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Conserved domains on  [gi|517186851|ref|WP_018375669|]
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histidine phosphatase family protein [Streptococcus orisratti]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10001383)

histidine phosphatase family protein is a probable phosphatase that may catalyze the dephosphorylation of a phosphorylated substrate involving a conserved catalytic histidine residue which becomes phosphorylated during the reaction

CATH:  3.40.50.1240
Gene Ontology:  GO:0016791
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-188 7.25e-52

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 165.50  E-value: 7.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFeeKGIRFDKVYSSTQERACDTAEIATGR--LDYQRLK 78
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERL--ADIPFDAVYSSPLQRARQTAEALAEAlgLPVEVDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  79 GLKEWDFGAFEAQPEylnPKLQDggiGYGDYFQQF----------GGENNEQVRDRMETCIRQILEEAGEEsSVLAVSHG 148
Cdd:COG0406   79 RLREIDFGDWEGLTF---AELEA---RYPEALAAWladpaefrppGGESLADVQARVRAALEELLARHPGG-TVLVVTHG 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 517186851 149 GAIAQFFRRVIHPNPDI---RKMRNCCILHFTYQDGVFELHSV 188
Cdd:COG0406  152 GVIRALLAHLLGLPLEAfwrLRIDNASVTVLEFDDGRWRLVAL 194
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-188 7.25e-52

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 165.50  E-value: 7.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFeeKGIRFDKVYSSTQERACDTAEIATGR--LDYQRLK 78
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERL--ADIPFDAVYSSPLQRARQTAEALAEAlgLPVEVDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  79 GLKEWDFGAFEAQPEylnPKLQDggiGYGDYFQQF----------GGENNEQVRDRMETCIRQILEEAGEEsSVLAVSHG 148
Cdd:COG0406   79 RLREIDFGDWEGLTF---AELEA---RYPEALAAWladpaefrppGGESLADVQARVRAALEELLARHPGG-TVLVVTHG 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 517186851 149 GAIAQFFRRVIHPNPDI---RKMRNCCILHFTYQDGVFELHSV 188
Cdd:COG0406  152 GVIRALLAHLLGLPLEAfwrLRIDNASVTVLEFDDGRWRLVAL 194
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-191 9.14e-50

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: 160.07  E-value: 9.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851    4 FYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFeeKGIRFDKVYSSTQERACDTAEIATGRLD--YQRLKGLK 81
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALGlpVEIDPRLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   82 EWDFGAFEAQPEY----LNPKLQDGGIGYGDYFQQFGGENNEQVRDRMETCIRQILEEAGEEsSVLAVSHGGAIAQFFRR 157
Cdd:pfam00300  79 EIDFGDWEGLTFEeiaeRYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARHPGK-TVLVVSHGGVIRALLAH 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 517186851  158 VIH-PNPDIRKMR--NCCILHFTYQDGVFELHSVYNP 191
Cdd:pfam00300 158 LLGlPLEALRRFPldNASLSILEFDGGGWVLVLLNDT 194
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-151 3.41e-39

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: 131.81  E-value: 3.41e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851     3 TFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYF-EEKGIRFDKVYSSTQERACDTAEIAtgrLDYQRLKGLK 81
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEAL---AIALGLPGLR 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517186851    82 EWDFGAFEAQP------EYLNPKLQDGGIGY-GDYFQQFGGENNEQVRDRMETCIRQILEEA-GEESSVLAVSHGGAI 151
Cdd:smart00855  78 ERDFGAWEGLTwdeiaaKYPEEYLAAWRDPYdPAPPAPPGGESLADLVERVEPALDELIATAdASGQNVLIVSHGGVI 155
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-181 7.69e-33

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: 115.50  E-value: 7.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   3 TFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQRLKglKE 82
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVE--VD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  83 WDFgafeaqpeylnpklqdggigygdyfqqfggenNEqvrDRMETCIRQILEEAGEEsSVLAVSHGGAIAQFFRRVIHPN 162
Cdd:cd07067   79 PRL--------------------------------RE---ARVLPALEELIAPHDGK-NVLIVSHGGVLRALLAYLLGLS 122

                        170       180
                 ....*....|....*....|..
gi 517186851 163 PDI---RKMRNCCILHFTYQDG 181
Cdd:cd07067  123 DEDilrLNLPNGSISVLELDEN 144
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-147 3.36e-22

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 92.35  E-value: 3.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   3 TFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGiRFDKVYSSTQERACDTAEIATGRL--DYQRLKGL 80
Cdd:PRK07238 173 RLLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALglDVTVDDDL 251

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517186851  81 KEWDFGAFE---------AQPEYLNPKLQDGGIgygdyfQQFGGENNEQVRDRMETCIRQILEEAGeESSVLAVSH 147
Cdd:PRK07238 252 IETDFGAWEgltfaeaaeRDPELHRAWLADTSV------APPGGESFDAVARRVRRARDRLIAEYP-GATVLVVSH 320
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 5-73 5.42e-06

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 44.44  E-value: 5.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517186851    5 YLMRHGQtrfneqGRIQGACDS--PLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLD 73
Cdd:TIGR00249   4 FIMRHGD------AALDAASDSvrPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLN 68
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-188 7.25e-52

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 165.50  E-value: 7.25e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFeeKGIRFDKVYSSTQERACDTAEIATGR--LDYQRLK 78
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGRLDVPLTELGRAQARALAERL--ADIPFDAVYSSPLQRARQTAEALAEAlgLPVEVDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  79 GLKEWDFGAFEAQPEylnPKLQDggiGYGDYFQQF----------GGENNEQVRDRMETCIRQILEEAGEEsSVLAVSHG 148
Cdd:COG0406   79 RLREIDFGDWEGLTF---AELEA---RYPEALAAWladpaefrppGGESLADVQARVRAALEELLARHPGG-TVLVVTHG 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 517186851 149 GAIAQFFRRVIHPNPDI---RKMRNCCILHFTYQDGVFELHSV 188
Cdd:COG0406  152 GVIRALLAHLLGLPLEAfwrLRIDNASVTVLEFDDGRWRLVAL 194
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-191 9.14e-50

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: 160.07  E-value: 9.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851    4 FYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFeeKGIRFDKVYSSTQERACDTAEIATGRLD--YQRLKGLK 81
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGRTDSPLTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALGlpVEIDPRLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   82 EWDFGAFEAQPEY----LNPKLQDGGIGYGDYFQQFGGENNEQVRDRMETCIRQILEEAGEEsSVLAVSHGGAIAQFFRR 157
Cdd:pfam00300  79 EIDFGDWEGLTFEeiaeRYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARHPGK-TVLVVSHGGVIRALLAH 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 517186851  158 VIH-PNPDIRKMR--NCCILHFTYQDGVFELHSVYNP 191
Cdd:pfam00300 158 LLGlPLEALRRFPldNASLSILEFDGGGWVLVLLNDT 194
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-151 3.41e-39

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: 131.81  E-value: 3.41e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851     3 TFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYF-EEKGIRFDKVYSSTQERACDTAEIAtgrLDYQRLKGLK 81
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGDTDVPLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEAL---AIALGLPGLR 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517186851    82 EWDFGAFEAQP------EYLNPKLQDGGIGY-GDYFQQFGGENNEQVRDRMETCIRQILEEA-GEESSVLAVSHGGAI 151
Cdd:smart00855  78 ERDFGAWEGLTwdeiaaKYPEEYLAAWRDPYdPAPPAPPGGESLADLVERVEPALDELIATAdASGQNVLIVSHGGVI 155
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-181 7.69e-33

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: 115.50  E-value: 7.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   3 TFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQRLKglKE 82
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVE--VD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  83 WDFgafeaqpeylnpklqdggigygdyfqqfggenNEqvrDRMETCIRQILEEAGEEsSVLAVSHGGAIAQFFRRVIHPN 162
Cdd:cd07067   79 PRL--------------------------------RE---ARVLPALEELIAPHDGK-NVLIVSHGGVLRALLAYLLGLS 122

                        170       180
                 ....*....|....*....|..
gi 517186851 163 PDI---RKMRNCCILHFTYQDG 181
Cdd:cd07067  123 DEDilrLNLPNGSISVLELDEN 144
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-190 4.87e-27

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: 100.57  E-value: 4.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   3 TFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIAtgrldyqrLKGLKE 82
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEII--------LEGLFE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  83 WDfgafeaqpeylnpklqdggigygdyfqqfggENNEQVRDRMETCIRQILEEA-GEESSVLAVSHGGAIAQFFRRVIHP 161
Cdd:cd07040   73 GL-------------------------------PVEVDPRARVLNALLELLARHlLDGKNVLIVSHGGTIRALLAALLGL 121

                        170       180       190
                 ....*....|....*....|....*....|..
gi 517186851 162 NPDI---RKMRNCCILHFTYQDGVFELHSVYN 190
Cdd:cd07040  122 SDEEilsLNLPNGSILVLELDECGGKYVRLLN 153
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 3-147 3.36e-22

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 92.35  E-value: 3.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   3 TFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGiRFDKVYSSTQERACDTAEIATGRL--DYQRLKGL 80
Cdd:PRK07238 173 RLLLLRHGQTELSVQRRYSGRGNPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALglDVTVDDDL 251

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517186851  81 KEWDFGAFE---------AQPEYLNPKLQDGGIgygdyfQQFGGENNEQVRDRMETCIRQILEEAGeESSVLAVSH 147
Cdd:PRK07238 252 IETDFGAWEgltfaeaaeRDPELHRAWLADTSV------APPGGESFDAVARRVRRARDRLIAEYP-GATVLVVSH 320
PRK13462 PRK13462
acid phosphatase; Provisional
 6-159 2.65e-16

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 73.71  E-value: 2.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   6 LMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDyQRLKGLKEWDF 85
Cdd:PRK13462  10 LLRHGETEWSKSGRHTGRTELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKLAGLTVD-EVSGLLAEWDY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  86 GAFE---------AQPEYL-----NPklqdggigygdyfqqfGGENNEQVRDRMETCIRQILEEAgEESSVLAVSHGgai 151
Cdd:PRK13462  89 GSYEglttpqireSEPDWLvwthgCP----------------GGESVAQVNERADRAVALALEHM-ESRDVVFVSHG--- 148


                 ....*...
gi 517186851 152 aQFFRRVI 159
Cdd:PRK13462 149 -HFSRAVI 155
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
1-152 9.30e-16

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 72.01  E-value: 9.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKtFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFeeKGIRFDKVYSSTQERACDTAEIATGRLDYQR--LK 78
Cdd:PRK15004   1 MR-LWLVRHGETQANVDGLYSGHAPTPLTARGIEQAQNLHTLL--RDVPFDLVLCSELERAQHTARLVLSDRQLPVhiIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  79 GLKEWDFGAFE---------AQPEYLNPKLQDggigygdyFQQ---FGGENNEQVRDRMETCIRQiLEEAGEESSVLAVS 146
Cdd:PRK15004  78 ELNEMFFGDWEmrhhrdlmqEDAENYAAWCND--------WQHaipTNGEGFQAFSQRVERFIAR-LSAFQHYQNLLIVS 148


                 ....*.
gi 517186851 147 HGGAIA 152
Cdd:PRK15004 149 HQGVLS 154
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-180 1.33e-15

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 72.07  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIrfDKVYSSTQERACDTAEI--ATGRLDYQRLK 78
Cdd:PRK03482   1 MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVAERAKELGI--THIISSDLGRTRRTAEIiaQACGCDIIFDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  79 GLKEWDFGAFEAQP-EYLNPK-----------LQDGGIGygdyfqqfGGENNEQVRDRMETCIRQILE-EAGeeSSVLAV 145
Cdd:PRK03482  79 RLRELNMGVLEKRHiDSLTEEeegwrrqlvngTVDGRIP--------EGESMQELSDRMHAALESCLElPQG--SRPLLV 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 517186851 146 SHGGAIAQFFRRVIH--PNPDIR-KMRNCCILHFTYQD 180
Cdd:PRK03482 149 SHGIALGCLVSTILGlpAWAERRlRLRNCSISRVDYQE 186
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
5-191 6.40e-13

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 63.35  E-value: 6.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   5 YLMRHGQTRFNEQGRIqgacDS--PLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYqrlkglke 82
Cdd:COG2062    2 ILVRHAKAEWRAPGGD----DFdrPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGL-------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  83 wdfgafEAQPEYLnPKLQDGGIgygdyfqqfggennEQVRDrmetcirqILEEAGEESSVLAVSHGGAIAQFFRRVIHPN 162
Cdd:COG2062   70 ------PPKVEVE-DELYDADP--------------EDLLD--------LLRELDDGETVLLVGHNPGLSELAALLAGGE 120

                        170       180       190
                 ....*....|....*....|....*....|....
gi 517186851 163 PdIRKMRNCCILHFTY-----QDGVFELHSVYNP 191
Cdd:COG2062  121 P-LDGFPTGGLAVLEFdiddlGPGKGRLVWFLTP 153
PRK13463 PRK13463
phosphoserine phosphatase 1;
1-150 1.73e-12

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 63.53  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKT-FYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFeeKGIRFDKVYSSTQERACDTAEIATGRLDYQRL-- 77
Cdd:PRK13463   1 MKTtVYVTRHGETEWNVAKRMQGRKNSALTENGILQAKQLGERM--KDLSIHAIYSSPSERTLHTAELIKGERDIPIIad 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851  78 KGLKEWDFGAFEAQ---------PE-----YLNPKLqdggigygdyFQQFGGENNEQVRDRMETCIRQILEEAGEEsSVL 143
Cdd:PRK13463  79 EHFYEINMGIWEGQtiddierqyPDdiqlfWNEPHL----------FQSTSGENFEAVHKRVIEGMQLLLEKHKGE-SIL 147


                 ....*..
gi 517186851 144 AVSHGGA 150
Cdd:PRK13463 148 IVSHAAA 154
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-68 1.47e-09

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 55.82  E-value: 1.47e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIA 68
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNLFTGWVDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTANLA 71
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
1-91 2.46e-09

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 54.92  E-value: 2.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQRLKGL 80
Cdd:PRK14116   1 MAKLVLIRHGQSEWNLSNQFTGWVDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTLHYALEESDQLWIPET 80

                         90
                 ....*....|....*.
gi 517186851  81 KEW-----DFGAFEAQ 91
Cdd:PRK14116  81 KTWrlnerHYGALQGL 96
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
6-83 3.15e-09

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 54.87  E-value: 3.15e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517186851   6 LMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQRLKGLKEW 83
Cdd:PRK14115   5 LIRHGESQWNKENRFTGWTDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWIVLDELDQMWLPVEKSW 82
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 2-86 1.85e-08

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 52.38  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   2 KTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTA-----EIATGRLDYQR 76
Cdd:PRK01295   3 RTLVLVRHGQSEWNLKNLFTGWRDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCqlileELGQPGLETIR 82

                         90
                 ....*....|
gi 517186851  77 LKGLKEWDFG 86
Cdd:PRK01295  83 DQALNERDYG 92
gpmA PRK14119
phosphoglyceromutase; Provisional
 1-83 5.94e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 48.35  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQRLKGL 80
Cdd:PRK14119   1 MPKLILCRHGQSEWNAKNLFTGWEDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTTHYILTESKQQWIPVY 80


                 ...
gi 517186851  81 KEW 83
Cdd:PRK14119  81 KSW 83
gpmA PRK14117
phosphoglyceromutase; Provisional
 1-83 2.42e-06

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 46.56  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQRLKGL 80
Cdd:PRK14117   1 MVKLVFARHGESEWNKANLFTGWADVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTTNLALEASDQLWVPVE 80


                 ...
gi 517186851  81 KEW 83
Cdd:PRK14117  81 KSW 83
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
 15-83 4.05e-06

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 45.80  E-value: 4.05e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517186851  15 NEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQRLKGLKEW 83
Cdd:PTZ00123   2 NKENRFTGWTDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAWIVLEELGQLHVPVIKSW 70
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 5-73 5.42e-06

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 44.44  E-value: 5.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517186851    5 YLMRHGQtrfneqGRIQGACDS--PLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLD 73
Cdd:TIGR00249   4 FIMRHGD------AALDAASDSvrPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLN 68
PRK06193 PRK06193
hypothetical protein; Provisional
 7-84 6.58e-06

hypothetical protein; Provisional


Pssm-ID: 235734  Cd Length: 206  Bit Score: 45.06  E-value: 6.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   7 MRHGQTRfneqgRIQGACDSP----------LTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQR 76
Cdd:PRK06193  48 FRHAATD-----RSQADQDTSdmddcstqrnLSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWETAQLAFGRHEKEI 122


                 ....*...
gi 517186851  77 LKGLKEWD 84
Cdd:PRK06193 123 RLNFLNSE 130
gpmA PRK14118
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
6-83 2.19e-05

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172608  Cd Length: 227  Bit Score: 43.81  E-value: 2.19e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517186851   6 LMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSYFEEKGIRFDKVYSSTQERACDTAEIATGRLDYQRLKGLKEW 83
Cdd:PRK14118   5 FIRHGFSEWNAKNLFTGWRDVNLTERGVEEAKAAGKKLKEAGYEFDIAFTSVLTRAIKTCNIVLEESNQLWIPQVKNW 82
PRK01112 PRK01112
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
1-68 2.28e-05

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 234902  Cd Length: 228  Bit Score: 43.56  E-value: 2.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517186851   1 MKTFYLMRHGQTRFNEQGRIQGACDSPLTDLGKEQAQAARSyfEEKGIRFDKVYSSTQERACDTAEIA 68
Cdd:PRK01112   1 MALLILLRHGQSVWNAKNLFTGWVDIPLSQQGIAEAIAAGE--KIKDLPIDCIFTSTLVRSLMTALLA 66
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 6-67 9.69e-05

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 42.10  E-value: 9.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517186851   6 LMRHGQ--TRFNEQGRIQGacdspLTDLGKEQAQAARSY----FEEKGI--RFDKVYSSTQERACDTAEI 67
Cdd:PTZ00122 107 LVRHGQyiNESSNDDNIKR-----LTELGKEQARITGKYlkeqFGEILVdkKVKAIYHSDMTRAKETAEI 171
 
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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