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Conserved domains on  [gi|765131098|ref|XP_011477820|]
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serine/threonine-protein phosphatase PGAM5, mitochondrial isoform X2 [Oryzias latipes]

Protein Classification

histidine phosphatase family protein( domain architecture ID 27749)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HP super family cl11399
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 68-294 4.84e-81

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


The actual alignment was detected with superfamily member PTZ00122:

Pssm-ID: 472174  Cd Length: 299  Bit Score: 247.03  E-value: 4.84e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  68 WDFNWDKRDPSVLS-NGKRkessTEDPSSEQdnskpkatRNILLIRHSQYNLSGTSD-KDRILTPLGREQAEFTGQRLAA 145
Cdd:PTZ00122  76 WNEDWDGNYKHRPKaRGKR----ADKSASHQ--------RQIILVRHGQYINESSNDdNIKRLTELGKEQARITGKYLKE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 146 LG------LKYDVLIHSSMARATETAQILSKYLPGVDLVSCDMLREGAPIQPVPPVTHWKPDA-VYHEDGARIEAAFRRY 218
Cdd:PTZ00122 144 QFgeilvdKKVKAIYHSDMTRAKETAEIISEAFPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIeEILEDMKRIEAAFEKY 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765131098 219 IHRadPKQKEDSYEIIVCHANVIRYFVCRALQFPPEGWLRMGLNNGSITWITIRPSGRVALRTLGDTGFMPVDKVT 294
Cdd:PTZ00122 224 FHR--PVEDEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMVT 297
 
Name Accession Description Interval E-value
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 68-294 4.84e-81

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 247.03  E-value: 4.84e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  68 WDFNWDKRDPSVLS-NGKRkessTEDPSSEQdnskpkatRNILLIRHSQYNLSGTSD-KDRILTPLGREQAEFTGQRLAA 145
Cdd:PTZ00122  76 WNEDWDGNYKHRPKaRGKR----ADKSASHQ--------RQIILVRHGQYINESSNDdNIKRLTELGKEQARITGKYLKE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 146 LG------LKYDVLIHSSMARATETAQILSKYLPGVDLVSCDMLREGAPIQPVPPVTHWKPDA-VYHEDGARIEAAFRRY 218
Cdd:PTZ00122 144 QFgeilvdKKVKAIYHSDMTRAKETAEIISEAFPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIeEILEDMKRIEAAFEKY 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765131098 219 IHRadPKQKEDSYEIIVCHANVIRYFVCRALQFPPEGWLRMGLNNGSITWITIRPSGRVALRTLGDTGFMPVDKVT 294
Cdd:PTZ00122 224 FHR--PVEDEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMVT 297
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 107-279 1.13e-35

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: 125.51  E-value: 1.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 107 NILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQILSKYLPGVDLVSCDM 182
Cdd:cd07067    1 RLYLVRHgeSEWNAEGrfQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 183 LREgapiqpvppvthwkpdavyhedgARIEAAFRRYIHRADPKqkedsYEIIVCHANVIRYFVCRALQFPPEGWLRMGLN 262
Cdd:cd07067   81 LRE-----------------------ARVLPALEELIAPHDGK-----NVLIVSHGGVLRALLAYLLGLSDEDILRLNLP 132

                        170
                 ....*....|....*..
gi 765131098 263 NGSITWITIRPSGRVAL 279
Cdd:cd07067  133 NGSISVLELDENGGGVL 149
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 108-285 6.38e-26

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: 101.13  E-value: 6.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  108 ILLIRH--SQYNLSGT--SDKDRILTPLGREQAEFTGQRLAALGLkyDVLIHSSMARATETAQILSKYLpGVDLVSCDML 183
Cdd:pfam00300   1 LYLVRHgeTEWNLEGRfqGRTDSPLTELGREQAEALAERLAGEPF--DAIYSSPLKRARQTAEIIAEAL-GLPVEIDPRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  184 RE-------GAPIQ------PVPPVTHWKPDAVYHEDG--------ARIEAAFRRYIHRADPKQkedsyEIIVCHANVIR 242
Cdd:pfam00300  78 REidfgdweGLTFEeiaeryPEEYDAWLADPADYRPPGgesladvrARVRAALEELAARHPGKT-----VLVVSHGGVIR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 765131098  243 YFVCRALQFPPEGWLRMGLNNGSITWITIRPSGRVaLRTLGDT 285
Cdd:pfam00300 153 ALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWV-LVLLNDT 194
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
105-283 4.99e-24

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 96.17  E-value: 4.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 105 TRNILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGLkyDVLIHSSMARATETAQILSKYLpGVDLVSC 180
Cdd:COG0406    1 MTRLYLVRHgeTEWNAEGrlQGRLDVPLTELGRAQARALAERLADIPF--DAVYSSPLQRARQTAEALAEAL-GLPVEVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 181 DMLRE-------GAPIQPV-----PPVTHWKPDAVYH--EDG-------ARIEAAFRRYIHRADPKQkedsyEIIVCHAN 239
Cdd:COG0406   78 PRLREidfgdweGLTFAELearypEALAAWLADPAEFrpPGGesladvqARVRAALEELLARHPGGT-----VLVVTHGG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 765131098 240 VIRYFVCRALQFPPEGWLRMGLNNGSITWITIRPsGRVALRTLG 283
Cdd:COG0406  153 VIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 108-244 8.69e-15

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: 70.57  E-value: 8.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098   108 ILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGL-KYDVLIHSSMARATETAQILSKYLPGVDLVSCDM 182
Cdd:smart00855   2 LYLIRHgeTEWNREGrlYGDTDVPLTELGRAQAEALGRLLASLLLpRFDVVYSSPLKRARQTAEALAIALGLPGLRERDF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098   183 -------LREGAPIQPVPPVTHWKPDAVYHEDG-----------ARIEAAFRRYIHRADpkqKEDSYEIIVCHANVIRYF 244
Cdd:smart00855  82 gawegltWDEIAAKYPEEYLAAWRDPYDPAPPAppggesladlvERVEPALDELIATAD---ASGQNVLIVSHGGVIRAL 158
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 107-210 2.51e-10

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 57.93  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  107 NILLIRHSQYNLSGTSDKDRILTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQILSKYLpgvDL-VSCDMLRE 185
Cdd:TIGR00249   2 QLFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCL---NLpSSAEVLEG 78

                          90       100
                  ....*....|....*....|....*
gi 765131098  186 GAPIQPVPPVTHWKpdAVYHEDGAR 210
Cdd:TIGR00249  79 LTPCGDIGLVSDYL--EALTNEGVA 101
 
Name Accession Description Interval E-value
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 68-294 4.84e-81

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 247.03  E-value: 4.84e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  68 WDFNWDKRDPSVLS-NGKRkessTEDPSSEQdnskpkatRNILLIRHSQYNLSGTSD-KDRILTPLGREQAEFTGQRLAA 145
Cdd:PTZ00122  76 WNEDWDGNYKHRPKaRGKR----ADKSASHQ--------RQIILVRHGQYINESSNDdNIKRLTELGKEQARITGKYLKE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 146 LG------LKYDVLIHSSMARATETAQILSKYLPGVDLVSCDMLREGAPIQPVPPVTHWKPDA-VYHEDGARIEAAFRRY 218
Cdd:PTZ00122 144 QFgeilvdKKVKAIYHSDMTRAKETAEIISEAFPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIeEILEDMKRIEAAFEKY 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765131098 219 IHRadPKQKEDSYEIIVCHANVIRYFVCRALQFPPEGWLRMGLNNGSITWITIRPSGRVALRTLGDTGFMPVDKVT 294
Cdd:PTZ00122 224 FHR--PVEDEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMVT 297
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 107-279 1.13e-35

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: 125.51  E-value: 1.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 107 NILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQILSKYLPGVDLVSCDM 182
Cdd:cd07067    1 RLYLVRHgeSEWNAEGrfQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 183 LREgapiqpvppvthwkpdavyhedgARIEAAFRRYIHRADPKqkedsYEIIVCHANVIRYFVCRALQFPPEGWLRMGLN 262
Cdd:cd07067   81 LRE-----------------------ARVLPALEELIAPHDGK-----NVLIVSHGGVLRALLAYLLGLSDEDILRLNLP 132

                        170
                 ....*....|....*..
gi 765131098 263 NGSITWITIRPSGRVAL 279
Cdd:cd07067  133 NGSISVLELDENGGGVL 149
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 108-282 8.18e-28

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: 105.19  E-value: 8.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 108 ILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQILSKYLPGvdlvscdml 183
Cdd:cd07040    2 LYLVRHgeREPNAEGrfTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFE--------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 184 regapiqpvppvthwkPDAVYHEDGARIEAAFRRYIHRADPKQKedsYEIIVCHANVIRYFVCRALQFPPEGWLRMGLNN 263
Cdd:cd07040   73 ----------------GLPVEVDPRARVLNALLELLARHLLDGK---NVLIVSHGGTIRALLAALLGLSDEEILSLNLPN 133

                        170
                 ....*....|....*....
gi 765131098 264 GSITWITIRPSGRVALRTL 282
Cdd:cd07040  134 GSILVLELDECGGKYVRLL 152
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 108-285 6.38e-26

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: 101.13  E-value: 6.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  108 ILLIRH--SQYNLSGT--SDKDRILTPLGREQAEFTGQRLAALGLkyDVLIHSSMARATETAQILSKYLpGVDLVSCDML 183
Cdd:pfam00300   1 LYLVRHgeTEWNLEGRfqGRTDSPLTELGREQAEALAERLAGEPF--DAIYSSPLKRARQTAEIIAEAL-GLPVEIDPRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  184 RE-------GAPIQ------PVPPVTHWKPDAVYHEDG--------ARIEAAFRRYIHRADPKQkedsyEIIVCHANVIR 242
Cdd:pfam00300  78 REidfgdweGLTFEeiaeryPEEYDAWLADPADYRPPGgesladvrARVRAALEELAARHPGKT-----VLVVSHGGVIR 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 765131098  243 YFVCRALQFPPEGWLRMGLNNGSITWITIRPSGRVaLRTLGDT 285
Cdd:pfam00300 153 ALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWV-LVLLNDT 194
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
105-283 4.99e-24

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 96.17  E-value: 4.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 105 TRNILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGLkyDVLIHSSMARATETAQILSKYLpGVDLVSC 180
Cdd:COG0406    1 MTRLYLVRHgeTEWNAEGrlQGRLDVPLTELGRAQARALAERLADIPF--DAVYSSPLQRARQTAEALAEAL-GLPVEVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 181 DMLRE-------GAPIQPV-----PPVTHWKPDAVYH--EDG-------ARIEAAFRRYIHRADPKQkedsyEIIVCHAN 239
Cdd:COG0406   78 PRLREidfgdweGLTFAELearypEALAAWLADPAEFrpPGGesladvqARVRAALEELLARHPGGT-----VLVVTHGG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 765131098 240 VIRYFVCRALQFPPEGWLRMGLNNGSITWITIRPsGRVALRTLG 283
Cdd:COG0406  153 VIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
108-188 8.62e-15

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 70.29  E-value: 8.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 108 ILLIRH--SQYNLSGTSDKDRILTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQILSKYLPGVDLVS-CDMLR 184
Cdd:COG2062    1 LILVRHakAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKVEvEDELY 80


                 ....
gi 765131098 185 EGAP 188
Cdd:COG2062   81 DADP 84
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 108-244 8.69e-15

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: 70.57  E-value: 8.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098   108 ILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGL-KYDVLIHSSMARATETAQILSKYLPGVDLVSCDM 182
Cdd:smart00855   2 LYLIRHgeTEWNREGrlYGDTDVPLTELGRAQAEALGRLLASLLLpRFDVVYSSPLKRARQTAEALAIALGLPGLRERDF 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098   183 -------LREGAPIQPVPPVTHWKPDAVYHEDG-----------ARIEAAFRRYIHRADpkqKEDSYEIIVCHANVIRYF 244
Cdd:smart00855  82 gawegltWDEIAAKYPEEYLAAWRDPYDPAPPAppggesladlvERVEPALDELIATAD---ASGQNVLIVSHGGVIRAL 158
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 72-289 2.38e-11

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 63.46  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  72 WDKRDPSVLSNGKRKESSTEDPSSEQDNSKPKATRnILLIRHSQYNL------SGTSDKDriLTPLGREQAEFTGQRLAA 145
Cdd:PRK07238 139 WGPSAAAADADPAKSAAPPAPTAPGWTGARGTPTR-LLLLRHGQTELsvqrrySGRGNPE--LTEVGRRQAAAAARYLAA 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 146 LGlKYDVLIHSSMARATETAQILSKYLpGVDLVSCDMLRE---GA-------------PIQ--------PVPPVTHWKPD 201
Cdd:PRK07238 216 RG-GIDAVVSSPLQRARDTAAAAAKAL-GLDVTVDDDLIEtdfGAwegltfaeaaerdPELhrawladtSVAPPGGESFD 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 202 AVYHedgaRIeAAFRRYIHRADPKQKedsyEIIVCHANVIRYFVCRALQFPPEGWLRMGLNNGSITWITIRPSGRVALRT 281
Cdd:PRK07238 294 AVAR----RV-RRARDRLIAEYPGAT----VLVVSHVTPIKTLLRLALDAGPGVLYRLHLDLASLSIAEFYPDGPASVRL 364


                 ....*...
gi 765131098 282 LGDTGFMP 289
Cdd:PRK07238 365 VNDTSHLR 372
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 107-210 2.51e-10

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 57.93  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098  107 NILLIRHSQYNLSGTSDKDRILTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQILSKYLpgvDL-VSCDMLRE 185
Cdd:TIGR00249   2 QLFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCL---NLpSSAEVLEG 78

                          90       100
                  ....*....|....*....|....*
gi 765131098  186 GAPIQPVPPVTHWKpdAVYHEDGAR 210
Cdd:TIGR00249  79 LTPCGDIGLVSDYL--EALTNEGVA 101
PRK06193 PRK06193
hypothetical protein; Provisional
 108-219 1.39e-07

hypothetical protein; Provisional


Pssm-ID: 235734  Cd Length: 206  Bit Score: 50.84  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 108 ILLIRHSQYNLS----GTSDKDRI-----LTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQILS---KYLPGV 175
Cdd:PRK06193  45 VIYFRHAATDRSqadqDTSDMDDCstqrnLSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWETAQLAFgrhEKEIRL 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 765131098 176 DLVSCDMLREGAP---IQPVPPVTHWKPDA------VYHEDGarIEAAFRRYI 219
Cdd:PRK06193 125 NFLNSEPVPAERNallKAGLRPLLTTPPDPgtntvlVGHDDN--LEAATGIYP 175
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 106-168 1.57e-07

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 50.84  E-value: 1.57e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 765131098 106 RNILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQIL 168
Cdd:PRK01295   3 RTLVLVRHgqSEWNLKNlfTGWRDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLI 69
PRK13462 PRK13462
acid phosphatase; Provisional
 108-167 1.01e-03

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 39.43  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 765131098 108 ILLIRH--SQYNLSG--TSDKDRILTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQI 167
Cdd:PRK13462   8 LLLLRHgeTEWSKSGrhTGRTELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKL 71
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
110-185 1.95e-03

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 38.56  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765131098 110 LIRH--SQYN----LSGTSDKDriLTPLGREQAEFTGQRLAALGLKYdvLIHSSMARATETAQILSKYLpGVDLVSCDML 183
Cdd:PRK03482   6 LVRHgeTQWNaerrIQGQSDSP--LTAKGEQQAMQVAERAKELGITH--IISSDLGRTRRTAEIIAQAC-GCDIIFDPRL 80


                 ..
gi 765131098 184 RE 185
Cdd:PRK03482  81 RE 82
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
108-167 3.96e-03

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 37.92  E-value: 3.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765131098 108 ILLIRH--SQYNL----SGTSDKDriLTPLGREQAEFTGQRLAALGLKYDVLIHSSMARATETAQI 167
Cdd:PRK14115   3 LVLIRHgeSQWNKenrfTGWTDVD--LSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTLWI 66
 
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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