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Conserved domains on  [gi|321264185|ref|XP_003196810|]
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Hypothetical protein CGB_K3040C [Cryptococcus gattii WM276]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10447784)

histidine phosphatase family protein is a probable phosphatase that may catalyze the dephosphorylation of a phosphorylated substrate involving a conserved catalytic histidine residue which becomes phosphorylated during the reaction

CATH:  3.40.50.1240
Gene Ontology:  GO:0003824
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 2-159 4.41e-26

Histidine phosphatase superfamily (branch 1); 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 larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


:

Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 100.36  E-value: 4.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185    2 QAKALGESLKDTKFDYIFTSDLKRAHWTSQQILKNQadpKPPLVVSELLREQHFGEGEQKPF--------GDGSRWVRQP 73
Cdd:pfam00300  32 QAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEAL---GLPVEIDPRLREIDFGDWEGLTFeeiaerypEEYDAWLADP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   74 GRvFKFPGGESLTDVRKRADQAVEQfiepILRECRGrpatsKHVAVVAHGIFNSEFLGALmarrkMNAPLE-WSYRGMTN 152
Cdd:pfam00300 109 AD-YRPPGGESLADVRARVRAALEE----LAARHPG-----KTVLVVSHGGVIRALLAHL-----LGLPLEaLRRFPLDN 173


                  ....*..
gi 321264185  153 TGWTKAE 159
Cdd:pfam00300 174 ASLSILE 180
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 2-159 4.41e-26

Histidine phosphatase superfamily (branch 1); 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 larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 100.36  E-value: 4.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185    2 QAKALGESLKDTKFDYIFTSDLKRAHWTSQQILKNQadpKPPLVVSELLREQHFGEGEQKPF--------GDGSRWVRQP 73
Cdd:pfam00300  32 QAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEAL---GLPVEIDPRLREIDFGDWEGLTFeeiaerypEEYDAWLADP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   74 GRvFKFPGGESLTDVRKRADQAVEQfiepILRECRGrpatsKHVAVVAHGIFNSEFLGALmarrkMNAPLE-WSYRGMTN 152
Cdd:pfam00300 109 AD-YRPPGGESLADVRARVRAALEE----LAARHPG-----KTVLVVSHGGVIRALLAHL-----LGLPLEaLRRFPLDN 173


                  ....*..
gi 321264185  153 TGWTKAE 159
Cdd:pfam00300 174 ASLSILE 180
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
2-161 7.36e-25

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 97.32  E-value: 7.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDTKFDYIFTSDLKRAHWTSQQILKNQadpKPPLVVSELLREQHFGEGEQKPFGD--------GSRWVRQP 73
Cdd:COG0406   35 QARALAERLADIPFDAVYSSPLQRARQTAEALAEAL---GLPVEVDPRLREIDFGDWEGLTFAElearypeaLAAWLADP 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185  74 GRvFKFPGGESLTDVRKRADQAVEQfiepILRECRGRpatskHVAVVAHGIFNSEFLGALmarrkMNAPLEWSYR-GMTN 152
Cdd:COG0406  112 AE-FRPPGGESLADVQARVRAALEE----LLARHPGG-----TVLVVTHGGVIRALLAHL-----LGLPLEAFWRlRIDN 176


                 ....*....
gi 321264185 153 TGWTKAEVG 161
Cdd:COG0406  177 ASVTVLEFD 185
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 1-123 8.71e-21

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 86.14  E-value: 8.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185    1 MQAKALGESLKDTKFDYIFTSDLKRAHWTSQqILKNQADPkpPLVVSELLREQHFGEGEQKPF-------GDGSRWVRQP 73
Cdd:TIGR03162  30 EQAAALREKLADVPFDAVYSSPLSRCRELAE-ILAERRGL--PIIKDDRLREMDFGDWEGRSWdeipeayPELDAWAADW 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 321264185   74 GRvFKFPGGESLTDVRKRadqaVEQFIEPILRECRGRpatskHVAVVAHG 123
Cdd:TIGR03162 107 QH-ARPPGGESFADFYQR----VSEFLEELLKAHEGD-----NVLIVTHG 146
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 2-123 1.40e-16

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 74.42  E-value: 1.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185     2 QAKALGESLK---DTKFDYIFTSDLKRAHWTSQQILKNQADPkpplvvseLLREQHFGEGEQKPFGDGSR---------- 68
Cdd:smart00855  33 QAEALGRLLAsllLPRFDVVYSSPLKRARQTAEALAIALGLP--------GLRERDFGAWEGLTWDEIAAkypeeylaaw 104

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 321264185    69 WVRQPGRVFKFPGGESLTDVRKRADQAVEQFIEPILREcrgrpatSKHVAVVAHG 123
Cdd:smart00855 105 RDPYDPAPPAPPGGESLADLVERVEPALDELIATADAS-------GQNVLIVSHG 152
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 2-157 2.40e-13

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 65.42  E-value: 2.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDT--KFDYIFTSDLKRAHWTSQQILKNQadPKPPLVVSELLREQhfgegeqkpfgdgsrwvrqpgrvfkf 79
Cdd:cd07067   33 QARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILEEL--PGLPVEVDPRLREA-------------------------- 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321264185  80 pggesltdvrkRADQAVEQFIepilrecrgRPATSKHVAVVAHGIFNSEFLGALMARrkmnAPLEWSYRGMTNTGWTK 157
Cdd:cd07067   85 -----------RVLPALEELI---------APHDGKNVLIVSHGGVLRALLAYLLGL----SDEDILRLNLPNGSISV 138
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 2-140 8.19e-09

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 53.92  E-value: 8.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDT--KFDYIFTSDLKRAHWTSQQILKNQADPKPPLVVSELLREQHFGE--GEQKpfgDGSR--WVRQPGR 75
Cdd:PRK01295  36 EAKAAGRKLKAAglKFDIAFTSALSRAQHTCQLILEELGQPGLETIRDQALNERDYGDlsGLNK---DDARakWGEEQVH 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321264185  76 VFKF------PGGESLTDVRKRADQAVEQFIEP-ILRecrgrpatSKHVAVVAHGifNSefLGAL-MARRKMN 140
Cdd:PRK01295 113 IWRRsydvppPGGESLKDTGARVLPYYLQEILPrVLR--------GERVLVAAHG--NS--LRALvMVLDGLT 173
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 2-159 4.41e-26

Histidine phosphatase superfamily (branch 1); 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 larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 100.36  E-value: 4.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185    2 QAKALGESLKDTKFDYIFTSDLKRAHWTSQQILKNQadpKPPLVVSELLREQHFGEGEQKPF--------GDGSRWVRQP 73
Cdd:pfam00300  32 QAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEAL---GLPVEIDPRLREIDFGDWEGLTFeeiaerypEEYDAWLADP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   74 GRvFKFPGGESLTDVRKRADQAVEQfiepILRECRGrpatsKHVAVVAHGIFNSEFLGALmarrkMNAPLE-WSYRGMTN 152
Cdd:pfam00300 109 AD-YRPPGGESLADVRARVRAALEE----LAARHPG-----KTVLVVSHGGVIRALLAHL-----LGLPLEaLRRFPLDN 173


                  ....*..
gi 321264185  153 TGWTKAE 159
Cdd:pfam00300 174 ASLSILE 180
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
2-161 7.36e-25

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 97.32  E-value: 7.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDTKFDYIFTSDLKRAHWTSQQILKNQadpKPPLVVSELLREQHFGEGEQKPFGD--------GSRWVRQP 73
Cdd:COG0406   35 QARALAERLADIPFDAVYSSPLQRARQTAEALAEAL---GLPVEVDPRLREIDFGDWEGLTFAElearypeaLAAWLADP 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185  74 GRvFKFPGGESLTDVRKRADQAVEQfiepILRECRGRpatskHVAVVAHGIFNSEFLGALmarrkMNAPLEWSYR-GMTN 152
Cdd:COG0406  112 AE-FRPPGGESLADVQARVRAALEE----LLARHPGG-----TVLVVTHGGVIRALLAHL-----LGLPLEAFWRlRIDN 176


                 ....*....
gi 321264185 153 TGWTKAEVG 161
Cdd:COG0406  177 ASVTVLEFD 185
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 1-123 8.71e-21

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 86.14  E-value: 8.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185    1 MQAKALGESLKDTKFDYIFTSDLKRAHWTSQqILKNQADPkpPLVVSELLREQHFGEGEQKPF-------GDGSRWVRQP 73
Cdd:TIGR03162  30 EQAAALREKLADVPFDAVYSSPLSRCRELAE-ILAERRGL--PIIKDDRLREMDFGDWEGRSWdeipeayPELDAWAADW 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 321264185   74 GRvFKFPGGESLTDVRKRadqaVEQFIEPILRECRGRpatskHVAVVAHG 123
Cdd:TIGR03162 107 QH-ARPPGGESFADFYQR----VSEFLEELLKAHEGD-----NVLIVTHG 146
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 2-123 1.40e-16

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 74.42  E-value: 1.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185     2 QAKALGESLK---DTKFDYIFTSDLKRAHWTSQQILKNQADPkpplvvseLLREQHFGEGEQKPFGDGSR---------- 68
Cdd:smart00855  33 QAEALGRLLAsllLPRFDVVYSSPLKRARQTAEALAIALGLP--------GLRERDFGAWEGLTWDEIAAkypeeylaaw 104

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 321264185    69 WVRQPGRVFKFPGGESLTDVRKRADQAVEQFIEPILREcrgrpatSKHVAVVAHG 123
Cdd:smart00855 105 RDPYDPAPPAPPGGESLADLVERVEPALDELIATADAS-------GQNVLIVSHG 152
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 2-157 2.40e-13

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 65.42  E-value: 2.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDT--KFDYIFTSDLKRAHWTSQQILKNQadPKPPLVVSELLREQhfgegeqkpfgdgsrwvrqpgrvfkf 79
Cdd:cd07067   33 QARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILEEL--PGLPVEVDPRLREA-------------------------- 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 321264185  80 pggesltdvrkRADQAVEQFIepilrecrgRPATSKHVAVVAHGIFNSEFLGALMARrkmnAPLEWSYRGMTNTGWTK 157
Cdd:cd07067   85 -----------RVLPALEELI---------APHDGKNVLIVSHGGVLRALLAYLLGL----SDEDILRLNLPNGSISV 138
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 2-140 8.19e-09

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 53.92  E-value: 8.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDT--KFDYIFTSDLKRAHWTSQQILKNQADPKPPLVVSELLREQHFGE--GEQKpfgDGSR--WVRQPGR 75
Cdd:PRK01295  36 EAKAAGRKLKAAglKFDIAFTSALSRAQHTCQLILEELGQPGLETIRDQALNERDYGDlsGLNK---DDARakWGEEQVH 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321264185  76 VFKF------PGGESLTDVRKRADQAVEQFIEP-ILRecrgrpatSKHVAVVAHGifNSefLGAL-MARRKMN 140
Cdd:PRK01295 113 IWRRsydvppPGGESLKDTGARVLPYYLQEILPrVLR--------GERVLVAAHG--NS--LRALvMVLDGLT 173
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 2-133 2.38e-08

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 51.65  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDT--KFDYIFTSDLKRAHWTSQQILKNQADPKPPLVvsellreqhfgegeqkpfgdgsrwvrqpgrvfkf 79
Cdd:cd07040   33 QARELGKALRERyiKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEV---------------------------------- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 321264185  80 pggesltDVRKRADQAVEQFIEPILREcrgrpatSKHVAVVAHGIFNSEFLGAL 133
Cdd:cd07040   79 -------DPRARVLNALLELLARHLLD-------GKNVLIVSHGGTIRALLAAL 118
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
2-148 1.90e-07

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 50.05  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDTKFDYIFTSDLKRAHWTSQQILknqADPKPPLVVSELLREQHFGEGEQKPFGDGSR--------WVRQ- 72
Cdd:PRK15004  34 QAQNLHTLLRDVPFDLVLCSELERAQHTARLVL---SDRQLPVHIIPELNEMFFGDWEMRHHRDLMQedaenyaaWCNDw 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185  73 ----PgrvfkfPGGESLTDVRKRadqaVEQFIEPILrecrgRPATSKHVAVVAH-GIfnsefLGALMARR-KMNAPLEWS 146
Cdd:PRK15004 111 qhaiP------TNGEGFQAFSQR----VERFIARLS-----AFQHYQNLLIVSHqGV-----LSLLIARLlGMPAEAMWH 170


                 ..
gi 321264185 147 YR 148
Cdd:PRK15004 171 FR 172
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
2-127 2.53e-07

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 50.10  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDTKFDYIFTSDLKRA---------HWTSQQI--LKNQADPKP---------------PLVVSELLREQHF 55
Cdd:PRK01112  35 EAIAAGEKIKDLPIDCIFTSTLVRSlmtallamtNHSSGKIpyIVHEEDDKKwmsriysdeepeqmiPLFQSSALNERMY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185  56 GE--GEQKP-----FGdgSRWVRQPGRVFKF--PGGESLTDVRKRADQAVEQFIEPILREcrgrpatSKHVAVVAHGifN 126
Cdd:PRK01112 115 GElqGKNKAetaekFG--EEQVKLWRRSYKTapPQGESLEDTGQRTLPYFQNRILPHLQQ-------GKNVFVSAHG--N 183


                 .
gi 321264185 127 S 127
Cdd:PRK01112 184 S 184
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 2-134 3.25e-06

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 46.96  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDT--KFDYIFTSDLKRAHWTSQQILKNQADPKPPLVVSELLREQHFG--------EGEQKpFG------- 64
Cdd:PTZ00123  22 EAREAGKLLKEKgfRFDVVYTSVLKRAIKTAWIVLEELGQLHVPVIKSWRLNERHYGalqglnksETAEK-HGeeqvkiw 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185  65 -------------DGSRWvrqPG--RVFK------FPGGESLTDVRKRADQAVEQFIEPILREcrgrpatSKHVAVVAHG 123
Cdd:PTZ00123 101 rrsydipppplekSDERY---PGndPVYKdipkdaLPNTECLKDTVERVLPYWEDHIAPDILA-------GKKVLVAAHG 170

                        170
                 ....*....|.
gi 321264185 124 ifNSefLGALM 134
Cdd:PTZ00123 171 --NS--LRALV 177
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 2-122 7.50e-06

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 46.12  E-value: 7.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDTK-FDYIFTSDLKRAHWTSQQILKNQAdpkPPLVVSELLREQHFGEGEQKPFG--------DGSRWVRQ 72
Cdd:PRK07238 205 QAAAAARYLAARGgIDAVVSSPLQRARDTAAAAAKALG---LDVTVDDDLIETDFGAWEGLTFAeaaerdpeLHRAWLAD 281

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 321264185  73 PGrvFKFPGGESLTDVRKRadqaVEQFIEPILRECRGRpatskHVAVVAH 122
Cdd:PRK07238 282 TS--VAPPGGESFDAVARR----VRRARDRLIAEYPGA-----TVLVVSH 320
PRK13462 PRK13462
acid phosphatase; Provisional
 2-136 4.17e-04

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 40.20  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321264185   2 QAKALGESLKDTKFD--YIFTSDLKRAHWTSQQILKNQADpkpplvVSELLREQHFGEGEqkpfGDGSRWVRQ--PG-RV 76
Cdd:PRK13462  39 QAELAGQALGELELDdpLVISSPRRRALDTAKLAGLTVDE------VSGLLAEWDYGSYE----GLTTPQIREsePDwLV 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 321264185  77 FKF--PGGESLTDVRKRADQAVEQFIEPIlrecrgrpaTSKHVAVVAHGIFNSeflgALMAR 136
Cdd:PRK13462 109 WTHgcPGGESVAQVNERADRAVALALEHM---------ESRDVVFVSHGHFSR----AVITR 157
 
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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