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Conserved domains on  [gi|51476595|emb|CAH18280|]
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hypothetical protein [Homo sapiens]

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 ...
 3-164 1.75e-44

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: 147.74  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595     3 LSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFA 78
Cdd:pfam00300  25 LTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLREIDFGDWEGLTFEEIAERYPEEYD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    79 LRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPV 155
Cdd:pfam00300 103 AWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHLLGLPLEALRRFPLDNASLSILEFD 182


                  ....*....
gi 51476595   156 AYGCKVETI 164
Cdd:pfam00300 183 GGGWVLVLL 191
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 3-164 1.75e-44

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: 147.74  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595     3 LSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFA 78
Cdd:pfam00300  25 LTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLREIDFGDWEGLTFEEIAERYPEEYD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    79 LRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPV 155
Cdd:pfam00300 103 AWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHLLGLPLEALRRFPLDNASLSILEFD 182


                  ....*....
gi 51476595   156 AYGCKVETI 164
Cdd:pfam00300 183 GGGWVLVLL 191
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
3-145 4.78e-37

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 128.52  E-value: 4.78e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   3 LSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFA 78
Cdd:COG0406  28 LTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEalaeALGLPVEVDPRLREIDFGDWEGLTFAELEARYPEALA 105

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595  79 LRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADELPYLRCP 145
Cdd:COG0406 106 AWLADPAEFRPPGGESLADVQARVRAALEELLARhpgGTVLVVTHGGVIRALLAHLLGLPLEAFWRLRID 175
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-127 1.80e-31

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: 112.94  E-value: 1.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595      3 LSVRGKQFAQALRKFL-EEQEITDLKVWTSQLKRTIQTAESLGVPYEQWkILNEIDAGVCEEMTYAEIEKRYPEEFALRD 81
Cdd:smart00855  26 LTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLP-GLRERDFGAWEGLTWDEIAAKYPEEYLAAW 104

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 51476595     82 QEKYLYRY---PGGESYQDLVQRLEPVIMELERQ-----GNVLVISHQAVMRCL 127
Cdd:smart00855 105 RDPYDPAPpapPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 3-159 6.16e-26

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: 99.23  E-value: 6.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595     3 LSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAESLGVPyEQWKI-----LNEIDAGVCEEMTYAEIEKRYPEef 77
Cdd:TIGR03162  24 LAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILAER-RGLPIikddrLREMDFGDWEGRSWDEIPEAYPE-- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    78 alrdQEKYL-----YRYPGGESYQDLVQRLEPV---IMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLrcplhti 149
Cdd:TIGR03162  99 ----LDAWAadwqhARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRALLAHLLGLPLEQWWSF------- 167

                         170
                  ....*....|
gi 51476595   150 fkltPVAYGC 159
Cdd:TIGR03162 168 ----AVEYGS 173
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-166 5.26e-24

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: 93.54  E-value: 5.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   3 LSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESL-----GVPYEQWKILNEidagvceemtyaeiekrypeef 77
Cdd:cd07067  26 LTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIIleelpGLPVEVDPRLRE---------------------- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595  78 alrdqekylyrypggesyqdlvQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTP 154
Cdd:cd07067  84 ----------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLAYLLGLSDEDILRLNLPNGSISVLEL 141

                       170
                ....*....|..
gi 51476595 155 VAYGCKVETIKL 166
Cdd:cd07067 142 DENGGGVLLLRL 153
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-139 1.09e-11

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 63.46  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    3 LSVRGKQFAQALRKFLEEQEITDLkVWTSQLKRTIQTA----ESLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFA 78
Cdd:PRK07238 198 LTEVGRRQAAAAARYLAARGGIDA-VVSSPLQRARDTAaaaaKALGLDVTVDDDLIETDFGAWEGLTFAEAAERDPELHR 276

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51476595   79 --LRDQEkylYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADEL 139
Cdd:PRK07238 277 awLADTS---VAPPGGESFDAVARRVRRARDRLIAEypgATVLVVSHVTPIKTLLRLALDAGPGVL 339
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 3-164 1.75e-44

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: 147.74  E-value: 1.75e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595     3 LSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFA 78
Cdd:pfam00300  25 LTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLREIDFGDWEGLTFEEIAERYPEEYD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    79 LRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPV 155
Cdd:pfam00300 103 AWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHLLGLPLEALRRFPLDNASLSILEFD 182


                  ....*....
gi 51476595   156 AYGCKVETI 164
Cdd:pfam00300 183 GGGWVLVLL 191
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
3-145 4.78e-37

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 128.52  E-value: 4.78e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   3 LSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFA 78
Cdd:COG0406  28 LTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEalaeALGLPVEVDPRLREIDFGDWEGLTFAELEARYPEALA 105

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595  79 LRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADELPYLRCP 145
Cdd:COG0406 106 AWLADPAEFRPPGGESLADVQARVRAALEELLARhpgGTVLVVTHGGVIRALLAHLLGLPLEAFWRLRID 175
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-127 1.80e-31

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: 112.94  E-value: 1.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595      3 LSVRGKQFAQALRKFL-EEQEITDLKVWTSQLKRTIQTAESLGVPYEQWkILNEIDAGVCEEMTYAEIEKRYPEEFALRD 81
Cdd:smart00855  26 LTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLP-GLRERDFGAWEGLTWDEIAAKYPEEYLAAW 104

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 51476595     82 QEKYLYRY---PGGESYQDLVQRLEPVIMELERQ-----GNVLVISHQAVMRCL 127
Cdd:smart00855 105 RDPYDPAPpapPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 3-159 6.16e-26

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: 99.23  E-value: 6.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595     3 LSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAESLGVPyEQWKI-----LNEIDAGVCEEMTYAEIEKRYPEef 77
Cdd:TIGR03162  24 LAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILAER-RGLPIikddrLREMDFGDWEGRSWDEIPEAYPE-- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    78 alrdQEKYL-----YRYPGGESYQDLVQRLEPV---IMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLrcplhti 149
Cdd:TIGR03162  99 ----LDAWAadwqhARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRALLAHLLGLPLEQWWSF------- 167

                         170
                  ....*....|
gi 51476595   150 fkltPVAYGC 159
Cdd:TIGR03162 168 ----AVEYGS 173
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-166 5.26e-24

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: 93.54  E-value: 5.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   3 LSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESL-----GVPYEQWKILNEidagvceemtyaeiekrypeef 77
Cdd:cd07067  26 LTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIIleelpGLPVEVDPRLRE---------------------- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595  78 alrdqekylyrypggesyqdlvQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTP 154
Cdd:cd07067  84 ----------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLAYLLGLSDEDILRLNLPNGSISVLEL 141

                       170
                ....*....|..
gi 51476595 155 VAYGCKVETIKL 166
Cdd:cd07067 142 DENGGGVLLLRL 153
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-153 2.36e-16

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: 73.22  E-value: 2.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   3 LSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPYEQWKILNEIDAgvceemtyaeiekrypeefalrdq 82
Cdd:cd07040  26 LTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEVDPR------------------------ 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51476595  83 ekylyrypggesyqdlvQRLEPVIMELERQ-----GNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLT 153
Cdd:cd07040  82 -----------------ARVLNALLELLARhlldgKNVLIVSHGGTIRALLAALLGLSDEEILSLNLPNGSILVLE 140
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-139 1.09e-11

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 63.46  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    3 LSVRGKQFAQALRKFLEEQEITDLkVWTSQLKRTIQTA----ESLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFA 78
Cdd:PRK07238 198 LTEVGRRQAAAAARYLAARGGIDA-VVSSPLQRARDTAaaaaKALGLDVTVDDDLIETDFGAWEGLTFAEAAERDPELHR 276

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51476595   79 --LRDQEkylYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYFLDKGADEL 139
Cdd:PRK07238 277 awLADTS---VAPPGGESFDAVARRVRRARDRLIAEypgATVLVVSHVTPIKTLLRLALDAGPGVL 339
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
3-133 2.90e-11

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 60.45  E-value: 2.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    3 LSVRGKQFAQALRKFLeeQEITDLKVWTSQLKRTIQTAE----SLGVPYEQWKILNEIDAGvceemtyaEIEKRYPEEFA 78
Cdd:PRK15004  27 LTARGIEQAQNLHTLL--RDVPFDLVLCSELERAQHTARlvlsDRQLPVHIIPELNEMFFG--------DWEMRHHRDLM 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51476595   79 LRDQEKYL-----YRY---PGGESYQDLVQRLEPVIMEL---ERQGNVLVISHQAVMRCLLAYFLD 133
Cdd:PRK15004  97 QEDAENYAawcndWQHaipTNGEGFQAFSQRVERFIARLsafQHYQNLLIVSHQGVLSLLIARLLG 162
PRK13463 PRK13463
phosphoserine phosphatase 1;
28-131 9.39e-11

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 59.29  E-value: 9.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   28 VWTSQLKRTIQTAESL----GVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQR-L 102
Cdd:PRK13463  52 IYSSPSERTLHTAELIkgerDIPIIADEHFYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvI 131

                         90       100       110
                 ....*....|....*....|....*....|.
gi 51476595  103 EPVIMELERQG--NVLVISHQAVMRCLLAYF 131
Cdd:PRK13463 132 EGMQLLLEKHKgeSILIVSHAAAAKLLVGHF 162
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 3-175 3.07e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    3 LSVRGKQFAQAL-RKFLEEQEITDLKVWTSQLKRTIQTAE---------------------SLGVPYEQWKILNEIDAGV 60
Cdd:PTZ00322 444 LTERGRAYSRALfEYFQKEISTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYFPTLDDINHGD 523

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   61 CEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGE-SYQDLVQRLEPVIMELERQGN-VLVISHQAVMRCLLAYFLDKGADE 138
Cdd:PTZ00322 524 CEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGEcIHQVFNARLEPHIHDIQASTTpVLVVSHLHLLQGLYSYFVTDGDNI 603

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 51476595  139 LP-----YLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHR 175
Cdd:PTZ00322 604 VApqnayKIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQ 645
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 3-138 6.01e-07

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 48.89  E-value: 6.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595    3 LSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTA----ESLGVPY----EQWKiLNEIDAGVCEEMTYAEIEKRYP 74
Cdd:PTZ00123  15 LSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAwivlEELGQLHvpviKSWR-LNERHYGALQGLNKSETAEKHG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   75 EE--------FALR--DQEKYLYRYPG---------------GESYQDLVQRLEP----VIMELERQG-NVLVISHQAVM 124
Cdd:PTZ00123  94 EEqvkiwrrsYDIPppPLEKSDERYPGndpvykdipkdalpnTECLKDTVERVLPywedHIAPDILAGkKVLVAAHGNSL 173

                        170
                 ....*....|....
gi 51476595  125 RCLLAYfLDKGADE 138
Cdd:PTZ00123 174 RALVKY-LDKMSEE 186
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-121 5.40e-05

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 42.17  E-value: 5.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51476595   3 LSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGvpyEQWKILNEIDagVCEEMTYAEIEkrypeefalrdq 82
Cdd:COG2062  23 LTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILA---EALGLPPKVE--VEDELYDADPE------------ 85

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 51476595  83 ekylyrypggesyqDLVQRLEpvimELERQGNVLVISHQ 121
Cdd:COG2062  86 --------------DLLDLLR----ELDDGETVLLVGHN 106
 
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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