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Conserved domains on  [gi|1622847800|ref|XP_014965221|]
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serine/threonine-protein phosphatase PGAM5, mitochondrial isoform X1 [Macaca mulatta]

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 ...
 58-287 2.76e-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: 247.41  E-value: 2.76e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  58 WDPNWDrreplslINLRKRNVESGeeelasKLDHYKAKATRHIFLIRHSQYHVDGSL-EKDRTLTPLGREQAELTGLRLA 136
Cdd:PTZ00122   76 WNEDWD-------GNYKHRPKARG------KRADKSASHQRQIILVRHGQYINESSNdDNIKRLTELGKEQARITGKYLK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 137 SLG------LKFNKIVHSSMTRAIETTDIISRHLPGVCKVSTDLLREGAPIEPDPPVSHWKPEAVQYYEDGARIEAAFRN 210
Cdd:PTZ00122  143 EQFgeilvdKKVKAIYHSDMTRAKETAEIISEAFPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIEEILEDMKRIEAAFEK 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622847800 211 YIHRADArqEEDSYEIFICHANVIRYIVCRALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMPPDKIT 287
Cdd:PTZ00122  223 YFHRPVE--DEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMVT 297
 
Name Accession Description Interval E-value
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 58-287 2.76e-81

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 247.41  E-value: 2.76e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  58 WDPNWDrreplslINLRKRNVESGeeelasKLDHYKAKATRHIFLIRHSQYHVDGSL-EKDRTLTPLGREQAELTGLRLA 136
Cdd:PTZ00122   76 WNEDWD-------GNYKHRPKARG------KRADKSASHQRQIILVRHGQYINESSNdDNIKRLTELGKEQARITGKYLK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 137 SLG------LKFNKIVHSSMTRAIETTDIISRHLPGVCKVSTDLLREGAPIEPDPPVSHWKPEAVQYYEDGARIEAAFRN 210
Cdd:PTZ00122  143 EQFgeilvdKKVKAIYHSDMTRAKETAEIISEAFPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIEEILEDMKRIEAAFEK 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622847800 211 YIHRADArqEEDSYEIFICHANVIRYIVCRALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMPPDKIT 287
Cdd:PTZ00122  223 YFHRPVE--DEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMVT 297
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 99-272 4.07e-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: 118.58  E-value: 4.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  99 HIFLIRH--SQYHVDGSL--EKDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDIISRHLPGVCKVSTDL 174
Cdd:cd07067     1 RLYLVRHgeSEWNAEGRFqgWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 175 LREgapiepdppvshwkpeavqyyedgARIEAAFRNYIHRADarqeeDSYEIFICHANVIRYIVCRALQFPPEGWLRLSL 254
Cdd:cd07067    81 LRE------------------------ARVLPALEELIAPHD-----GKNVLIVSHGGVLRALLAYLLGLSDEDILRLNL 131

                         170
                  ....*....|....*...
gi 1622847800 255 NNGSITHLVIRPNGRVAL 272
Cdd:cd07067   132 PNGSISVLELDENGGGVL 149
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 100-278 2.97e-21

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 88.81  E-value: 2.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 100 IFLIRH--SQYHVDGSLE--KDRTLTPLGREQAELTGLRLAslGLKFNKIVHSSMTRAIETTDIISRHLpGVCKVSTDLL 175
Cdd:pfam00300   1 LYLVRHgeTEWNLEGRFQgrTDSPLTELGREQAEALAERLA--GEPFDAIYSSPLKRARQTAEIIAEAL-GLPVEIDPRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 176 RE-------GAPIE------PDPPVSHWKPEAVQYYEDG-------ARIEAAFRnyihraDARQEEDSYEIFIC-HANVI 234
Cdd:pfam00300  78 REidfgdweGLTFEeiaeryPEEYDAWLADPADYRPPGGesladvrARVRAALE------ELAARHPGKTVLVVsHGGVI 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622847800 235 RYIVCRALQFPPEGWLRLSLNNGSITHLVIRPNGRVaLRTLGDT 278
Cdd:pfam00300 152 RALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWV-LVLLNDT 194
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
97-276 1.54e-18

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 81.53  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  97 TRHIFLIRHSQyhVDGSLEK------DRTLTPLGREQAELTGLRLAslGLKFNKIVHSSMTRAIETTDIISRHLPgvCKV 170
Cdd:COG0406     1 MTRLYLVRHGE--TEWNAEGrlqgrlDVPLTELGRAQARALAERLA--DIPFDAVYSSPLQRARQTAEALAEALG--LPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 171 STD-LLRE-------GAPI----EPDPPV-SHWKPEAVQY-------YED-GARIEAAFRNYIHRADARQEedsyeIFIC 229
Cdd:COG0406    75 EVDpRLREidfgdweGLTFaeleARYPEAlAAWLADPAEFrppggesLADvQARVRAALEELLARHPGGTV-----LVVT 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622847800 230 HANVIRYIVCRALQFPPEGWLRLSLNNGSITHLVIRpNGRVALRTLG 276
Cdd:COG0406   150 HGGVIRALLAHLLGLPLEAFWRLRIDNASVTVLEFD-DGRWRLVALN 195
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 99-237 1.15e-09

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: 55.93  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800   99 HIFLIRH--SQYHVDGSL--EKDRTLTPLGREQAELTGLRLASLGL-KFNKIVHSSMTRAIETTDIIS----------RH 163
Cdd:smart00855   1 RLYLIRHgeTEWNREGRLygDTDVPLTELGRAQAEALGRLLASLLLpRFDVVYSSPLKRARQTAEALAialglpglreRD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622847800  164 LPGVCKVSTDLLREGAPIEP---DPPVSHWKPEAVQYYEDGARIEAAFRNYIHRADARQEEDSYEIFIC-HANVIRYI 237
Cdd:smart00855  81 FGAWEGLTWDEIAAKYPEEYlaaWRDPYDPAPPAPPGGESLADLVERVEPALDELIATADASGQNVLIVsHGGVIRAL 158
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 100-203 6.13e-08

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 50.99  E-value: 6.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 100 IFLIRHSQYHVDGSLEKDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDIISRHLpgVCKVSTDLLREGA 179
Cdd:TIGR00249   3 LFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCL--NLPSSAEVLEGLT 80

                          90       100
                  ....*....|....*....|....
gi 1622847800 180 PIEPDPPVSHWKPEavqYYEDGAR 203
Cdd:TIGR00249  81 PCGDIGLVSDYLEA---LTNEGVA 101
 
Name Accession Description Interval E-value
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 58-287 2.76e-81

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 247.41  E-value: 2.76e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  58 WDPNWDrreplslINLRKRNVESGeeelasKLDHYKAKATRHIFLIRHSQYHVDGSL-EKDRTLTPLGREQAELTGLRLA 136
Cdd:PTZ00122   76 WNEDWD-------GNYKHRPKARG------KRADKSASHQRQIILVRHGQYINESSNdDNIKRLTELGKEQARITGKYLK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 137 SLG------LKFNKIVHSSMTRAIETTDIISRHLPGVCKVSTDLLREGAPIEPDPPVSHWKPEAVQYYEDGARIEAAFRN 210
Cdd:PTZ00122  143 EQFgeilvdKKVKAIYHSDMTRAKETAEIISEAFPGVRLIEDPNLAEGVPCAPDPPSRGFKPTIEEILEDMKRIEAAFEK 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622847800 211 YIHRADArqEEDSYEIFICHANVIRYIVCRALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMPPDKIT 287
Cdd:PTZ00122  223 YFHRPVE--DEDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMVT 297
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 99-272 4.07e-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: 118.58  E-value: 4.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  99 HIFLIRH--SQYHVDGSL--EKDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDIISRHLPGVCKVSTDL 174
Cdd:cd07067     1 RLYLVRHgeSEWNAEGRFqgWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 175 LREgapiepdppvshwkpeavqyyedgARIEAAFRNYIHRADarqeeDSYEIFICHANVIRYIVCRALQFPPEGWLRLSL 254
Cdd:cd07067    81 LRE------------------------ARVLPALEELIAPHD-----GKNVLIVSHGGVLRALLAYLLGLSDEDILRLNL 131

                         170
                  ....*....|....*...
gi 1622847800 255 NNGSITHLVIRPNGRVAL 272
Cdd:cd07067   132 PNGSISVLELDENGGGVL 149
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 99-275 2.66e-24

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: 95.56  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  99 HIFLIRH--SQYHVDGSL--EKDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDIISRHLPgvckvstdl 174
Cdd:cd07040     1 VLYLVRHgeREPNAEGRFtgWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLF--------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 175 lregapiePDPPVshwkpeavqYYEDGARIEAAFRNYIHRADarqEEDSYEIFICHANVIRYIVCRALQFPPEGWLRLSL 254
Cdd:cd07040    72 --------EGLPV---------EVDPRARVLNALLELLARHL---LDGKNVLIVSHGGTIRALLAALLGLSDEEILSLNL 131

                         170       180
                  ....*....|....*....|.
gi 1622847800 255 NNGSITHLVIRPNGRVALRTL 275
Cdd:cd07040   132 PNGSILVLELDECGGKYVRLL 152
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 100-278 2.97e-21

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.


Pssm-ID: 459751 [Multi-domain]  Cd Length: 194  Bit Score: 88.81  E-value: 2.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 100 IFLIRH--SQYHVDGSLE--KDRTLTPLGREQAELTGLRLAslGLKFNKIVHSSMTRAIETTDIISRHLpGVCKVSTDLL 175
Cdd:pfam00300   1 LYLVRHgeTEWNLEGRFQgrTDSPLTELGREQAEALAERLA--GEPFDAIYSSPLKRARQTAEIIAEAL-GLPVEIDPRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 176 RE-------GAPIE------PDPPVSHWKPEAVQYYEDG-------ARIEAAFRnyihraDARQEEDSYEIFIC-HANVI 234
Cdd:pfam00300  78 REidfgdweGLTFEeiaeryPEEYDAWLADPADYRPPGGesladvrARVRAALE------ELAARHPGKTVLVVsHGGVI 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622847800 235 RYIVCRALQFPPEGWLRLSLNNGSITHLVIRPNGRVaLRTLGDT 278
Cdd:pfam00300 152 RALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWV-LVLLNDT 194
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
97-276 1.54e-18

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 81.53  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  97 TRHIFLIRHSQyhVDGSLEK------DRTLTPLGREQAELTGLRLAslGLKFNKIVHSSMTRAIETTDIISRHLPgvCKV 170
Cdd:COG0406     1 MTRLYLVRHGE--TEWNAEGrlqgrlDVPLTELGRAQARALAERLA--DIPFDAVYSSPLQRARQTAEALAEALG--LPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 171 STD-LLRE-------GAPI----EPDPPV-SHWKPEAVQY-------YED-GARIEAAFRNYIHRADARQEedsyeIFIC 229
Cdd:COG0406    75 EVDpRLREidfgdweGLTFaeleARYPEAlAAWLADPAEFrppggesLADvQARVRAALEELLARHPGGTV-----LVVT 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622847800 230 HANVIRYIVCRALQFPPEGWLRLSLNNGSITHLVIRpNGRVALRTLG 276
Cdd:COG0406   150 HGGVIRALLAHLLGLPLEAFWRLRIDNASVTVLEFD-DGRWRLVALN 195
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
100-173 8.64e-13

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 64.51  E-value: 8.64e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622847800 100 IFLIRH--SQYHVDGSLEKDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDIISRHLPGVCKVSTD 173
Cdd:COG2062     1 LILVRHakAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKVEVE 76
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 99-237 1.15e-09

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: 55.93  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800   99 HIFLIRH--SQYHVDGSL--EKDRTLTPLGREQAELTGLRLASLGL-KFNKIVHSSMTRAIETTDIIS----------RH 163
Cdd:smart00855   1 RLYLIRHgeTEWNREGRLygDTDVPLTELGRAQAEALGRLLASLLLpRFDVVYSSPLKRARQTAEALAialglpglreRD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622847800  164 LPGVCKVSTDLLREGAPIEP---DPPVSHWKPEAVQYYEDGARIEAAFRNYIHRADARQEEDSYEIFIC-HANVIRYI 237
Cdd:smart00855  81 FGAWEGLTWDEIAAKYPEEYlaaWRDPYDPAPPAPPGGESLADLVERVEPALDELIATADASGQNVLIVsHGGVIRAL 158
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 100-203 6.13e-08

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 50.99  E-value: 6.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 100 IFLIRHSQYHVDGSLEKDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDIISRHLpgVCKVSTDLLREGA 179
Cdd:TIGR00249   3 LFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCL--NLPSSAEVLEGLT 80

                          90       100
                  ....*....|....*....|....
gi 1622847800 180 PIEPDPPVSHWKPEavqYYEDGAR 203
Cdd:TIGR00249  81 PCGDIGLVSDYLEA---LTNEGVA 101
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 93-282 2.69e-04

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 41.89  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800  93 KAKATRhIFLIRHSQYHVdgSLEK------DRTLTPLGREQAELTGLRLASLGlKFNKIVHSSMTRAIETTDIISRHLpG 166
Cdd:PRK07238  168 RGTPTR-LLLLRHGQTEL--SVQRrysgrgNPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKAL-G 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622847800 167 VCKVSTDLLRE-----------GAPIEPDPPVSH-W------KPEAVQYYEDGARIEAAFRNYIHRADARQEedsyEIFI 228
Cdd:PRK07238  243 LDVTVDDDLIEtdfgawegltfAEAAERDPELHRaWladtsvAPPGGESFDAVARRVRRARDRLIAEYPGAT----VLVV 318

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622847800 229 CHANVIRYIVCRALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMP 282
Cdd:PRK07238  319 SHVTPIKTLLRLALDAGPGVLYRLHLDLASLSIAEFYPDGPASVRLVNDTSHLR 372
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 98-160 2.76e-03

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 38.13  E-value: 2.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622847800  98 RHIFLIRHSQyhVDGSLE------KDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAIETTDII 160
Cdd:PRK01295    3 RTLVLVRHGQ--SEWNLKnlftgwRDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLI 69
 
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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