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Conserved domains on  [gi|880806349|ref|WP_048658527|]
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histidine phosphatase family protein [Vibrio crassostreae]

Protein Classification

histidine phosphatase family protein( domain architecture ID 27749)

histidine phosphatase family protein contains a conserved His residue that is transiently phosphorylated during the catalytic cycle

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HP super family cl11399
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 9-185 2.69e-48

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.


The actual alignment was detected with superfamily member TIGR03162:

Pssm-ID: 472174 [Multi-domain]  Cd Length: 177  Bit Score: 155.86  E-value: 2.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349    9 IYLLRHGKVEGKAALN-GLSDVLVSPELQEQiCQALAT--QDITFDSVVTSPLRRCGGLASLYAERMSVPLSVAPGFQEM 85
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCyGQTDVPLAESGEEQ-AAALREklADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDRLREM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   86 NFGEVDGVPFDELEDKWGMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLLNNPS-DNILLVTHGGVIRILLAECLDI 164
Cdd:TIGR03162  80 DFGDWEGRSWDEIPEAYPELDAWAADWQHARPPGGESFADFYQRVSEFLEELLKAHEgDNVLIVTHGGVIRALLAHLLGL 159

                         170       180
                  ....*....|....*....|.
gi 880806349  165 DwkNPSLYSkLSIENASITHI 185
Cdd:TIGR03162 160 P--LEQWWS-FAVEYGSITLI 177
 
Name Accession Description Interval E-value
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 9-185 2.69e-48

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: 155.86  E-value: 2.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349    9 IYLLRHGKVEGKAALN-GLSDVLVSPELQEQiCQALAT--QDITFDSVVTSPLRRCGGLASLYAERMSVPLSVAPGFQEM 85
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCyGQTDVPLAESGEEQ-AAALREklADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDRLREM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   86 NFGEVDGVPFDELEDKWGMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLLNNPS-DNILLVTHGGVIRILLAECLDI 164
Cdd:TIGR03162  80 DFGDWEGRSWDEIPEAYPELDAWAADWQHARPPGGESFADFYQRVSEFLEELLKAHEgDNVLIVTHGGVIRALLAHLLGL 159

                         170       180
                  ....*....|....*....|.
gi 880806349  165 DwkNPSLYSkLSIENASITHI 185
Cdd:TIGR03162 160 P--LEQWWS-FAVEYGSITLI 177
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
6-189 2.47e-44

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 146.24  E-value: 2.47e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   6 TKNIYLLRHGKVEGKAA--LNGLSDVLVSPELQEQIcQALAT--QDITFDSVVTSPLRRCGGLASLYAERMSVPLSVAPG 81
Cdd:COG0406    1 MTRLYLVRHGETEWNAEgrLQGRLDVPLTELGRAQA-RALAErlADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  82 FQEMNFGEVDGVPFDELEDKW-GMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLL-NNPSDNILLVTHGGVIRILLA 159
Cdd:COG0406   80 LREIDFGDWEGLTFAELEARYpEALAAWLADPAEFRPPGGESLADVQARVRAALEELLaRHPGGTVLVVTHGGVIRALLA 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 880806349 160 ECLDIDwknPSLYSKLSIENASITHIQITQ 189
Cdd:COG0406  160 HLLGLP---LEAFWRLRIDNASVTVLEFDD 186
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 9-188 4.83e-39

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: 132.72  E-value: 4.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349    9 IYLLRHGKVEGKAA--LNGLSDVLVSPELQEQIcQALAT--QDITFDSVVTSPLRRCGGLASLYAERMSVPLSVAPGFQE 84
Cdd:pfam00300   1 LYLVRHGETEWNLEgrFQGRTDSPLTELGREQA-EALAErlAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   85 MNFGEVDGVPFDELEDKW-GMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLLN-NPSDNILLVTHGGVIRILLAECL 162
Cdd:pfam00300  80 IDFGDWEGLTFEEIAERYpEEYDAWLADPADYRPPGGESLADVRARVRAALEELAArHPGKTVLVVSHGGVIRALLAHLL 159

                         170       180
                  ....*....|....*....|....*.
gi 880806349  163 DIDwknPSLYSKLSIENASITHIQIT 188
Cdd:pfam00300 160 GLP---LEALRRFPLDNASLSILEFD 182
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 9-157 8.47e-28

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: 102.54  E-value: 8.47e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349     9 IYLLRHGKVEGKAA--LNGLSDVLVSPELQEQIcQALATQ-----DITFDSVVTSPLRRCGGLASLYAERMSVPlsvapG 81
Cdd:smart00855   2 LYLIRHGETEWNREgrLYGDTDVPLTELGRAQA-EALGRLlasllLPRFDVVYSSPLKRARQTAEALAIALGLP-----G 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349    82 FQEMNFGEVDGVPFDELEDKWG----MLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLLN---NPSDNILLVTHGGVI 154
Cdd:smart00855  76 LRERDFGAWEGLTWDEIAAKYPeeylAAWRDPYDPAPPAPPGGESLADLVERVEPALDELIAtadASGQNVLIVSHGGVI 155


                   ...
gi 880806349   155 RIL 157
Cdd:smart00855 156 RAL 158
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 11-183 4.08e-19

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 83.87  E-value: 4.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  11 LLRHGKVEGKAA--LNGLSDvlvsPEL----QEQICQA---LATQDiTFDSVVTSPLRRCGGLASLYAERMSVPLSVAPG 81
Cdd:PRK07238 176 LLRHGQTELSVQrrYSGRGN----PELtevgRRQAAAAaryLAARG-GIDAVVSSPLQRARDTAAAAAKALGLDVTVDDD 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  82 FQEMNFGEVDGVPFDELEDKWGMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLL-NNPSDNILLVTHGGVIRILLAE 160
Cdd:PRK07238 251 LIETDFGAWEGLTFAEAAERDPELHRAWLADTSVAPPGGESFDAVARRVRRARDRLIaEYPGATVLVVSHVTPIKTLLRL 330

                        170       180
                 ....*....|....*....|...
gi 880806349 161 CLDidwKNPSLYSKLSIENASIT 183
Cdd:PRK07238 331 ALD---AGPGVLYRLHLDLASLS 350
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 8-187 2.97e-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: 77.75  E-value: 2.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   8 NIYLLRHGKVEGKAA--LNGLSDVLVSPELQEQ---ICQALATQDITFDSVVTSPLRRCGGLASLYAERMS-VPLSVAPG 81
Cdd:cd07067    1 RLYLVRHGESEWNAEgrFQGWTDVPLTEKGREQaraLGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPgLPVEVDPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  82 FQEmnfgevdgvpfdeledkwgmletfwqnpanhqltgaeslqsfhDRVTQAWSQLLNNPSD-NILLVTHGGVIRILLAE 160
Cdd:cd07067   81 LRE-------------------------------------------ARVLPALEELIAPHDGkNVLIVSHGGVLRALLAY 117

                        170       180
                 ....*....|....*....|....*..
gi 880806349 161 CLDIDWKNpslYSKLSIENASITHIQI 187
Cdd:cd07067  118 LLGLSDED---ILRLNLPNGSISVLEL 141
 
Name Accession Description Interval E-value
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 9-185 2.69e-48

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: 155.86  E-value: 2.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349    9 IYLLRHGKVEGKAALN-GLSDVLVSPELQEQiCQALAT--QDITFDSVVTSPLRRCGGLASLYAERMSVPLSVAPGFQEM 85
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCyGQTDVPLAESGEEQ-AAALREklADVPFDAVYSSPLSRCRELAEILAERRGLPIIKDDRLREM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   86 NFGEVDGVPFDELEDKWGMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLLNNPS-DNILLVTHGGVIRILLAECLDI 164
Cdd:TIGR03162  80 DFGDWEGRSWDEIPEAYPELDAWAADWQHARPPGGESFADFYQRVSEFLEELLKAHEgDNVLIVTHGGVIRALLAHLLGL 159

                         170       180
                  ....*....|....*....|.
gi 880806349  165 DwkNPSLYSkLSIENASITHI 185
Cdd:TIGR03162 160 P--LEQWWS-FAVEYGSITLI 177
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
6-189 2.47e-44

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 146.24  E-value: 2.47e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   6 TKNIYLLRHGKVEGKAA--LNGLSDVLVSPELQEQIcQALAT--QDITFDSVVTSPLRRCGGLASLYAERMSVPLSVAPG 81
Cdd:COG0406    1 MTRLYLVRHGETEWNAEgrLQGRLDVPLTELGRAQA-RALAErlADIPFDAVYSSPLQRARQTAEALAEALGLPVEVDPR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  82 FQEMNFGEVDGVPFDELEDKW-GMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLL-NNPSDNILLVTHGGVIRILLA 159
Cdd:COG0406   80 LREIDFGDWEGLTFAELEARYpEALAAWLADPAEFRPPGGESLADVQARVRAALEELLaRHPGGTVLVVTHGGVIRALLA 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 880806349 160 ECLDIDwknPSLYSKLSIENASITHIQITQ 189
Cdd:COG0406  160 HLLGLP---LEAFWRLRIDNASVTVLEFDD 186
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 9-188 4.83e-39

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: 132.72  E-value: 4.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349    9 IYLLRHGKVEGKAA--LNGLSDVLVSPELQEQIcQALAT--QDITFDSVVTSPLRRCGGLASLYAERMSVPLSVAPGFQE 84
Cdd:pfam00300   1 LYLVRHGETEWNLEgrFQGRTDSPLTELGREQA-EALAErlAGEPFDAIYSSPLKRARQTAEIIAEALGLPVEIDPRLRE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   85 MNFGEVDGVPFDELEDKW-GMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLLN-NPSDNILLVTHGGVIRILLAECL 162
Cdd:pfam00300  80 IDFGDWEGLTFEEIAERYpEEYDAWLADPADYRPPGGESLADVRARVRAALEELAArHPGKTVLVVSHGGVIRALLAHLL 159

                         170       180
                  ....*....|....*....|....*.
gi 880806349  163 DIDwknPSLYSKLSIENASITHIQIT 188
Cdd:pfam00300 160 GLP---LEALRRFPLDNASLSILEFD 182
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 9-157 8.47e-28

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: 102.54  E-value: 8.47e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349     9 IYLLRHGKVEGKAA--LNGLSDVLVSPELQEQIcQALATQ-----DITFDSVVTSPLRRCGGLASLYAERMSVPlsvapG 81
Cdd:smart00855   2 LYLIRHGETEWNREgrLYGDTDVPLTELGRAQA-EALGRLlasllLPRFDVVYSSPLKRARQTAEALAIALGLP-----G 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349    82 FQEMNFGEVDGVPFDELEDKWG----MLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLLN---NPSDNILLVTHGGVI 154
Cdd:smart00855  76 LRERDFGAWEGLTWDEIAAKYPeeylAAWRDPYDPAPPAPPGGESLADLVERVEPALDELIAtadASGQNVLIVSHGGVI 155


                   ...
gi 880806349   155 RIL 157
Cdd:smart00855 156 RAL 158
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 11-183 4.08e-19

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 83.87  E-value: 4.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  11 LLRHGKVEGKAA--LNGLSDvlvsPEL----QEQICQA---LATQDiTFDSVVTSPLRRCGGLASLYAERMSVPLSVAPG 81
Cdd:PRK07238 176 LLRHGQTELSVQrrYSGRGN----PELtevgRRQAAAAaryLAARG-GIDAVVSSPLQRARDTAAAAAKALGLDVTVDDD 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  82 FQEMNFGEVDGVPFDELEDKWGMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLL-NNPSDNILLVTHGGVIRILLAE 160
Cdd:PRK07238 251 LIETDFGAWEGLTFAEAAERDPELHRAWLADTSVAPPGGESFDAVARRVRRARDRLIaEYPGATVLVVSHVTPIKTLLRL 330

                        170       180
                 ....*....|....*....|...
gi 880806349 161 CLDidwKNPSLYSKLSIENASIT 183
Cdd:PRK07238 331 ALD---AGPGVLYRLHLDLASLS 350
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 8-187 2.97e-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: 77.75  E-value: 2.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   8 NIYLLRHGKVEGKAA--LNGLSDVLVSPELQEQ---ICQALATQDITFDSVVTSPLRRCGGLASLYAERMS-VPLSVAPG 81
Cdd:cd07067    1 RLYLVRHGESEWNAEgrFQGWTDVPLTEKGREQaraLGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPgLPVEVDPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  82 FQEmnfgevdgvpfdeledkwgmletfwqnpanhqltgaeslqsfhDRVTQAWSQLLNNPSD-NILLVTHGGVIRILLAE 160
Cdd:cd07067   81 LRE-------------------------------------------ARVLPALEELIAPHDGkNVLIVSHGGVLRALLAY 117

                        170       180
                 ....*....|....*....|....*..
gi 880806349 161 CLDIDWKNpslYSKLSIENASITHIQI 187
Cdd:cd07067  118 LLGLSDED---ILRLNLPNGSISVLEL 141
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
9-164 9.92e-18

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 77.40  E-value: 9.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   9 IYLLRHGKVEGKAA--LNGLSDVLVSPELQEQiCQALAT--QDITFDSVVTSPLRRCGGLASLYAERMSVPLSVAPGFQE 84
Cdd:PRK15004   3 LWLVRHGETQANVDglYSGHAPTPLTARGIEQ-AQNLHTllRDVPFDLVLCSELERAQHTARLVLSDRQLPVHIIPELNE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  85 MNFGEVDGVPFDEL--ED--KWGMLETFWQNPANhqlTGAESLQSFHDRVTQAWSQLLN-NPSDNILLVTHGGVIRILLA 159
Cdd:PRK15004  82 MFFGDWEMRHHRDLmqEDaeNYAAWCNDWQHAIP---TNGEGFQAFSQRVERFIARLSAfQHYQNLLIVSHQGVLSLLIA 158


                 ....*
gi 880806349 160 ECLDI 164
Cdd:PRK15004 159 RLLGM 163
PRK13463 PRK13463
phosphoserine phosphatase 1;
9-191 1.69e-13

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 66.23  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   9 IYLLRHGKVEGKAA--LNGLSD-------VLVSPELQEQIcqalatQDITFDSVVTSPLRRCGGLASLYAERMSVPLSVA 79
Cdd:PRK13463   5 VYVTRHGETEWNVAkrMQGRKNsaltengILQAKQLGERM------KDLSIHAIYSSPSERTLHTAELIKGERDIPIIAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  80 PGFQEMNFGEVDGVPFDELEDKW-GMLETFWQNPANHQLTGAESLQSFHDRVTQAWSQLL-NNPSDNILLVTHGGVIRIL 157
Cdd:PRK13463  79 EHFYEINMGIWEGQTIDDIERQYpDDIQLFWNEPHLFQSTSGENFEAVHKRVIEGMQLLLeKHKGESILIVSHAAAAKLL 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 880806349 158 LAECLDID----WKNPSLYS-KLSIENASITHIQITQFA 191
Cdd:PRK13463 159 VGHFAGIEienvWDDPFMHSaSLSIIEFEDGKGEVKQFA 197
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 9-197 4.96e-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: 63.97  E-value: 4.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   9 IYLLRHGKVEGKAALN--GLSDVLVSPE--LQ-EQICQALATQDITFDSVVTSPLRRCgglaslyaeRMSVplsvapgfq 83
Cdd:cd07040    2 LYLVRHGEREPNAEGRftGWGDGPLTEKgrQQaRELGKALRERYIKFDRIYSSPLKRA---------IQTA--------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  84 emnfgevdgvpfdeledkWGMLETFWQNPANHQLTGaeslqsfhDRVTQAWSQLLNN---PSDNILLVTHGGVIRILLAE 160
Cdd:cd07040   64 ------------------EIILEGLFEGLPVEVDPR--------ARVLNALLELLARhllDGKNVLIVSHGGTIRALLAA 117

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 880806349 161 CLDIDWKNPslySKLSIENASITHIQITQFAQSFISV 197
Cdd:cd07040  118 LLGLSDEEI---LSLNLPNGSILVLELDECGGKYVRL 151
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
9-189 3.03e-07

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 48.96  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   9 IYLLRHGKVEGKAA--LNGLSDVLVSP--ELQ-EQICQALATQDITfdSVVTSPLRRCGGLASLYAERMSVPLSVAPGFQ 83
Cdd:PRK03482   4 VYLVRHGETQWNAErrIQGQSDSPLTAkgEQQaMQVAERAKELGIT--HIISSDLGRTRRTAEIIAQACGCDIIFDPRLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  84 EMNFGEVDGVPFDELEDKwgmlETFWQ-----NPANHQLTGAESLQSFHDRVTQAWSQLLNNPSDN-ILLVTHGGVIRIL 157
Cdd:PRK03482  82 ELNMGVLEKRHIDSLTEE----EEGWRrqlvnGTVDGRIPEGESMQELSDRMHAALESCLELPQGSrPLLVSHGIALGCL 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 880806349 158 LAECLDIDwknPSLYSKLSIENASITHIQITQ 189
Cdd:PRK03482 158 VSTILGLP---AWAERRLRLRNCSISRVDYQE 186
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
9-78 5.59e-04

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 38.70  E-value: 5.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349   9 IYLLRHGKVEGKAA--------LN--GLSDVlvspelqEQICQALATQDITFDSVVTSPLRRCGGLASLYAERMSVPLSV 78
Cdd:COG2062    1 LILVRHAKAEWRAPggddfdrpLTerGRRQA-------RAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKV 73
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 11-103 1.10e-03

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 38.52  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880806349  11 LLRHGKVEG--KAALNGLSDvlvsPELQEQ-------ICQALATQDITFDSVVTSPLRRCGGLASLYAERM---SVPLSV 78
Cdd:PRK01295   7 LVRHGQSEWnlKNLFTGWRD----PDLTEQgvaeakaAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEELgqpGLETIR 82

                         90       100
                 ....*....|....*....|....*
gi 880806349  79 APGFQEMNFGEVDGVPFDELEDKWG 103
Cdd:PRK01295  83 DQALNERDYGDLSGLNKDDARAKWG 107
 
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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