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Conserved domains on  [gi|9966849|ref|NP_065108|]
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fructose-2,6-bisphosphatase TIGAR [Homo sapiens]

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];
6-246 4.48e-37

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 129.68  E-value: 4.48e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERSkfckDMTVKYDS 85
Cdd:COG0406   4 LYLVRHGETEWNAEGRLQGRL-DVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEAL----GLPVEVDP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849   86 RLRERKYGVVEGKALSELRA----MAKAAREECPVFTPPGGETLDQVKMRGIDFFEflcQLILKEADQkeqfsqgspsnc 161
Cdd:COG0406  79 RLREIDFGDWEGLTFAELEArypeALAAWLADPAEFRPPGGESLADVQARVRAALE---ELLARHPGG------------ 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849  162 letslaeifplgknhsskvnsdsgipglaaSVLVVSHGAYMRSLFDYFLtdlkcslpaTLSRSELMSVTPNTGmSLFIIN 241
Cdd:COG0406 144 ------------------------------TVLVVTHGGVIRALLAHLL---------GLPLEAFWRLRIDNA-SVTVLE 183


                ....*
gi 9966849  242 FEEGR 246
Cdd:COG0406 184 FDDGR 188
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
6-246 4.48e-37

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 129.68  E-value: 4.48e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERSkfckDMTVKYDS 85
Cdd:COG0406   4 LYLVRHGETEWNAEGRLQGRL-DVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEAL----GLPVEVDP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849   86 RLRERKYGVVEGKALSELRA----MAKAAREECPVFTPPGGETLDQVKMRGIDFFEflcQLILKEADQkeqfsqgspsnc 161
Cdd:COG0406  79 RLREIDFGDWEGLTFAELEArypeALAAWLADPAEFRPPGGESLADVQARVRAALE---ELLARHPGG------------ 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849  162 letslaeifplgknhsskvnsdsgipglaaSVLVVSHGAYMRSLFDYFLtdlkcslpaTLSRSELMSVTPNTGmSLFIIN 241
Cdd:COG0406 144 ------------------------------TVLVVTHGGVIRALLAHLL---------GLPLEAFWRLRIDNA-SVTVLE 183


                ....*
gi 9966849  242 FEEGR 246
Cdd:COG0406 184 FDDGR 188
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-210 4.62e-36

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: 126.94  E-value: 4.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849      6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERskfcKDMTVKYDS 85
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRT-DSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEA----LGLPVEIDP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     86 RLRERKYGVVEGKALSELRAM----AKAAREECPVFTPPGGETLDQVKMRGIDFFEFLCqlilkeadqkeqfsqgspsnc 161
Cdd:pfam00300  76 RLREIDFGDWEGLTFEEIAERypeeYDAWLADPADYRPPGGESLADVRARVRAALEELA--------------------- 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 9966849    162 letslaeifplgKNHSSKvnsdsgipglaaSVLVVSHGAYMRSLFDYFL 210
Cdd:pfam00300 135 ------------ARHPGK------------TVLVVSHGGVIRALLAHLL 159
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 6-205 1.20e-30

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 112.17  E-value: 1.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849       6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFL---NNVKFTHAFSSDLMRTKQTMHGILERSKFCkdmtvk 82
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGDT-DVPLTELGRAQAEALGRLLaslLLPRFDVVYSSPLKRARQTAEALAIALGLP------ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849      83 ydsRLRERKYGVVEGKALSELRAMAKAAREECP-------VFTPPGGETLDQVKMRGIDFFEFLCQLILKEADqkeqfsq 155
Cdd:smart00855  75 ---GLRERDFGAWEGLTWDEIAAKYPEEYLAAWrdpydpaPPAPPGGESLADLVERVEPALDELIATADASGQ------- 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 9966849     156 gspsncletslaeifplgknhsskvnsdsgipglaaSVLVVSHGAYMRSL 205
Cdd:smart00855 145 ------------------------------------NVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 6-89 9.54e-22

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: 88.53  E-value: 9.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    6 LTVVRHGETRFNKEKIIQGQgVDEPLSETGFKQAAAAGIFLNNV--KFTHAFSSDLMRTKQTMHGILERSKFCKdmtVKY 83
Cdd:cd07067   2 LYLVRHGESEWNAEGRFQGW-TDVPLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILEELPGLP---VEV 77


                ....*.
gi 9966849   84 DSRLRE 89
Cdd:cd07067  78 DPRLRE 83
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
9-131 1.51e-18

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 81.70  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     9 VRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHgILERSKFCKdmtVKYDSRLR 88
Cdd:PRK03482   7 VRHGETQWNAERRIQGQS-DSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAE-IIAQACGCD---IIFDPRLR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 9966849    89 ERKYGVVEGKALSELRAMAKAAREECPVFTP----PGGETLDQVKMR 131
Cdd:PRK03482  82 ELNMGVLEKRHIDSLTEEEEGWRRQLVNGTVdgriPEGESMQELSDR 128
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 6-137 1.21e-15

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 72.65  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849      6 LTVVRHGETRFNKeKIIQGQgVDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERskfcKDMTVKYDS 85
Cdd:TIGR03162   1 LYLIRHGETDVNA-GLCYGQ-TDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAER----RGLPIIKDD 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 9966849     86 RLRERKYGVVEGKALSEL--RAMAKAAREECPV-FTPPGGETLDQVKMRGIDFFE 137
Cdd:TIGR03162  75 RLREMDFGDWEGRSWDEIpeAYPELDAWAADWQhARPPGGESFADFYQRVSEFLE 129
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
6-246 4.48e-37

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 129.68  E-value: 4.48e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERSkfckDMTVKYDS 85
Cdd:COG0406   4 LYLVRHGETEWNAEGRLQGRL-DVPLTELGRAQARALAERLADIPFDAVYSSPLQRARQTAEALAEAL----GLPVEVDP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849   86 RLRERKYGVVEGKALSELRA----MAKAAREECPVFTPPGGETLDQVKMRGIDFFEflcQLILKEADQkeqfsqgspsnc 161
Cdd:COG0406  79 RLREIDFGDWEGLTFAELEArypeALAAWLADPAEFRPPGGESLADVQARVRAALE---ELLARHPGG------------ 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849  162 letslaeifplgknhsskvnsdsgipglaaSVLVVSHGAYMRSLFDYFLtdlkcslpaTLSRSELMSVTPNTGmSLFIIN 241
Cdd:COG0406 144 ------------------------------TVLVVTHGGVIRALLAHLL---------GLPLEAFWRLRIDNA-SVTVLE 183


                ....*
gi 9966849  242 FEEGR 246
Cdd:COG0406 184 FDDGR 188
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-210 4.62e-36

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: 126.94  E-value: 4.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849      6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERskfcKDMTVKYDS 85
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRT-DSPLTELGREQAEALAERLAGEPFDAIYSSPLKRARQTAEIIAEA----LGLPVEIDP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     86 RLRERKYGVVEGKALSELRAM----AKAAREECPVFTPPGGETLDQVKMRGIDFFEFLCqlilkeadqkeqfsqgspsnc 161
Cdd:pfam00300  76 RLREIDFGDWEGLTFEEIAERypeeYDAWLADPADYRPPGGESLADVRARVRAALEELA--------------------- 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 9966849    162 letslaeifplgKNHSSKvnsdsgipglaaSVLVVSHGAYMRSLFDYFL 210
Cdd:pfam00300 135 ------------ARHPGK------------TVLVVSHGGVIRALLAHLL 159
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 6-205 1.20e-30

Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 112.17  E-value: 1.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849       6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFL---NNVKFTHAFSSDLMRTKQTMHGILERSKFCkdmtvk 82
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGDT-DVPLTELGRAQAEALGRLLaslLLPRFDVVYSSPLKRARQTAEALAIALGLP------ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849      83 ydsRLRERKYGVVEGKALSELRAMAKAAREECP-------VFTPPGGETLDQVKMRGIDFFEFLCQLILKEADqkeqfsq 155
Cdd:smart00855  75 ---GLRERDFGAWEGLTWDEIAAKYPEEYLAAWrdpydpaPPAPPGGESLADLVERVEPALDELIATADASGQ------- 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 9966849     156 gspsncletslaeifplgknhsskvnsdsgipglaaSVLVVSHGAYMRSL 205
Cdd:smart00855 145 ------------------------------------NVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 6-89 9.54e-22

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: 88.53  E-value: 9.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    6 LTVVRHGETRFNKEKIIQGQgVDEPLSETGFKQAAAAGIFLNNV--KFTHAFSSDLMRTKQTMHGILERSKFCKdmtVKY 83
Cdd:cd07067   2 LYLVRHGESEWNAEGRFQGW-TDVPLTEKGREQARALGKRLKELgiKFDRIYSSPLKRAIQTAEIILEELPGLP---VEV 77


                ....*.
gi 9966849   84 DSRLRE 89
Cdd:cd07067  78 DPRLRE 83
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
9-131 1.51e-18

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 81.70  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     9 VRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHgILERSKFCKdmtVKYDSRLR 88
Cdd:PRK03482   7 VRHGETQWNAERRIQGQS-DSPLTAKGEQQAMQVAERAKELGITHIISSDLGRTRRTAE-IIAQACGCD---IIFDPRLR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 9966849    89 ERKYGVVEGKALSELRAMAKAAREECPVFTP----PGGETLDQVKMR 131
Cdd:PRK03482  82 ELNMGVLEKRHIDSLTEEEEGWRRQLVNGTVdgriPEGESMQELSDR 128
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 6-88 1.85e-17

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: 77.07  E-value: 1.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFL--NNVKFTHAFSSDLMRTKQTMHGILErsKFCKDMTVKY 83
Cdd:cd07040   2 LYLVRHGEREPNAEGRFTGWG-DGPLTEKGRQQARELGKALreRYIKFDRIYSSPLKRAIQTAEIILE--GLFEGLPVEV 78


                ....*
gi 9966849   84 DSRLR 88
Cdd:cd07040  79 DPRAR 83
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 6-137 1.21e-15

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 72.65  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849      6 LTVVRHGETRFNKeKIIQGQgVDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERskfcKDMTVKYDS 85
Cdd:TIGR03162   1 LYLIRHGETDVNA-GLCYGQ-TDVPLAESGEEQAAALREKLADVPFDAVYSSPLSRCRELAEILAER----RGLPIIKDD 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 9966849     86 RLRERKYGVVEGKALSEL--RAMAKAAREECPV-FTPPGGETLDQVKMRGIDFFE 137
Cdd:TIGR03162  75 RLREMDFGDWEGRSWDEIpeAYPELDAWAADWQhARPPGGESFADFYQRVSEFLE 129
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 2-131 4.65e-11

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 62.30  E-value: 4.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     2 ARFALtvVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFL-NNVKFTHAFSSDLMRTKQTMHGILERskFCKDMT 80
Cdd:PRK07238 172 TRLLL--LRHGQTELSVQRRYSGRG-NPELTEVGRRQAAAAARYLaARGGIDAVVSSPLQRARDTAAAAAKA--LGLDVT 246

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 9966849    81 VkyDSRLRERKYGVVEGKALSELRAMAKAAREEC---PVFTPPGGETLDQVKMR 131
Cdd:PRK07238 247 V--DDDLIETDFGAWEGLTFAEAAERDPELHRAWladTSVAPPGGESFDAVARR 298
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 6-125 4.41e-10

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 57.78  E-value: 4.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNN--VKFTHAFSSDLMRTKQTMHGILERSKFcKDMTVKY 83
Cdd:PRK01295   5 LVLVRHGQSEWNLKNLFTGWR-DPDLTEQGVAEAKAAGRKLKAagLKFDIAFTSALSRAQHTCQLILEELGQ-PGLETIR 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 9966849    84 DSRLRERKYGVVEGkaLSELRAMAKAAREECPVF------TPPGGETL 125
Cdd:PRK01295  83 DQALNERDYGDLSG--LNKDDARAKWGEEQVHIWrrsydvPPPGGESL 128
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
1-98 5.72e-09

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 54.92  E-value: 5.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     1 MARfaLTVVRHGETRFNKEKIIQGQgVDEPLSETGFKQAAAAGIFLNN--VKFTHAFSSDLMRTKQTMHGILERSKFCKD 78
Cdd:PRK14116   1 MAK--LVLIRHGQSEWNLSNQFTGW-VDVDLSEKGVEEAKKAGRLIKEagLEFDQAYTSVLTRAIKTLHYALEESDQLWI 77

                         90       100
                 ....*....|....*....|
gi 9966849    79 MTVKyDSRLRERKYGVVEGK 98
Cdd:PRK14116  78 PETK-TWRLNERHYGALQGL 96
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 17-97 1.20e-08

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 54.28  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    17 NKEKIIQGQgVDEPLSETGFKQAAAAGIFL--NNVKFTHAFSSDLMRTKQTMHGILERSKfCKDMTVKYDSRLRERKYGV 94
Cdd:PTZ00123   2 NKENRFTGW-TDVPLSEKGVQEAREAGKLLkeKGFRFDVVYTSVLKRAIKTAWIVLEELG-QLHVPVIKSWRLNERHYGA 79


                 ...
gi 9966849    95 VEG 97
Cdd:PTZ00123  80 LQG 82
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
6-124 1.92e-08

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 53.13  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     6 LTVVRHGETRFNKEKIIQGQgVDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERSkfckDMTVKYDS 85
Cdd:PRK15004   3 LWLVRHGETQANVDGLYSGH-APTPLTARGIEQAQNLHTLLRDVPFDLVLCSELERAQHTARLVLSDR----QLPVHIIP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 9966849    86 RLRERKYGVvegkalSELRAMAKAAREECPVFT----------PPGGET 124
Cdd:PRK15004  78 ELNEMFFGD------WEMRHHRDLMQEDAENYAawcndwqhaiPTNGEG 120
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
1-137 3.59e-08

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 52.80  E-value: 3.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     1 MARfaLTVVRHGETRFNKEKIIQGQgVDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTM------HG------ 68
Cdd:PRK01112   1 MAL--LILLRHGQSVWNAKNLFTGW-VDIPLSQQGIAEAIAAGEKIKDLPIDCIFTSTLVRSLMTAllamtnHSsgkipy 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    69 ILERSKFCKDMT-VKYD------------SRLRERKYGVVEGKALSElrAMAKAAREECPVF------TPPGGETLDQVK 129
Cdd:PRK01112  78 IVHEEDDKKWMSrIYSDeepeqmiplfqsSALNERMYGELQGKNKAE--TAEKFGEEQVKLWrrsyktAPPQGESLEDTG 155


                 ....*...
gi 9966849   130 MRGIDFFE 137
Cdd:PRK01112 156 QRTLPYFQ 163
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
6-99 4.09e-08

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 52.55  E-value: 4.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     6 LTVVRHGETRFNKEKIIQGQgVDEPLSETGFKQAAAAGIFL--NNVKFTHAFSSDLMRTKQTMHGILERSkfckDMT--- 80
Cdd:PRK14115   3 LVLIRHGESQWNKENRFTGW-TDVDLSEKGVSEAKAAGKLLkeEGYTFDVAYTSVLKRAIRTLWIVLDEL----DQMwlp 77

                         90       100
                 ....*....|....*....|.
gi 9966849    81 VKYDSRLRERKYGVVEG--KA 99
Cdd:PRK14115  78 VEKSWRLNERHYGALQGlnKA 98
gpmA PRK14117
phosphoglyceromutase; Provisional
 6-113 8.23e-08

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 51.56  E-value: 8.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLN--NVKFTHAFSSDLMRTKQTMHGILERSKFCKdMTVKY 83
Cdd:PRK14117   4 LVFARHGESEWNKANLFTGWA-DVDLSEKGTQQAIDAGKLIKeaGIEFDLAFTSVLKRAIKTTNLALEASDQLW-VPVEK 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 9966849    84 DSRLRERKYGVVEGKALSElrAMAKAAREE 113
Cdd:PRK14117  82 SWRLNERHYGGLTGKNKAE--AAEQFGDEQ 109
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-105 3.08e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 50.04  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     1 MARFALTVVRHGETRFNKEKIIQGQgVDEPLSETGFKQAAAAGIFL--NNVKFTHAFSSDLMRTKQTMHGILERSkfckD 78
Cdd:PRK14120   2 MMTYTLVLLRHGESEWNAKNLFTGW-VDVDLTEKGEAEAKRGGELLaeAGVLPDVVYTSLLRRAIRTANLALDAA----D 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 9966849    79 MT---VKYDSRLRERKYGVVEGKALSELRA 105
Cdd:PRK14120  77 RLwipVRRSWRLNERHYGALQGKDKAETKA 106
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
6-109 1.22e-06

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 47.18  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849    6 LTVVRHGETRFNkekiiQGQGVDE--PLSETGFKQAAAAGIFL--NNVKFTHAFSSDLMRTKQTMHGILERSKFckDMTV 81
Cdd:COG2062   1 LILVRHAKAEWR-----APGGDDFdrPLTERGRRQARAMARWLaaLGLKPDRILSSPALRARQTAEILAEALGL--PPKV 73

                        90       100
                ....*....|....*....|....*...
gi 9966849   82 KYDSRLrerkYGVVEGKALSELRAMAKA 109
Cdd:COG2062  74 EVEDEL----YDADPEDLLDLLRELDDG 97
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
6-97 1.56e-06

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 48.04  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     6 LTVVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFL--NNVKFTHAFSSDLMRTKQTMHGILERSKFCKDMTVKy 83
Cdd:PRK14118   3 LVFIRHGFSEWNAKNLFTGWR-DVNLTERGVEEAKAAGKKLkeAGYEFDIAFTSVLTRAIKTCNIVLEESNQLWIPQVK- 80

                         90
                 ....*....|....
gi 9966849    84 DSRLRERKYGVVEG 97
Cdd:PRK14118  81 NWRLNERHYGALQG 94
PRK13463 PRK13463
phosphoserine phosphatase 1;
8-141 8.47e-06

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 45.43  E-value: 8.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     8 VVRHGETRFNKEKIIQGQGvDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGIlersKFCKDMTVKYDSRL 87
Cdd:PRK13463   7 VTRHGETEWNVAKRMQGRK-NSALTENGILQAKQLGERMKDLSIHAIYSSPSERTLHTAELI----KGERDIPIIADEHF 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 9966849    88 RERKYGVVEGKALSELRAMAKAARE----ECPVFTPPGGETLDQVKMRGIDFFEFLCQ 141
Cdd:PRK13463  82 YEINMGIWEGQTIDDIERQYPDDIQlfwnEPHLFQSTSGENFEAVHKRVIEGMQLLLE 139
PRK13462 PRK13462
acid phosphatase; Provisional
 6-131 7.30e-04

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 39.81  E-value: 7.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966849     6 LTVVRHGETRFNKEKIIQGqGVDEPLSETGFKQAAAAGIFLNNVKFTH--AFSSDLMRTKQTMHgilerskfCKDMTV-K 82
Cdd:PRK13462   8 LLLLRHGETEWSKSGRHTG-RTELELTETGRTQAELAGQALGELELDDplVISSPRRRALDTAK--------LAGLTVdE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 9966849    83 YDSRLRERKYGVVEGKALSELramakaaREECP---VFTP--PGGETLDQVKMR 131
Cdd:PRK13462  79 VSGLLAEWDYGSYEGLTTPQI-------RESEPdwlVWTHgcPGGESVAQVNER 125
 
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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