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Conserved domains on  [gi|32564174|ref|NP_495593|]
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Serine/threonine-protein phosphatase Pgam5, mitochondrial [Caenorhabditis elegans]

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 ...
 56-281 1.09e-74

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: 230.46  E-value: 1.09e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174   56 WDKNWDfrdpislvdkGKWEkaDEEGKKKLIEEKKATATRNIFLIRHGQYHL----DHEVKMLTPLGREQAELLGKRLA- 130
Cdd:PTZ00122  76 WNEDWD----------GNYK--HRPKARGKRADKSASHQRQIILVRHGQYINessnDDNIKRLTELGKEQARITGKYLKe 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  131 -----NSDIKFTNMTMSTMVRATETANIILKHLPDdLTRTSSPFIEEGPPYPPVPDHKTWRPLDPEFYTEAARIESAYRK 205
Cdd:PTZ00122 144 qfgeiLVDKKVKAIYHSDMTRAKETAEIISEAFPG-VRLIEDPNLAEGVPCAPDPPSRGFKPTIEEILEDMKRIEAAFEK 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32564174  206 IFHRASPSqkEDSFELIVCHANVIRYFICRALQFPPEGWLRMSLGNCSLTWITIRPKGHVSVRSIGDIGHLPPNKI 281
Cdd:PTZ00122 223 YFHRPVED--EDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMV 296
 
Name Accession Description Interval E-value
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 56-281 1.09e-74

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 230.46  E-value: 1.09e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174   56 WDKNWDfrdpislvdkGKWEkaDEEGKKKLIEEKKATATRNIFLIRHGQYHL----DHEVKMLTPLGREQAELLGKRLA- 130
Cdd:PTZ00122  76 WNEDWD----------GNYK--HRPKARGKRADKSASHQRQIILVRHGQYINessnDDNIKRLTELGKEQARITGKYLKe 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  131 -----NSDIKFTNMTMSTMVRATETANIILKHLPDdLTRTSSPFIEEGPPYPPVPDHKTWRPLDPEFYTEAARIESAYRK 205
Cdd:PTZ00122 144 qfgeiLVDKKVKAIYHSDMTRAKETAEIISEAFPG-VRLIEDPNLAEGVPCAPDPPSRGFKPTIEEILEDMKRIEAAFEK 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32564174  206 IFHRASPSqkEDSFELIVCHANVIRYFICRALQFPPEGWLRMSLGNCSLTWITIRPKGHVSVRSIGDIGHLPPNKI 281
Cdd:PTZ00122 223 YFHRPVED--EDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMV 296
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 96-270 1.01e-31

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: 115.11  E-value: 1.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  96 NIFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLANSDIKFTNMTMSTMVRATETANIILKHLPDdltrtssp 168
Cdd:cd07067   1 RLYLVRHGESEWNAEGRFqgwtdvpLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPG-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174 169 fieegppyPPVpdHKTWRpLDPEfyteaaRIESAYRKIFHRAspsqkEDSFELIVCHANVIRYFICRALQFPPEGWLRMS 248
Cdd:cd07067  73 --------LPV--EVDPR-LREA------RVLPALEELIAPH-----DGKNVLIVSHGGVLRALLAYLLGLSDEDILRLN 130

                       170       180
                ....*....|....*....|..
gi 32564174 249 LGNCSLTWITIRPKGHVSVRSI 270
Cdd:cd07067 131 LPNGSISVLELDENGGGVLLLR 152
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 97-268 2.66e-27

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: 104.60  E-value: 2.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174    97 IFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLANSDIK--FTnmtmSTMVRATETANIILKHLPDDLT---- 163
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFqgrtdspLTELGREQAEALAERLAGEPFDaiYS----SPLKRARQTAEIIAEALGLPVEidpr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174   164 -----------RTSSPFIEEGPPYPPVPDH--KTWRPLDPEFYTE-AARIESAYRKIFHRAspsqkEDSFELIVCHANVI 229
Cdd:pfam00300  77 lreidfgdwegLTFEEIAERYPEEYDAWLAdpADYRPPGGESLADvRARVRAALEELAARH-----PGKTVLVVSHGGVI 151

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 32564174   230 RYFICRALQFPPEGWLRMSLGNCSLTWITIRPKGHVSVR 268
Cdd:pfam00300 152 RALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWVLVL 190
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
94-271 1.85e-24

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 97.32  E-value: 1.85e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  94 TRNIFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLAnsDIKFTNMTMSTMVRATETANIILKHLPDDLtRTS 166
Cdd:COG0406   1 MTRLYLVRHGETEWNAEGRLqgrldvpLTELGRAQARALAERLA--DIPFDAVYSSPLQRARQTAEALAEALGLPV-EVD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174 167 SPFIE------EGPPYPPVPDH-----KTWRPLDPEF-------YTE-AARIESAYRKIFHRAspsqkEDSFELIVCHAN 227
Cdd:COG0406  78 PRLREidfgdwEGLTFAELEARypealAAWLADPAEFrppggesLADvQARVRAALEELLARH-----PGGTVLVVTHGG 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 32564174 228 VIRYFICRALQFPPEGWLRMSLGNCSLTWITIRPkGHVSVRSIG 271
Cdd:COG0406 153 VIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 97-257 2.98e-15

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


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 71.88  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174    97 IFLIRHGQ--------Y-HLDheVKmLTPLGREQAELLGKRLAnsDIKFTNMTMSTMVRATETANIILKHLPDDLTRtSS 167
Cdd:TIGR03162   1 LYLIRHGEtdvnaglcYgQTD--VP-LAESGEEQAAALREKLA--DVPFDAVYSSPLSRCRELAEILAERRGLPIIK-DD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174   168 PFIE------EGPPYPPVPDH-----------KTWRPLDPEFYTE-AARIESAYRKIfhrASPSQKEDSfeLIVCHANVI 229
Cdd:TIGR03162  75 RLREmdfgdwEGRSWDEIPEAypeldawaadwQHARPPGGESFADfYQRVSEFLEEL---LKAHEGDNV--LIVTHGGVI 149

                         170       180
                  ....*....|....*....|....*...
gi 32564174   230 RYFICRALQFPPEGWLRMSLGNCSLTWI 257
Cdd:TIGR03162 150 RALLAHLLGLPLEQWWSFAVEYGSITLI 177
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 97-232 2.69e-13

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


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 65.95  E-value: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174     97 IFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLAN-SDIKFTNMTMSTMVRATETANIILKHLPD-------- 160
Cdd:smart00855   2 LYLIRHGETEWNREGRLygdtdvpLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALAIALGLpglrerdf 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174    161 -DLTRTSSPFIEEGPPYPPVPDHKTWRPLDP------EFYTE-AARIESAYRKIFHRASPSQKEdsfELIVCHANVIRYF 232
Cdd:smart00855  82 gAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPpappggESLADlVERVEPALDELIATADASGQN---VLIVSHGGVIRAL 158
 
Name Accession Description Interval E-value
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 56-281 1.09e-74

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 230.46  E-value: 1.09e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174   56 WDKNWDfrdpislvdkGKWEkaDEEGKKKLIEEKKATATRNIFLIRHGQYHL----DHEVKMLTPLGREQAELLGKRLA- 130
Cdd:PTZ00122  76 WNEDWD----------GNYK--HRPKARGKRADKSASHQRQIILVRHGQYINessnDDNIKRLTELGKEQARITGKYLKe 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  131 -----NSDIKFTNMTMSTMVRATETANIILKHLPDdLTRTSSPFIEEGPPYPPVPDHKTWRPLDPEFYTEAARIESAYRK 205
Cdd:PTZ00122 144 qfgeiLVDKKVKAIYHSDMTRAKETAEIISEAFPG-VRLIEDPNLAEGVPCAPDPPSRGFKPTIEEILEDMKRIEAAFEK 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32564174  206 IFHRASPSqkEDSFELIVCHANVIRYFICRALQFPPEGWLRMSLGNCSLTWITIRPKGHVSVRSIGDIGHLPPNKI 281
Cdd:PTZ00122 223 YFHRPVED--EDSVEIIVCHGNVIRYLVCRALQLPPEAWLRLSLYNCGITWIVISSEGHVSLSGFGSVGHLPPDMV 296
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 96-270 1.01e-31

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: 115.11  E-value: 1.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  96 NIFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLANSDIKFTNMTMSTMVRATETANIILKHLPDdltrtssp 168
Cdd:cd07067   1 RLYLVRHGESEWNAEGRFqgwtdvpLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPG-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174 169 fieegppyPPVpdHKTWRpLDPEfyteaaRIESAYRKIFHRAspsqkEDSFELIVCHANVIRYFICRALQFPPEGWLRMS 248
Cdd:cd07067  73 --------LPV--EVDPR-LREA------RVLPALEELIAPH-----DGKNVLIVSHGGVLRALLAYLLGLSDEDILRLN 130

                       170       180
                ....*....|....*....|..
gi 32564174 249 LGNCSLTWITIRPKGHVSVRSI 270
Cdd:cd07067 131 LPNGSISVLELDENGGGVLLLR 152
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 97-268 2.66e-27

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: 104.60  E-value: 2.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174    97 IFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLANSDIK--FTnmtmSTMVRATETANIILKHLPDDLT---- 163
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFqgrtdspLTELGREQAEALAERLAGEPFDaiYS----SPLKRARQTAEIIAEALGLPVEidpr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174   164 -----------RTSSPFIEEGPPYPPVPDH--KTWRPLDPEFYTE-AARIESAYRKIFHRAspsqkEDSFELIVCHANVI 229
Cdd:pfam00300  77 lreidfgdwegLTFEEIAERYPEEYDAWLAdpADYRPPGGESLADvRARVRAALEELAARH-----PGKTVLVVSHGGVI 151

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 32564174   230 RYFICRALQFPPEGWLRMSLGNCSLTWITIRPKGHVSVR 268
Cdd:pfam00300 152 RALLAHLLGLPLEALRRFPLDNASLSILEFDGGGWVLVL 190
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 97-268 6.31e-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: 102.49  E-value: 6.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  97 IFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLANSDIKFTNMTMSTMVRATETANIILKHLpddltrtsspf 169
Cdd:cd07040   2 LYLVRHGEREPNAEGRFtgwgdgpLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGL----------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174 170 ieegppYPPVPDHKTWRpldpefyteaARIESAYRKIFHRASPSQKedsFELIVCHANVIRYFICRALQFPPEGWLRMSL 249
Cdd:cd07040  71 ------FEGLPVEVDPR----------ARVLNALLELLARHLLDGK---NVLIVSHGGTIRALLAALLGLSDEEILSLNL 131

                       170
                ....*....|....*....
gi 32564174 250 GNCSLTWITIRPKGHVSVR 268
Cdd:cd07040 132 PNGSILVLELDECGGKYVR 150
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
94-271 1.85e-24

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 97.32  E-value: 1.85e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  94 TRNIFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLAnsDIKFTNMTMSTMVRATETANIILKHLPDDLtRTS 166
Cdd:COG0406   1 MTRLYLVRHGETEWNAEGRLqgrldvpLTELGRAQARALAERLA--DIPFDAVYSSPLQRARQTAEALAEALGLPV-EVD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174 167 SPFIE------EGPPYPPVPDH-----KTWRPLDPEF-------YTE-AARIESAYRKIFHRAspsqkEDSFELIVCHAN 227
Cdd:COG0406  78 PRLREidfgdwEGLTFAELEARypealAAWLADPAEFrppggesLADvQARVRAALEELLARH-----PGGTVLVVTHGG 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 32564174 228 VIRYFICRALQFPPEGWLRMSLGNCSLTWITIRPkGHVSVRSIG 271
Cdd:COG0406 153 VIRALLAHLLGLPLEAFWRLRIDNASVTVLEFDD-GRWRLVALN 195
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 97-257 2.98e-15

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


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 71.88  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174    97 IFLIRHGQ--------Y-HLDheVKmLTPLGREQAELLGKRLAnsDIKFTNMTMSTMVRATETANIILKHLPDDLTRtSS 167
Cdd:TIGR03162   1 LYLIRHGEtdvnaglcYgQTD--VP-LAESGEEQAAALREKLA--DVPFDAVYSSPLSRCRELAEILAERRGLPIIK-DD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174   168 PFIE------EGPPYPPVPDH-----------KTWRPLDPEFYTE-AARIESAYRKIfhrASPSQKEDSfeLIVCHANVI 229
Cdd:TIGR03162  75 RLREmdfgdwEGRSWDEIPEAypeldawaadwQHARPPGGESFADfYQRVSEFLEEL---LKAHEGDNV--LIVTHGGVI 149

                         170       180
                  ....*....|....*....|....*...
gi 32564174   230 RYFICRALQFPPEGWLRMSLGNCSLTWI 257
Cdd:TIGR03162 150 RALLAHLLGLPLEQWWSFAVEYGSITLI 177
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 97-232 2.69e-13

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


Pssm-ID: 214859 [Multi-domain]  Cd Length: 158  Bit Score: 65.95  E-value: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174     97 IFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLAN-SDIKFTNMTMSTMVRATETANIILKHLPD-------- 160
Cdd:smart00855   2 LYLIRHGETEWNREGRLygdtdvpLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALAIALGLpglrerdf 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174    161 -DLTRTSSPFIEEGPPYPPVPDHKTWRPLDP------EFYTE-AARIESAYRKIFHRASPSQKEdsfELIVCHANVIRYF 232
Cdd:smart00855  82 gAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPpappggESLADlVERVEPALDELIATADASGQN---VLIVSHGGVIRAL 158
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 90-277 5.83e-09

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 56.14  E-value: 5.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174   90 KATATRnIFLIRHGQYHLDHEVKM-------LTPLGREQAELLGKRLANSDiKFTNMTMSTMVRATETANIILKHLPDDL 162
Cdd:PRK07238 168 RGTPTR-LLLLRHGQTELSVQRRYsgrgnpeLTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALGLDV 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  163 TrTSSPFIE------EGPPYPPV----PD-HKTW------RPLDPE-FYTEAARIESAYRKIF--HRASPSqkedsfeLI 222
Cdd:PRK07238 246 T-VDDDLIEtdfgawEGLTFAEAaerdPElHRAWladtsvAPPGGEsFDAVARRVRRARDRLIaeYPGATV-------LV 317

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 32564174  223 VCHANVIRYFICRALQFPPEGWLRMSLGNCSLTWITIRPKGHVSVRSIGDIGHLP 277
Cdd:PRK07238 318 VSHVTPIKTLLRLALDAGPGVLYRLHLDLASLSIAEFYPDGPASVRLVNDTSHLR 372
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
97-175 8.26e-09

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 53.34  E-value: 8.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  97 IFLIRHGQ------YHLDHEVKmLTPLGREQAELLGKRLANSDIKFTNMTMSTMVRATETANIILKHLPDDLTRTSSPFI 170
Cdd:COG2062   1 LILVRHAKaewrapGGDDFDRP-LTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKVEVEDEL 79


                ....*
gi 32564174 171 EEGPP 175
Cdd:COG2062  80 YDADP 84
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 96-158 6.23e-06

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 45.21  E-value: 6.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32564174    96 NIFLIRHGQYHLDHEV---KMLTPLGREQAELLGKRLANSDIKFTNMTMSTMVRATETANIILKHL 158
Cdd:TIGR00249   2 QLFIMRHGDAALDAASdsvRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCL 67
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 99-186 4.77e-05

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-dependent) is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440353  Cd Length: 229  Bit Score: 43.53  E-value: 4.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564174  99 LIRHGQ--YHLD------HEVKmLTPLGREQAELLGKRLANS----DIKFTnmtmSTMVRATETANIILKHLpdDLtrts 166
Cdd:COG0588   5 LLRHGEseWNLEnrftgwTDVD-LSEKGRAEAKRAGRLLKEAgflfDVAYT----SVLKRAIRTLWIVLDEM--DR---- 73

                        90       100
                ....*....|....*....|
gi 32564174 167 spfieegpPYPPVpdHKTWR 186
Cdd:COG0588  74 --------LWIPV--EKSWR 83
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
97-155 5.33e-04

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 40.03  E-value: 5.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32564174   97 IFLIRHGQYHLD-------HEVKMLTPLGREQAELLGKRLANsdIKFTNMTMSTMVRATETANIIL 155
Cdd:PRK15004   3 LWLVRHGETQANvdglysgHAPTPLTARGIEQAQNLHTLLRD--VPFDLVLCSELERAQHTARLVL 66
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 95-158 3.32e-03

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 37.75  E-value: 3.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32564174   95 RNIFLIRHGQYhlDHEVKML---------TPLGREQAELLGKRLANSDIKFTNMTMSTMVRATETANIILKHL 158
Cdd:PRK01295   3 RTLVLVRHGQS--EWNLKNLftgwrdpdlTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEEL 73
 
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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