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Conserved domains on  [gi|1993677805|gb|QSB39273|]
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histidine phosphatase family protein [Pseudomonas hygromyciniae]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10001383)

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:0016791
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-203 9.06e-28

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 105.80  E-value: 9.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   1 MKHVRLIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQ-APDLIVASPFSRAQATAmQTVAAFPSVPFEIWP- 78
Cdd:COG0406     1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADiPFDAVYSSPLQRARQTA-EALAEALGLPVEVDPr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  79 IHEFTY--LEparciNTTVAQRRAWVEGYWAK--SDPAFTDGEGAESFLDFISRGQSFLDRLAE-HPAQDIAVFSHGQLI 153
Cdd:COG0406    80 LREIDFgdWE-----GLTFAELEARYPEALAAwlADPAEFRPPGGESLADVQARVRAALEELLArHPGGTVLVVTHGGVI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1993677805 154 NAVAWLIEcrpqkidGQAMAVWREyeitHHVPNCSGYKLtkHPDDAGWRV 203
Cdd:COG0406   155 RALLAHLL-------GLPLEAFWR----LRIDNASVTVL--EFDDGRWRL 191
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-203 9.06e-28

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 105.80  E-value: 9.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   1 MKHVRLIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQ-APDLIVASPFSRAQATAmQTVAAFPSVPFEIWP- 78
Cdd:COG0406     1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADiPFDAVYSSPLQRARQTA-EALAEALGLPVEVDPr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  79 IHEFTY--LEparciNTTVAQRRAWVEGYWAK--SDPAFTDGEGAESFLDFISRGQSFLDRLAE-HPAQDIAVFSHGQLI 153
Cdd:COG0406    80 LREIDFgdWE-----GLTFAELEARYPEALAAwlADPAEFRPPGGESLADVQARVRAALEELLArHPGGTVLVVTHGGVI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1993677805 154 NAVAWLIEcrpqkidGQAMAVWREyeitHHVPNCSGYKLtkHPDDAGWRV 203
Cdd:COG0406   155 RALLAHLL-------GLPLEAFWR----LRIDNASVTVL--EFDDGRWRL 191
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-203 1.46e-27

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: 105.37  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQAP-DLIVASPFSRAQATAmQTVAAFPSVPFEIWP-IHEFT 83
Cdd:pfam00300   3 LVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPfDAIYSSPLKRARQTA-EIIAEALGLPVEIDPrLREID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  84 Y--LEpARCINTTVAQRRAWVEGYWAksDPAFTDGEGAESFLDFISRGQSFLDRLAE-HPAQDIAVFSHGQLINAVAWLI 160
Cdd:pfam00300  82 FgdWE-GLTFEEIAERYPEEYDAWLA--DPADYRPPGGESLADVRARVRAALEELAArHPGKTVLVVSHGGVIRALLAHL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1993677805 161 ECRPQKidgqamAVWReyeitHHVPNCSGYKLTkhPDDAGWRV 203
Cdd:pfam00300 159 LGLPLE------ALRR-----FPLDNASLSILE--FDGGGWVL 188
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 6-156 6.42e-21

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: 86.75  E-value: 6.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805    6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQA----PDLIVASPFSRAQatamQTVAAFpSVPFEIWPIHE 81
Cdd:smart00855   4 LIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASLllprFDVVYSSPLKRAR----QTAEAL-AIALGLPGLRE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   82 FTY--LEPaRCINTTVAQRRAWVEGYWAKS-DPAFTDGEGAESFLDFISRGQSFLDRLAE---HPAQDIAVFSHGQLINA 155
Cdd:smart00855  79 RDFgaWEG-LTWDEIAAKYPEEYLAAWRDPyDPAPPAPPGGESLADLVERVEPALDELIAtadASGQNVLIVSHGGVIRA 157


                   .
gi 1993677805  156 V 156
Cdd:smart00855 158 L 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 6-164 4.82e-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: 4.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQA---PDLIVASPFSRAQATAMQTVAAFPSVPFEIWPIhef 82
Cdd:cd07067     4 LVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELgikFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  83 tyLEPARcinttvaqrrawVEGYWAksdpaftdgegaesfldfisrgqsflDRLAEHPAQDIAVFSHGQLINAVAWLIEC 162
Cdd:cd07067    81 --LREAR------------VLPALE--------------------------ELIAPHDGKNVLIVSHGGVLRALLAYLLG 120


                  ..
gi 1993677805 163 RP 164
Cdd:cd07067   121 LS 122
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
6-149 1.55e-12

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 64.69  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQAP-DLIVASPFSRAQATAmQTVAAFPSVPFEIWP-IHEFT 83
Cdd:PRK15004    5 LVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDVPfDLVLCSELERAQHTA-RLVLSDRQLPVHIIPeLNEMF 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993677805  84 YLEPARCINTTVAQR-----RAWVeGYWAKSDPafTDGEGaesFLDFISRGQSFLDRLAE-HPAQDIAVFSH 149
Cdd:PRK15004   84 FGDWEMRHHRDLMQEdaenyAAWC-NDWQHAIP--TNGEG---FQAFSQRVERFIARLSAfQHYQNLLIVSH 149
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 6-157 1.83e-12

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: 64.18  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQpSLDHASIPLTPKGVEQARQVAGSFAQAP-DLIVASPFSRAQATAmQTVAAFPSVPFEIWP----IH 80
Cdd:TIGR03162   3 LIRHGETDVNAGL-CYGQTDVPLAESGEEQAAALREKLADVPfDAVYSSPLSRCRELA-EILAERRGLPIIKDDrlreMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  81 eFTYLE--PARCINTTVAQRRAWVegywakSDPA---FTDGegaESFLDFISRGQSFLDRLAEHPAQD-IAVFSHGQLIN 154
Cdd:TIGR03162  81 -FGDWEgrSWDEIPEAYPELDAWA------ADWQharPPGG---ESFADFYQRVSEFLEELLKAHEGDnVLIVTHGGVIR 150


                  ...
gi 1993677805 155 AVA 157
Cdd:TIGR03162 151 ALL 153
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-203 9.06e-28

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 105.80  E-value: 9.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   1 MKHVRLIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQ-APDLIVASPFSRAQATAmQTVAAFPSVPFEIWP- 78
Cdd:COG0406     1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERLADiPFDAVYSSPLQRARQTA-EALAEALGLPVEVDPr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  79 IHEFTY--LEparciNTTVAQRRAWVEGYWAK--SDPAFTDGEGAESFLDFISRGQSFLDRLAE-HPAQDIAVFSHGQLI 153
Cdd:COG0406    80 LREIDFgdWE-----GLTFAELEARYPEALAAwlADPAEFRPPGGESLADVQARVRAALEELLArHPGGTVLVVTHGGVI 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1993677805 154 NAVAWLIEcrpqkidGQAMAVWREyeitHHVPNCSGYKLtkHPDDAGWRV 203
Cdd:COG0406   155 RALLAHLL-------GLPLEAFWR----LRIDNASVTVL--EFDDGRWRL 191
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-203 1.46e-27

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: 105.37  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQAP-DLIVASPFSRAQATAmQTVAAFPSVPFEIWP-IHEFT 83
Cdd:pfam00300   3 LVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERLAGEPfDAIYSSPLKRARQTA-EIIAEALGLPVEIDPrLREID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  84 Y--LEpARCINTTVAQRRAWVEGYWAksDPAFTDGEGAESFLDFISRGQSFLDRLAE-HPAQDIAVFSHGQLINAVAWLI 160
Cdd:pfam00300  82 FgdWE-GLTFEEIAERYPEEYDAWLA--DPADYRPPGGESLADVRARVRAALEELAArHPGKTVLVVSHGGVIRALLAHL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1993677805 161 ECRPQKidgqamAVWReyeitHHVPNCSGYKLTkhPDDAGWRV 203
Cdd:pfam00300 159 LGLPLE------ALRR-----FPLDNASLSILE--FDGGGWVL 188
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 6-156 6.42e-21

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: 86.75  E-value: 6.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805    6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQA----PDLIVASPFSRAQatamQTVAAFpSVPFEIWPIHE 81
Cdd:smart00855   4 LIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLASLllprFDVVYSSPLKRAR----QTAEAL-AIALGLPGLRE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   82 FTY--LEPaRCINTTVAQRRAWVEGYWAKS-DPAFTDGEGAESFLDFISRGQSFLDRLAE---HPAQDIAVFSHGQLINA 155
Cdd:smart00855  79 RDFgaWEG-LTWDEIAAKYPEEYLAAWRDPyDPAPPAPPGGESLADLVERVEPALDELIAtadASGQNVLIVSHGGVIRA 157


                   .
gi 1993677805  156 V 156
Cdd:smart00855 158 L 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 6-164 4.82e-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: 4.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQA---PDLIVASPFSRAQATAMQTVAAFPSVPFEIWPIhef 82
Cdd:cd07067     4 LVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELgikFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  83 tyLEPARcinttvaqrrawVEGYWAksdpaftdgegaesfldfisrgqsflDRLAEHPAQDIAVFSHGQLINAVAWLIEC 162
Cdd:cd07067    81 --LREAR------------VLPALE--------------------------ELIAPHDGKNVLIVSHGGVLRALLAYLLG 120


                  ..
gi 1993677805 163 RP 164
Cdd:cd07067   121 LS 122
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 6-78 1.00e-13

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: 67.05  E-value: 1.00e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993677805   6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQA---PDLIVASPFSRAQATAMQTVAAF-PSVPFEIWP 78
Cdd:cd07040     4 LVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALRERyikFDRIYSSPLKRAIQTAEIILEGLfEGLPVEVDP 80
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
6-149 1.55e-12

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 64.69  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQAP-DLIVASPFSRAQATAmQTVAAFPSVPFEIWP-IHEFT 83
Cdd:PRK15004    5 LVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLLRDVPfDLVLCSELERAQHTA-RLVLSDRQLPVHIIPeLNEMF 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993677805  84 YLEPARCINTTVAQR-----RAWVeGYWAKSDPafTDGEGaesFLDFISRGQSFLDRLAE-HPAQDIAVFSH 149
Cdd:PRK15004   84 FGDWEMRHHRDLMQEdaenyAAWC-NDWQHAIP--TNGEG---FQAFSQRVERFIARLSAfQHYQNLLIVSH 149
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 6-157 1.83e-12

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: 64.18  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQpSLDHASIPLTPKGVEQARQVAGSFAQAP-DLIVASPFSRAQATAmQTVAAFPSVPFEIWP----IH 80
Cdd:TIGR03162   3 LIRHGETDVNAGL-CYGQTDVPLAESGEEQAAALREKLADVPfDAVYSSPLSRCRELA-EILAERRGLPIIKDDrlreMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  81 eFTYLE--PARCINTTVAQRRAWVegywakSDPA---FTDGegaESFLDFISRGQSFLDRLAEHPAQD-IAVFSHGQLIN 154
Cdd:TIGR03162  81 -FGDWEgrSWDEIPEAYPELDAWA------ADWQharPPGG---ESFADFYQRVSEFLEELLKAHEGDnVLIVTHGGVIR 150


                  ...
gi 1993677805 155 AVA 157
Cdd:TIGR03162 151 ALL 153
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
6-78 2.33e-10

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 57.58  E-value: 2.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993677805   6 LIRHGESAANAGQPSlDHASiPLTPKGVEQARQVAGSFAQ---APDLIVASPFSRAQATAMQTVAAFP-SVPFEIWP 78
Cdd:COG2062     3 LVRHAKAEWRAPGGD-DFDR-PLTERGRRQARAMARWLAAlglKPDRILSSPALRARQTAEILAEALGlPPKVEVED 77
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 6-149 1.21e-07

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 52.29  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   6 LIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQ--APDLIVASPFSRAQATAmQTVAAFPSVPFEI------- 76
Cdd:PRK07238  176 LLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAArgGIDAVVSSPLQRARDTA-AAAAKALGLDVTVdddliet 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805  77 ----WpiHEFTYLEparcinttVAQR-----RAWVegywakSDPAfTDGEGAESFLDFISRGQSFLDRL-AEHPAQDIAV 146
Cdd:PRK07238  255 dfgaW--EGLTFAE--------AAERdpelhRAWL------ADTS-VAPPGGESFDAVARRVRRARDRLiAEYPGATVLV 317


                  ...
gi 1993677805 147 FSH 149
Cdd:PRK07238  318 VSH 320
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-62 1.08e-05

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 45.49  E-value: 1.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993677805   1 MKHVRLIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAgsfAQAPDL----IVASPFSRAQATA 62
Cdd:PRK03482    1 MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVA---ERAKELgithIISSDLGRTRRTA 63
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 6-78 3.11e-05

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 43.29  E-value: 3.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993677805   6 LIRHGESAANAGQPSLDHasipLTPKGVEQARQVAGSFAQAP---DLIVASPFSRAQATAMQTVAAF-PSVPFEIWP 78
Cdd:TIGR00249   5 IMRHGDAALDAASDSVRP----LTTNGCDESRLVAQWLKGQGveiERILVSPFVRAEQTAEIVGDCLnLPSSAEVLE 77
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 6-62 3.69e-04

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-dependent) is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440353  Cd Length: 229  Bit Score: 40.83  E-value: 3.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993677805   6 LIRHGESAANA-----GQpsLDhasIPLTPKGVEQARQVAGSFAQA---PDLIVASPFSRAQATA 62
Cdd:COG0588     5 LLRHGESEWNLenrftGW--TD---VDLSEKGRAEAKRAGRLLKEAgflFDVAYTSVLKRAIRTL 64
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
1-63 1.58e-03

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 38.93  E-value: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993677805   1 MKHVRLIRHGESAANAGQPSLDHASIPLTPKGVEQARQVAGSFAQAP-DLIVASPFSRAQATAM 63
Cdd:PRK01112    1 MALLILLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGEKIKDLPiDCIFTSTLVRSLMTAL 64
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 2-79 5.43e-03

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 37.48  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993677805   2 KHVRLIRHGESAANAgqpSLDHASIPLTPKGVEQARQVA---------GSFAQAPDLIVASPFSRAQATAMQTVAAFPSV 72
Cdd:PTZ00122  103 RQIILVRHGQYINES---SNDDNIKRLTELGKEQARITGkylkeqfgeILVDKKVKAIYHSDMTRAKETAEIISEAFPGV 179


                  ....*..
gi 1993677805  73 PFEIWPI 79
Cdd:PTZ00122  180 RLIEDPN 186
 
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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