cdd:pfam00328 232 ALHNEYLLDLEEYYgLAGIGNELKKTIGGPLLNELLARLTNDLVCTQeatfplDAKLYLYFTHDTTIYSLLSALGLFDDL 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 19111973   358 TPEHPLPTdknifTYSLKTSSFVPFAGNLITELFLCSDNK--YYVRHLVN 405
Cdd:pfam00328 312 PPLSSLRV-----LDGYSASGEVPYGARLVFELYECSSEKdsRYVRLLLN 356
 
Name Accession Description Interval E-value
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
60-405 4.33e-102

Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 308.95  E-value: 4.33e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973    60 IKQVHLLQRHGSRNPTGDDTATDVSsaqyiDIFQNKLLNGSIPVNFSYPENPLYFVKHWTPVIkaenaDQLSSSGRIELF 139
Cdd:pfam00328   2 LEQVQVVSRHGDRTPTQKFKKSYES-----LIFKILSLAGSLEGKLSFPGDYRYFKLQYTLGW-----GGLTPSGRVQAE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   140 DLGRQVFERYY-ELFDT----DVYDINTAAQERVVDSAEWFSYGMFGDDMQ---------NKTNFIVLPEDDSAGANSLA 205
Cdd:pfam00328  72 NLGRYFRQRYVgGLLRDgynaKDIYIRASSEGRVIASAQAFAEGLFGPEGEdvdkdllddSNVAKVTIDEDKKALANNLT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   206 MYY-SCPVYEDNNIDENTTEAAHTSWRNVFLKPIANRLNKYFDSGYNLTVSDVRSLYYICVYEIALRDNSDFCSLFTPSE 284
Cdd:pfam00328 152 AGYcSCPAFEWPLQLLKQVDEALDYYLPVFLEPIAKRLEQLCPGETNLTADDVWALLFLCFFETNKADLSPFCDLFTEED 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   285 FLNFEYDSDLDYAY-WGGPASEWASTLGGAYVNNLANNLRKGVNNAS------DRKVFLAFTHDSQIIPVEAALGFFPDI 357
Cdd:pfam00328 232 ALHNEYLLDLEEYYgLAGIGNELKKTIGGPLLNELLARLTNDLVCTQeatfplDAKLYLYFTHDTTIYSLLSALGLFDDL 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 19111973   358 TPEHPLPTdknifTYSLKTSSFVPFAGNLITELFLCSDNK--YYVRHLVN 405
Cdd:pfam00328 312 PPLSSLRV-----LDGYSASGEVPYGARLVFELYECSSEKdsRYVRLLLN 356
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
60-405 1.46e-49

Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.


Pssm-ID: 132717 [Multi-domain]  Cd Length: 242  Bit Score: 169.09  E-value: 1.46e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973  60 IKQVHLLQRHGSRNPtgddtatdvssaqyidifqnkllngsipvnfsypenplyfvkhwtpvikaenaDQLSSSGRIELF 139
Cdd:cd07061   2 LEQVQVLSRHGDRYP-----------------------------------------------------GELTPFGRQQAF 28
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973 140 DLGRQVFERYYELFDTDVYD-----INTAAQERVVDSAEWFSYGMFGDDMQNKTNFIVLPEDDSaganslamyyscpvye 214
Cdd:cd07061  29 ELGRYFRQRYGELLLLHSYNrsdlyIRSSDSQRTLQSAQAFLAGLFPPDGWQPIAVHTIPEEED---------------- 92
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973 215 dnnidentteaahtswrnvflkpianrlnkyfdsgynltvsDVRSLYYICVYEIALRDNS-DFCSLFTPSEFLNFEYDSD 293
Cdd:cd07061  93 -----------------------------------------DVSNLFDLCAYETVAKGYSaPFCDLFTEEEWVKLEYLND 131
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973 294 LDYAYWGGPASEWASTLGGAYVNNLANNLRKGVNNAS----DRKVFLAFTHDSQIIPVEAALGFFPDITPEHPlptdknI 369
Cdd:cd07061 132 LKFYYGYGPGNPLARAQGSPLLNELLARLTNGPSGSQtfplDRKLYLYFSHDTTILPLLTALGLFDFAEPLPP------D 205
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 19111973 370 FTYSLKTSSFVPFAGNLITELFLCS-DNKYYVRHLVN 405
Cdd:cd07061 206 FLRGFSESDYPPFAARLVFELWRCPgDGESYVRVLVN 242
 
Name Accession Description Interval E-value
His_Phos_2 pfam00328
Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so ...
60-405 4.33e-102

Histidine phosphatase superfamily (branch 2); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.


Pssm-ID: 395259 [Multi-domain]  Cd Length: 356  Bit Score: 308.95  E-value: 4.33e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973    60 IKQVHLLQRHGSRNPTGDDTATDVSsaqyiDIFQNKLLNGSIPVNFSYPENPLYFVKHWTPVIkaenaDQLSSSGRIELF 139
Cdd:pfam00328   2 LEQVQVVSRHGDRTPTQKFKKSYES-----LIFKILSLAGSLEGKLSFPGDYRYFKLQYTLGW-----GGLTPSGRVQAE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   140 DLGRQVFERYY-ELFDT----DVYDINTAAQERVVDSAEWFSYGMFGDDMQ---------NKTNFIVLPEDDSAGANSLA 205
Cdd:pfam00328  72 NLGRYFRQRYVgGLLRDgynaKDIYIRASSEGRVIASAQAFAEGLFGPEGEdvdkdllddSNVAKVTIDEDKKALANNLT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   206 MYY-SCPVYEDNNIDENTTEAAHTSWRNVFLKPIANRLNKYFDSGYNLTVSDVRSLYYICVYEIALRDNSDFCSLFTPSE 284
Cdd:pfam00328 152 AGYcSCPAFEWPLQLLKQVDEALDYYLPVFLEPIAKRLEQLCPGETNLTADDVWALLFLCFFETNKADLSPFCDLFTEED 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973   285 FLNFEYDSDLDYAY-WGGPASEWASTLGGAYVNNLANNLRKGVNNAS------DRKVFLAFTHDSQIIPVEAALGFFPDI 357
Cdd:pfam00328 232 ALHNEYLLDLEEYYgLAGIGNELKKTIGGPLLNELLARLTNDLVCTQeatfplDAKLYLYFTHDTTIYSLLSALGLFDDL 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 19111973   358 TPEHPLPTdknifTYSLKTSSFVPFAGNLITELFLCSDNK--YYVRHLVN 405
Cdd:pfam00328 312 PPLSSLRV-----LDGYSASGEVPYGARLVFELYECSSEKdsRYVRLLLN 356
HP_HAP_like cd07061
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His ...
60-405 1.46e-49

Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.


Pssm-ID: 132717 [Multi-domain]  Cd Length: 242  Bit Score: 169.09  E-value: 1.46e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973  60 IKQVHLLQRHGSRNPtgddtatdvssaqyidifqnkllngsipvnfsypenplyfvkhwtpvikaenaDQLSSSGRIELF 139
Cdd:cd07061   2 LEQVQVLSRHGDRYP-----------------------------------------------------GELTPFGRQQAF 28
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973 140 DLGRQVFERYYELFDTDVYD-----INTAAQERVVDSAEWFSYGMFGDDMQNKTNFIVLPEDDSaganslamyyscpvye 214
Cdd:cd07061  29 ELGRYFRQRYGELLLLHSYNrsdlyIRSSDSQRTLQSAQAFLAGLFPPDGWQPIAVHTIPEEED---------------- 92
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973 215 dnnidentteaahtswrnvflkpianrlnkyfdsgynltvsDVRSLYYICVYEIALRDNS-DFCSLFTPSEFLNFEYDSD 293
Cdd:cd07061  93 -----------------------------------------DVSNLFDLCAYETVAKGYSaPFCDLFTEEEWVKLEYLND 131
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111973 294 LDYAYWGGPASEWASTLGGAYVNNLANNLRKGVNNAS----DRKVFLAFTHDSQIIPVEAALGFFPDITPEHPlptdknI 369
Cdd:cd07061 132 LKFYYGYGPGNPLARAQGSPLLNELLARLTNGPSGSQtfplDRKLYLYFSHDTTILPLLTALGLFDFAEPLPP------D 205
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 19111973 370 FTYSLKTSSFVPFAGNLITELFLCS-DNKYYVRHLVN 405
Cdd:cd07061 206 FLRGFSESDYPPFAARLVFELWRCPgDGESYVRVLVN 242
 
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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