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Conserved domains on  [gi|1246742154|ref|NP_001343043|]
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phosphoglycerate mutase/6-phosphofructo-2-kinase family [Schizosaccharomyces pombe]

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 ...
 10-171 2.15e-21

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: 87.26  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGppgnhRRI--------NQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELP 81
Cdd:pfam00300   1 LYLVRHGETEWNLE-----GRFqgrtdsplTELGREQAEALAERLAG--EPFDAIYSSPLKRARQTAEI-----IAEALG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  82 VPIKISPLFEES--GNWpcdcaMDLSSTE--KLFPDY--DFSSCYDDIYPLRrglyGTTYDENYCRAQKPLKHLASLH-E 154
Cdd:pfam00300  69 LPVEIDPRLREIdfGDW-----EGLTFEEiaERYPEEydAWLADPADYRPPG----GESLADVRARVRAALEELAARHpG 139

                         170
                  ....*....|....*..
gi 1246742154 155 KNIVVVTHSVYLRFLLR 171
Cdd:pfam00300 140 KTVLVVSHGGVIRALLA 156
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 10-171 2.15e-21

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: 87.26  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGppgnhRRI--------NQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELP 81
Cdd:pfam00300   1 LYLVRHGETEWNLE-----GRFqgrtdsplTELGREQAEALAERLAG--EPFDAIYSSPLKRARQTAEI-----IAEALG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  82 VPIKISPLFEES--GNWpcdcaMDLSSTE--KLFPDY--DFSSCYDDIYPLRrglyGTTYDENYCRAQKPLKHLASLH-E 154
Cdd:pfam00300  69 LPVEIDPRLREIdfGDW-----EGLTFEEiaERYPEEydAWLADPADYRPPG----GESLADVRARVRAALEELAARHpG 139

                         170
                  ....*....|....*..
gi 1246742154 155 KNIVVVTHSVYLRFLLR 171
Cdd:pfam00300 140 KTVLVVSHGGVIRALLA 156
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
10-208 1.69e-18

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 79.60  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGppgnhRRI--------NQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELP 81
Cdd:COG0406     4 LYLVRHGETEWNAE-----GRLqgrldvplTELGRAQARALAERLAD--IPFDAVYSSPLQRARQTAEA-----LAEALG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  82 VPIKISPLFEE--SGNWPcdcAMDLSSTEKLFPDYDFSSCYDDIYPLRRGlyGTTYDENYCRAQKPLKHLASLHE-KNIV 158
Cdd:COG0406    72 LPVEVDPRLREidFGDWE---GLTFAELEARYPEALAAWLADPAEFRPPG--GESLADVQARVRAALEELLARHPgGTVL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1246742154 159 VVTHSVYLRFLLR--EQRPEDNMNFMPPEkvfrNCEIRKynLCHTGFQWELI 208
Cdd:COG0406   147 VVTHGGVIRALLAhlLGLPLEAFWRLRID----NASVTV--LEFDDGRWRLV 192
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 10-202 4.69e-15

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: 69.27  E-value: 4.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGPP--GNH-RRINQVGIKQWEALHNWLVDNPIPIDVIVCSPLRRTLQTMEIsfksyIHKELP-VPIK 85
Cdd:cd07067     2 LYLVRHGESEWNAEGRfqGWTdVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEI-----ILEELPgLPVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  86 ISPLFEESgnwpcdcamdlssteklfpdydfsscyddiyplrrglygttydenycRAQKPLKHLASLH-EKNIVVVTHSV 164
Cdd:cd07067    77 VDPRLREA-----------------------------------------------RVLPALEELIAPHdGKNVLIVSHGG 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1246742154 165 YLRFLLR--EQRPEDNMNFMPpekvFRNCEIRKYNLCHTG 202
Cdd:cd07067   110 VLRALLAylLGLSDEDILRLN----LPNGSISVLELDENG 145
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 10-169 5.30e-13

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: 64.02  E-value: 5.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154   10 IWLVRHAQAEHNVGPPGNHRR---INQVGIKQWEALHNWLVD-NPIPIDVIVCSPLRRTLQTMEISFksyIHKELPVPIK 85
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGDTdvpLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALA---IALGLPGLRE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154   86 ISPlfeesGNWpcdCAMDLSSTEKLFPDYDFSSCYDDIYPLRRGLY-GTTYDENYCRAQKPLKHLASLH---EKNIVVVT 161
Cdd:smart00855  79 RDF-----GAW---EGLTWDEIAAKYPEEYLAAWRDPYDPAPPAPPgGESLADLVERVEPALDELIATAdasGQNVLIVS 150


                   ....*...
gi 1246742154  162 HSVYLRFL 169
Cdd:smart00855 151 HGGVIRAL 158
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
10-96 4.12e-07

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 48.51  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNV-GPPGNHR--RINQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELPVPIKI 86
Cdd:PRK15004    3 LWLVRHGETQANVdGLYSGHAptPLTARGIEQAQNLHTLLRD--VPFDLVLCSELERAQHTARL-----VLSDRQLPVHI 75

                          90
                  ....*....|..
gi 1246742154  87 SPLFEES--GNW 96
Cdd:PRK15004   76 IPELNEMffGDW 87
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 10-170 2.74e-06

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: 46.08  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGPPGNHRRI--NQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELPVPIKIS 87
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGQTDVplAESGEEQAAALREKLAD--VPFDAVYSSPLSRCRELAEI-----LAERRGLPIIKD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  88 PLFEEsgnwpcdcaMDLSSTE--------KLFPDYD-FSSCYDDIYPLRrglyGTTYDENYCRAQKPLKHLASLHE-KNI 157
Cdd:TIGR03162  74 DRLRE---------MDFGDWEgrswdeipEAYPELDaWAADWQHARPPG----GESFADFYQRVSEFLEELLKAHEgDNV 140

                         170
                  ....*....|...
gi 1246742154 158 VVVTHSVYLRFLL 170
Cdd:TIGR03162 141 LIVTHGGVIRALL 153
 
Name Accession Description Interval E-value
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 10-171 2.15e-21

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: 87.26  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGppgnhRRI--------NQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELP 81
Cdd:pfam00300   1 LYLVRHGETEWNLE-----GRFqgrtdsplTELGREQAEALAERLAG--EPFDAIYSSPLKRARQTAEI-----IAEALG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  82 VPIKISPLFEES--GNWpcdcaMDLSSTE--KLFPDY--DFSSCYDDIYPLRrglyGTTYDENYCRAQKPLKHLASLH-E 154
Cdd:pfam00300  69 LPVEIDPRLREIdfGDW-----EGLTFEEiaERYPEEydAWLADPADYRPPG----GESLADVRARVRAALEELAARHpG 139

                         170
                  ....*....|....*..
gi 1246742154 155 KNIVVVTHSVYLRFLLR 171
Cdd:pfam00300 140 KTVLVVSHGGVIRALLA 156
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
10-208 1.69e-18

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 79.60  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGppgnhRRI--------NQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELP 81
Cdd:COG0406     4 LYLVRHGETEWNAE-----GRLqgrldvplTELGRAQARALAERLAD--IPFDAVYSSPLQRARQTAEA-----LAEALG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  82 VPIKISPLFEE--SGNWPcdcAMDLSSTEKLFPDYDFSSCYDDIYPLRRGlyGTTYDENYCRAQKPLKHLASLHE-KNIV 158
Cdd:COG0406    72 LPVEVDPRLREidFGDWE---GLTFAELEARYPEALAAWLADPAEFRPPG--GESLADVQARVRAALEELLARHPgGTVL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1246742154 159 VVTHSVYLRFLLR--EQRPEDNMNFMPPEkvfrNCEIRKynLCHTGFQWELI 208
Cdd:COG0406   147 VVTHGGVIRALLAhlLGLPLEAFWRLRID----NASVTV--LEFDDGRWRLV 192
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 10-202 4.69e-15

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: 69.27  E-value: 4.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGPP--GNH-RRINQVGIKQWEALHNWLVDNPIPIDVIVCSPLRRTLQTMEIsfksyIHKELP-VPIK 85
Cdd:cd07067     2 LYLVRHGESEWNAEGRfqGWTdVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEI-----ILEELPgLPVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  86 ISPLFEESgnwpcdcamdlssteklfpdydfsscyddiyplrrglygttydenycRAQKPLKHLASLH-EKNIVVVTHSV 164
Cdd:cd07067    77 VDPRLREA-----------------------------------------------RVLPALEELIAPHdGKNVLIVSHGG 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1246742154 165 YLRFLLR--EQRPEDNMNFMPpekvFRNCEIRKYNLCHTG 202
Cdd:cd07067   110 VLRALLAylLGLSDEDILRLN----LPNGSISVLELDENG 145
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
10-86 9.87e-15

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 68.36  E-value: 9.87e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246742154  10 IWLVRHAQAEHNVGPPGNH-RRINQVGIKQWEALHNWLVDNPIPIDVIVCSPLRRTLQTMEIsfksyIHKELPVPIKI 86
Cdd:COG2062     1 LILVRHAKAEWRAPGGDDFdRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEI-----LAEALGLPPKV 73
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 10-169 5.30e-13

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: 64.02  E-value: 5.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154   10 IWLVRHAQAEHNVGPPGNHRR---INQVGIKQWEALHNWLVD-NPIPIDVIVCSPLRRTLQTMEISFksyIHKELPVPIK 85
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGDTdvpLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALA---IALGLPGLRE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154   86 ISPlfeesGNWpcdCAMDLSSTEKLFPDYDFSSCYDDIYPLRRGLY-GTTYDENYCRAQKPLKHLASLH---EKNIVVVT 161
Cdd:smart00855  79 RDF-----GAW---EGLTWDEIAAKYPEEYLAAWRDPYDPAPPAPPgGESLADLVERVEPALDELIATAdasGQNVLIVS 150


                   ....*...
gi 1246742154  162 HSVYLRFL 169
Cdd:smart00855 151 HGGVIRAL 158
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 9-86 1.53e-10

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: 57.42  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154   9 VIWLVRHAQAEHNVGP---PGNHRRINQVGIKQWEALHNWLVDNPIPIDVIVCSPLRRTLQTMEIsfksyIHKELPVPIK 85
Cdd:cd07040     1 VLYLVRHGEREPNAEGrftGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEI-----ILEGLFEGLP 75


                  .
gi 1246742154  86 I 86
Cdd:cd07040    76 V 76
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
10-96 4.12e-07

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 48.51  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNV-GPPGNHR--RINQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELPVPIKI 86
Cdd:PRK15004    3 LWLVRHGETQANVdGLYSGHAptPLTARGIEQAQNLHTLLRD--VPFDLVLCSELERAQHTARL-----VLSDRQLPVHI 75

                          90
                  ....*....|..
gi 1246742154  87 SPLFEES--GNW 96
Cdd:PRK15004   76 IPELNEMffGDW 87
PRK13463 PRK13463
phosphoserine phosphatase 1;
10-170 1.83e-06

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 46.97  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGPPGNHRR---INQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELPVPIKI 86
Cdd:PRK13463    5 VYVTRHGETEWNVAKRMQGRKnsaLTENGILQAKQLGERMKD--LSIHAIYSSPSERTLHTAEL-----IKGERDIPIIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  87 SPLFEE--SGNWPCDCAMDLsstEKLFPDyDFSSCYDDIYpLRRGLYGTTYDENYCRAQKPLKHLASLHE-KNIVVVTHS 163
Cdd:PRK13463   78 DEHFYEinMGIWEGQTIDDI---ERQYPD-DIQLFWNEPH-LFQSTSGENFEAVHKRVIEGMQLLLEKHKgESILIVSHA 152


                  ....*..
gi 1246742154 164 VYLRFLL 170
Cdd:PRK13463  153 AAAKLLV 159
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 10-170 2.74e-06

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: 46.08  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  10 IWLVRHAQAEHNVGPPGNHRRI--NQVGIKQWEALHNWLVDnpIPIDVIVCSPLRRTLQTMEIsfksyIHKELPVPIKIS 87
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGQTDVplAESGEEQAAALREKLAD--VPFDAVYSSPLSRCRELAEI-----LAERRGLPIIKD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  88 PLFEEsgnwpcdcaMDLSSTE--------KLFPDYD-FSSCYDDIYPLRrglyGTTYDENYCRAQKPLKHLASLHE-KNI 157
Cdd:TIGR03162  74 DRLRE---------MDFGDWEgrswdeipEAYPELDaWAADWQHARPPG----GESFADFYQRVSEFLEELLKAHEgDNV 140

                         170
                  ....*....|...
gi 1246742154 158 VVVTHSVYLRFLL 170
Cdd:TIGR03162 141 LIVTHGGVIRALL 153
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 11-172 5.49e-05

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 43.04  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  11 WLVRHAQAEHNVgppgnHRR--------INQVGIKQWEALHNWLVDNPiPIDVIVCSPLRRTLQTMEISfksyiHKELPV 82
Cdd:PRK07238  175 LLLRHGQTELSV-----QRRysgrgnpeLTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAA-----AKALGL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742154  83 PIKISPLFEES--GNWPcdcAMDLSSTEKLFPDyDFSSCYDDIYPLRRGlyGTTYDENYCRAQKPLKHLASLHE-KNIVV 159
Cdd:PRK07238  244 DVTVDDDLIETdfGAWE---GLTFAEAAERDPE-LHRAWLADTSVAPPG--GESFDAVARRVRRARDRLIAEYPgATVLV 317

                         170
                  ....*....|...
gi 1246742154 160 VTHSVYLRFLLRE 172
Cdd:PRK07238  318 VSHVTPIKTLLRL 330
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 10-88 1.55e-04

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 40.59  E-value: 1.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246742154  10 IWLVRHAQAEHNvGPPGNHRRINQVGIKQWEALHNWLVDNPIPIDVIVCSPLRRTLQTMEISFKsyiHKELPVPIKISP 88
Cdd:TIGR00249   3 LFIMRHGDAALD-AASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGD---CLNLPSSAEVLE 77
 
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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