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Conserved domains on  [gi|1985320837|ref|XP_039394747|]
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fructose-2,6-bisphosphatase TIGAR isoform X1 [Mauremys reevesii]

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 ...
 18-147 1.29e-34

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: 123.86  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKnkfcKDIVIQYDARLRERK 97
Cdd:pfam00300   7 GETEWNLEGRFQGRT-DSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEA----LGLPVEIDPRLREID 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985320837  98 YGIAEGRPLSDLKAM----AKAAGEQCPLFTPSGGETLDEVRARAKNFFEFLCQ 147
Cdd:pfam00300  82 FGDWEGLTFEEIAERypeeYDAWLADPADYRPPGGESLADVRARVRAALEELAA 135
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 18-147 1.29e-34

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: 123.86  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKnkfcKDIVIQYDARLRERK 97
Cdd:pfam00300   7 GETEWNLEGRFQGRT-DSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEA----LGLPVEIDPRLREID 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985320837  98 YGIAEGRPLSDLKAM----AKAAGEQCPLFTPSGGETLDEVRARAKNFFEFLCQ 147
Cdd:pfam00300  82 FGDWEGLTFEEIAERypeeYDAWLADPADYRPPGGESLADVRARVRAALEELAA 135
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
18-147 1.03e-32

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 118.89  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKNkfckDIVIQYDARLRERK 97
Cdd:COG0406    10 GETEWNAEGRLQGRL-DVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEAL----GLPVEVDPRLREID 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985320837  98 YGIAEGRPLSDLKA----MAKAAGEQCPLFTPSGGETLDEVRARAKNFFEFLCQ 147
Cdd:COG0406    85 FGDWEGLTFAELEArypeALAAWLADPAEFRPPGGESLADVQARVRAALEELLA 138
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 18-153 1.10e-27

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: 104.47  E-value: 1.10e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837   18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLS---NVKFTHVFSSDLLRAKQTASAIIGKNKFckdiviqydARLR 94
Cdd:smart00855   8 GETEWNREGRLYGDT-DVPLTELGRAQAEALGRLLAsllLPRFDVVYSSPLKRARQTAEALAIALGL---------PGLR 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985320837   95 ERKYGIAEGRPLSDLKAMAKAAGEQCPL-------FTPSGGETLDEVRARAKNFFEFLCQLSIEEE 153
Cdd:smart00855  78 ERDFGAWEGLTWDEIAAKYPEEYLAAWRdpydpapPAPPGGESLADLVERVEPALDELIATADASG 143
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 18-95 5.01e-18

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: 78.90  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQgVDEPLSATGFRQADAAGIFLSNV--KFTHVFSSDLLRAKQTASAIigkNKFCKDIVIQYDARLRE 95
Cdd:cd07067     8 GESEWNAEGRFQGW-TDVPLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEII---LEELPGLPVEVDPRLRE 83
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
18-137 2.12e-15

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 73.22  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASaIIGKNKFCKdivIQYDARLRERK 97
Cdd:PRK03482   10 GETQWNAERRIQGQS-DSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAE-IIAQACGCD---IIFDPRLRELN 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1985320837  98 YGIAEGRPLSDLKAMAKAAGEQCPLFTPSG----GETLDEVRAR 137
Cdd:PRK03482   85 MGVLEKRHIDSLTEEEEGWRRQLVNGTVDGripeGESMQELSDR 128
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 18-143 6.04e-15

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: 71.11  E-value: 6.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKdKILQGQgVDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKnkfcKDIVIQYDARLRERK 97
Cdd:TIGR03162   7 GETDVNA-GLCYGQ-TDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAER----RGLPIIKDDRLREMD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1985320837  98 YGIAEGRPLSDLKAMAKAAGEQC--PL-FTPSGGETLDEVRARAKNFFE 143
Cdd:TIGR03162  81 FGDWEGRSWDEIPEAYPELDAWAadWQhARPPGGESFADFYQRVSEFLE 129
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 18-147 1.29e-34

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: 123.86  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKnkfcKDIVIQYDARLRERK 97
Cdd:pfam00300   7 GETEWNLEGRFQGRT-DSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEA----LGLPVEIDPRLREID 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985320837  98 YGIAEGRPLSDLKAM----AKAAGEQCPLFTPSGGETLDEVRARAKNFFEFLCQ 147
Cdd:pfam00300  82 FGDWEGLTFEEIAERypeeYDAWLADPADYRPPGGESLADVRARVRAALEELAA 135
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
18-147 1.03e-32

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 118.89  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKNkfckDIVIQYDARLRERK 97
Cdd:COG0406    10 GETEWNAEGRLQGRL-DVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEAL----GLPVEVDPRLREID 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985320837  98 YGIAEGRPLSDLKA----MAKAAGEQCPLFTPSGGETLDEVRARAKNFFEFLCQ 147
Cdd:COG0406    85 FGDWEGLTFAELEArypeALAAWLADPAEFRPPGGESLADVQARVRAALEELLA 138
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 18-153 1.10e-27

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: 104.47  E-value: 1.10e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837   18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLS---NVKFTHVFSSDLLRAKQTASAIIGKNKFckdiviqydARLR 94
Cdd:smart00855   8 GETEWNREGRLYGDT-DVPLTELGRAQAEALGRLLAsllLPRFDVVYSSPLKRARQTAEALAIALGL---------PGLR 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985320837   95 ERKYGIAEGRPLSDLKAMAKAAGEQCPL-------FTPSGGETLDEVRARAKNFFEFLCQLSIEEE 153
Cdd:smart00855  78 ERDFGAWEGLTWDEIAAKYPEEYLAAWRdpydpapPAPPGGESLADLVERVEPALDELIATADASG 143
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 18-95 5.01e-18

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: 78.90  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQgVDEPLSATGFRQADAAGIFLSNV--KFTHVFSSDLLRAKQTASAIigkNKFCKDIVIQYDARLRE 95
Cdd:cd07067     8 GESEWNAEGRFQGW-TDVPLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEII---LEELPGLPVEVDPRLRE 83
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
18-137 2.12e-15

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 73.22  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASaIIGKNKFCKdivIQYDARLRERK 97
Cdd:PRK03482   10 GETQWNAERRIQGQS-DSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAE-IIAQACGCD---IIFDPRLRELN 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1985320837  98 YGIAEGRPLSDLKAMAKAAGEQCPLFTPSG----GETLDEVRAR 137
Cdd:PRK03482   85 MGVLEKRHIDSLTEEEEGWRRQLVNGTVDGripeGESMQELSDR 128
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 18-143 6.04e-15

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: 71.11  E-value: 6.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKdKILQGQgVDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKnkfcKDIVIQYDARLRERK 97
Cdd:TIGR03162   7 GETDVNA-GLCYGQ-TDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAER----RGLPIIKDDRLREMD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1985320837  98 YGIAEGRPLSDLKAMAKAAGEQC--PL-FTPSGGETLDEVRARAKNFFE 143
Cdd:TIGR03162  81 FGDWEGRSWDEIPEAYPELDAWAadWQhARPPGGESFADFYQRVSEFLE 129
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 18-94 2.70e-14

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: 68.59  E-value: 2.70e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNV--KFTHVFSSDLLRAKQTAsAIIGKNKFCkDIVIQYDARLR 94
Cdd:cd07040     8 GEREPNAEGRFTGWG-DGPLTEKGRQQARELGKALRERyiKFDRIYSSPLKRAIQTA-EIILEGLFE-GLPVEVDPRAR 83
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
18-163 1.15e-10

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 59.68  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQgVDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKnkfcKDIVIQYDARLRERK 97
Cdd:PRK15004    9 GETQANVDGLYSGH-APTPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLSD----RQLPVHIIPELNEMF 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985320837  98 YGIAEGRPLSDL-KAMAKAAGEQCPLF---TPSGGETLDEVRARAKNFFEflcQLSIEEECQK-----EQAVLGM 163
Cdd:PRK15004   84 FGDWEMRHHRDLmQEDAENYAAWCNDWqhaIPTNGEGFQAFSQRVERFIA---RLSAFQHYQNllivsHQGVLSL 155
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 18-141 2.57e-07

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 51.13  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  18 GETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLS-NVKFTHVFSSDLLRAKQTASAI---IGKnkfckDIVIQYDarL 93
Cdd:PRK07238  180 GQTELSVQRRYSGRG-NPELTEVGRRQAAAAARYLAaRGGIDAVVSSPLQRARDTAAAAakaLGL-----DVTVDDD--L 251

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985320837  94 RERKYGIAEGRPLSDLKAMAKAAGEQC---PLFTPSGGETLDEVRARAKNF 141
Cdd:PRK07238  252 IETDFGAWEGLTFAEAAERDPELHRAWladTSVAPPGGESFDAVARRVRRA 302
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 22-103 6.17e-07

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 49.27  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  22 YNKDKILQGQgVDEPLSATGFRQADAAGIFL--SNVKFTHVFSSDLLRAKQTASaIIGKNKFCKDIVIQYDARLRERKYG 99
Cdd:PTZ00123    1 WNKENRFTGW-TDVPLSEKGVQEAREAGKLLkeKGFRFDVVYTSVLKRAIKTAW-IVLEELGQLHVPVIKSWRLNERHYG 78


                  ....
gi 1985320837 100 IAEG 103
Cdd:PTZ00123   79 ALQG 82
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
36-95 1.40e-06

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 47.18  E-value: 1.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985320837  36 PLSATGFRQADAAGIFLS--NVKFTHVFSSDLLRAKQTAsAIIGKnKFCKDIVIQYDARLRE 95
Cdd:COG2062    22 PLTERGRRQARAMARWLAalGLKPDRILSSPALRARQTA-EILAE-ALGLPPKVEVEDELYD 81
PRK13463 PRK13463
phosphoserine phosphatase 1;
15-147 2.12e-05

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 44.27  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  15 TISGETRYNKDKILQGQGvDEPLSATGFRQADAAGIFLSNVKFTHVFSSDLLRAKQTASAIIGKnkfcKDIVIQYDARLR 94
Cdd:PRK13463    8 TRHGETEWNVAKRMQGRK-NSALTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELIKGE----RDIPIIADEHFY 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985320837  95 ERKYGIAEGRPLSDLKamakaagEQCP-----------LFTPSGGETLDEVRARAKNFFEFLCQ 147
Cdd:PRK13463   83 EINMGIWEGQTIDDIE-------RQYPddiqlfwnephLFQSTSGENFEAVHKRVIEGMQLLLE 139
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 34-138 2.56e-04

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 41.21  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985320837  34 DEPLSATGFRQADAAGIFLSN--VKFTHVFSSDLLRAKQTASAIIGKNKFcKDIVIQYDARLRERKYGIAEGrpLSDLKA 111
Cdd:PRK01295   26 DPDLTEQGVAEAKAAGRKLKAagLKFDIAFTSALSRAQHTCQLILEELGQ-PGLETIRDQALNERDYGDLSG--LNKDDA 102

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1985320837 112 MAKAAGEQCPLF------TPSGGETLDEVRARA 138
Cdd:PRK01295  103 RAKWGEEQVHIWrrsydvPPPGGESLKDTGARV 135
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 37-96 3.62e-03

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 38.25  E-value: 3.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985320837  37 LSATGFRQADAAGIFLS--------NVKFTHVFSSDLLRAKQTASAIigkNKFCKDIVIQYDARLRER 96
Cdd:PTZ00122  126 LTELGKEQARITGKYLKeqfgeilvDKKVKAIYHSDMTRAKETAEII---SEAFPGVRLIEDPNLAEG 190
 
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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