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Conserved domains on  [gi|1953602848|gb|KAG0682995|]
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hypothetical protein C6P41_003399 [Kluyveromyces marxianus]

Protein Classification

HP_PGM_like and TFIIIC_sub6 domain-containing protein( domain architecture ID 10785449)

HP_PGM_like and TFIIIC_sub6 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TFIIIC_sub6 pfam10419
TFIIIC subunit triple barrel domain; This is a family of proteins subunits of TFIIIC. TFIIIC ...
 313-409 1.84e-26

TFIIIC subunit triple barrel domain; This is a family of proteins subunits of TFIIIC. TFIIIC in yeast and humans is required for transcription of tRNA and 5 S RNA genes by RNA polymerase III. Yeast members of this family are fused to phosphoglycerate mutase domain.


:

Pssm-ID: 463085  Cd Length: 91  Bit Score: 101.49  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848 313 EEYEHVYVSLDVENRNYREKQTVQNQATLQHSGLESDKPLVKIGDNVYEGTWKKPLGTELAFasegskTDSNDSDSKTTD 392
Cdd:pfam10419   1 EETETVYVTLDLSGPLYSERLPDEEDATIQILGLDTENPLLQIGGQVYEGEWEETIGTELLF------EEDDDANKKSLE 74

                          90
                  ....*....|....*..
gi 1953602848 393 RVYRVTDSIDLHPIQPM 409
Cdd:pfam10419  75 LLGKSSKRLVLTRVFLK 91
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-172 1.79e-23

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: 96.89  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   6 IYIARHGyRSNWlptppaHPAPPTGVNSDVPLAPHGIEQARELAHYLISIDnqPQLIVSSPLYRCLQTSEPIADLLELPI 85
Cdd:pfam00300   1 LYLVRHG-ETEW------NLEGRFQGRTDSPLTELGREQAEALAERLAGEP--FDAIYSSPLKRARQTAEIIAEALGLPV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  86 YFDRGLGEWY------KPDRDIIPEPAsyDILNNFFpgklksEWPHSAIPSNkGETEEEIFERCKKfwpvFIKTVEERFP 159
Cdd:pfam00300  72 EIDPRLREIDfgdwegLTFEEIAERYP--EEYDAWL------ADPADYRPPG-GESLADVRARVRA----ALEELAARHP 138

                         170
                  ....*....|...
gi 1953602848 160 EvETILLVTHAAT 172
Cdd:pfam00300 139 G-KTVLVVSHGGV 150
 
Name Accession Description Interval E-value
TFIIIC_sub6 pfam10419
TFIIIC subunit triple barrel domain; This is a family of proteins subunits of TFIIIC. TFIIIC ...
 313-409 1.84e-26

TFIIIC subunit triple barrel domain; This is a family of proteins subunits of TFIIIC. TFIIIC in yeast and humans is required for transcription of tRNA and 5 S RNA genes by RNA polymerase III. Yeast members of this family are fused to phosphoglycerate mutase domain.


Pssm-ID: 463085  Cd Length: 91  Bit Score: 101.49  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848 313 EEYEHVYVSLDVENRNYREKQTVQNQATLQHSGLESDKPLVKIGDNVYEGTWKKPLGTELAFasegskTDSNDSDSKTTD 392
Cdd:pfam10419   1 EETETVYVTLDLSGPLYSERLPDEEDATIQILGLDTENPLLQIGGQVYEGEWEETIGTELLF------EEDDDANKKSLE 74

                          90
                  ....*....|....*..
gi 1953602848 393 RVYRVTDSIDLHPIQPM 409
Cdd:pfam10419  75 LLGKSSKRLVLTRVFLK 91
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-172 1.79e-23

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: 96.89  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   6 IYIARHGyRSNWlptppaHPAPPTGVNSDVPLAPHGIEQARELAHYLISIDnqPQLIVSSPLYRCLQTSEPIADLLELPI 85
Cdd:pfam00300   1 LYLVRHG-ETEW------NLEGRFQGRTDSPLTELGREQAEALAERLAGEP--FDAIYSSPLKRARQTAEIIAEALGLPV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  86 YFDRGLGEWY------KPDRDIIPEPAsyDILNNFFpgklksEWPHSAIPSNkGETEEEIFERCKKfwpvFIKTVEERFP 159
Cdd:pfam00300  72 EIDPRLREIDfgdwegLTFEEIAERYP--EEYDAWL------ADPADYRPPG-GESLADVRARVRA----ALEELAARHP 138

                         170
                  ....*....|...
gi 1953602848 160 EvETILLVTHAAT 172
Cdd:pfam00300 139 G-KTVLVVSHGGV 150
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
5-172 3.95e-22

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 93.08  E-value: 3.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   5 TIYIARHGyRSNWlptppAHPAPPTGvNSDVPLAPHGIEQARELAHYLISIDnqPQLIVSSPLYRCLQTSEPIADLLELP 84
Cdd:COG0406     3 RLYLVRHG-ETEW-----NAEGRLQG-RLDVPLTELGRAQARALAERLADIP--FDAVYSSPLQRARQTAEALAEALGLP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  85 IYFDRGLGEWY------KPDRDIIPE-PASYDilnnffpgKLKSEWPHSAIPSnkGETEEEIFERCKKFWpvfiKTVEER 157
Cdd:COG0406    74 VEVDPRLREIDfgdwegLTFAELEARyPEALA--------AWLADPAEFRPPG--GESLADVQARVRAAL----EELLAR 139

                         170
                  ....*....|....*
gi 1953602848 158 FPEvETILLVTHAAT 172
Cdd:COG0406   140 HPG-GTVLVVTHGGV 153
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-207 1.02e-20

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: 87.76  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   5 TIYIARHGYRSNWLPTPPAHPapptgvnSDVPLAPHGIEQARELAHYLISIDNQPQLIVSSPLYRCLQTSEPIAD-LLEL 83
Cdd:cd07067     1 RLYLVRHGESEWNAEGRFQGW-------TDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEeLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  84 PIYFDRGLGEwykpdrdiipepasydilnnffpgklksewphsaipsnkgeteeeifERCKKFWpvfiKTVEERFPEvET 163
Cdd:cd07067    74 PVEVDPRLRE-----------------------------------------------ARVLPAL----EELIAPHDG-KN 101

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953602848 164 ILLVTHAATKIALGMTLLKFNsvrdtlDEDGNVIHCGSCSLDKY 207
Cdd:cd07067   102 VLIVSHGGVLRALLAYLLGLS------DEDILRLNLPNGSISVL 139
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 5-172 1.54e-19

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: 84.82  E-value: 1.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848    5 TIYIARHGyRSNWlptppaHPAPPTGVNSDVPLAPHGIEQARELAHYLIS-IDNQPQLIVSSPLYRCLQTSEPIADLLEL 83
Cdd:smart00855   1 RLYLIRHG-ETEW------NREGRLYGDTDVPLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALAIALGL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   84 PIYFDRGLGEWYKPDRDIIPEPASYDILNNFFPGKlksewPHSAIPSNKGETEEEIFERCKKFWpvfIKTVEERFPEVET 163
Cdd:smart00855  74 PGLRERDFGAWEGLTWDEIAAKYPEEYLAAWRDPY-----DPAPPAPPGGESLADLVERVEPAL---DELIATADASGQN 145


                   ....*....
gi 1953602848  164 ILLVTHAAT 172
Cdd:smart00855 146 VLIVSHGGV 154
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 33-169 2.01e-07

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 52.67  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  33 SDVPLAPHGIEQARELAHYLISiDNQPQLIVSSPLYRCLQTSEPIADLLELPIYFDRGL-----GEWykpdrdiipEPAS 107
Cdd:PRK07238  194 GNPELTEVGRRQAAAAARYLAA-RGGIDAVVSSPLQRARDTAAAAAKALGLDVTVDDDLietdfGAW---------EGLT 263

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953602848 108 YDILNNFFPGkLKSEW---PHSAIPSnkGETEEEIFERCKKfwpvFIKTVEERFPEvETILLVTH 169
Cdd:PRK07238  264 FAEAAERDPE-LHRAWladTSVAPPG--GESFDAVARRVRR----ARDRLIAEYPG-ATVLVVSH 320
 
Name Accession Description Interval E-value
TFIIIC_sub6 pfam10419
TFIIIC subunit triple barrel domain; This is a family of proteins subunits of TFIIIC. TFIIIC ...
 313-409 1.84e-26

TFIIIC subunit triple barrel domain; This is a family of proteins subunits of TFIIIC. TFIIIC in yeast and humans is required for transcription of tRNA and 5 S RNA genes by RNA polymerase III. Yeast members of this family are fused to phosphoglycerate mutase domain.


Pssm-ID: 463085  Cd Length: 91  Bit Score: 101.49  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848 313 EEYEHVYVSLDVENRNYREKQTVQNQATLQHSGLESDKPLVKIGDNVYEGTWKKPLGTELAFasegskTDSNDSDSKTTD 392
Cdd:pfam10419   1 EETETVYVTLDLSGPLYSERLPDEEDATIQILGLDTENPLLQIGGQVYEGEWEETIGTELLF------EEDDDANKKSLE 74

                          90
                  ....*....|....*..
gi 1953602848 393 RVYRVTDSIDLHPIQPM 409
Cdd:pfam10419  75 LLGKSSKRLVLTRVFLK 91
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-172 1.79e-23

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: 96.89  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   6 IYIARHGyRSNWlptppaHPAPPTGVNSDVPLAPHGIEQARELAHYLISIDnqPQLIVSSPLYRCLQTSEPIADLLELPI 85
Cdd:pfam00300   1 LYLVRHG-ETEW------NLEGRFQGRTDSPLTELGREQAEALAERLAGEP--FDAIYSSPLKRARQTAEIIAEALGLPV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  86 YFDRGLGEWY------KPDRDIIPEPAsyDILNNFFpgklksEWPHSAIPSNkGETEEEIFERCKKfwpvFIKTVEERFP 159
Cdd:pfam00300  72 EIDPRLREIDfgdwegLTFEEIAERYP--EEYDAWL------ADPADYRPPG-GESLADVRARVRA----ALEELAARHP 138

                         170
                  ....*....|...
gi 1953602848 160 EvETILLVTHAAT 172
Cdd:pfam00300 139 G-KTVLVVSHGGV 150
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
5-172 3.95e-22

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 93.08  E-value: 3.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   5 TIYIARHGyRSNWlptppAHPAPPTGvNSDVPLAPHGIEQARELAHYLISIDnqPQLIVSSPLYRCLQTSEPIADLLELP 84
Cdd:COG0406     3 RLYLVRHG-ETEW-----NAEGRLQG-RLDVPLTELGRAQARALAERLADIP--FDAVYSSPLQRARQTAEALAEALGLP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  85 IYFDRGLGEWY------KPDRDIIPE-PASYDilnnffpgKLKSEWPHSAIPSnkGETEEEIFERCKKFWpvfiKTVEER 157
Cdd:COG0406    74 VEVDPRLREIDfgdwegLTFAELEARyPEALA--------AWLADPAEFRPPG--GESLADVQARVRAAL----EELLAR 139

                         170
                  ....*....|....*
gi 1953602848 158 FPEvETILLVTHAAT 172
Cdd:COG0406   140 HPG-GTVLVVTHGGV 153
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-207 1.02e-20

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: 87.76  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   5 TIYIARHGYRSNWLPTPPAHPapptgvnSDVPLAPHGIEQARELAHYLISIDNQPQLIVSSPLYRCLQTSEPIAD-LLEL 83
Cdd:cd07067     1 RLYLVRHGESEWNAEGRFQGW-------TDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEeLPGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  84 PIYFDRGLGEwykpdrdiipepasydilnnffpgklksewphsaipsnkgeteeeifERCKKFWpvfiKTVEERFPEvET 163
Cdd:cd07067    74 PVEVDPRLRE-----------------------------------------------ARVLPAL----EELIAPHDG-KN 101

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953602848 164 ILLVTHAATKIALGMTLLKFNsvrdtlDEDGNVIHCGSCSLDKY 207
Cdd:cd07067   102 VLIVSHGGVLRALLAYLLGLS------DEDILRLNLPNGSISVL 139
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 5-172 1.54e-19

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: 84.82  E-value: 1.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848    5 TIYIARHGyRSNWlptppaHPAPPTGVNSDVPLAPHGIEQARELAHYLIS-IDNQPQLIVSSPLYRCLQTSEPIADLLEL 83
Cdd:smart00855   1 RLYLIRHG-ETEW------NREGRLYGDTDVPLTELGRAQAEALGRLLASlLLPRFDVVYSSPLKRARQTAEALAIALGL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   84 PIYFDRGLGEWYKPDRDIIPEPASYDILNNFFPGKlksewPHSAIPSNKGETEEEIFERCKKFWpvfIKTVEERFPEVET 163
Cdd:smart00855  74 PGLRERDFGAWEGLTWDEIAAKYPEEYLAAWRDPY-----DPAPPAPPGGESLADLVERVEPAL---DELIATADASGQN 145


                   ....*....
gi 1953602848  164 ILLVTHAAT 172
Cdd:smart00855 146 VLIVSHGGV 154
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 5-184 5.00e-15

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: 72.06  E-value: 5.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   5 TIYIARHGYRSNWLPTPPAHPApptgvnsDVPLAPHGIEQARELAHYLISIDNQPQLIVSSPLYRCLQTSEPIADLLELP 84
Cdd:cd07040     1 VLYLVRHGEREPNAEGRFTGWG-------DGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  85 IyfdrglgewykpdrdiipepasydilnnffpgklksewphsaipsnkgETEEEIFERCKKFWpvfIKTVEERFPEVETI 164
Cdd:cd07040    74 L------------------------------------------------PVEVDPRARVLNAL---LELLARHLLDGKNV 102

                         170       180
                  ....*....|....*....|
gi 1953602848 165 LLVTHAATKIALGMTLLKFN 184
Cdd:cd07040   103 LIVSHGGTIRALLAALLGLS 122
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
6-91 4.62e-11

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 60.66  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   6 IYIARHG---YRSNWLPtppahpapptgvNSDVPLAPHGIEQARELAHYLISIDNQPQLIVSSPLYRCLQTSEPIADLLE 82
Cdd:COG2062     1 LILVRHAkaeWRAPGGD------------DFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALG 68

                          90
                  ....*....|.
gi 1953602848  83 LP--IYFDRGL 91
Cdd:COG2062    69 LPpkVEVEDEL 79
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 33-169 2.01e-07

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 52.67  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  33 SDVPLAPHGIEQARELAHYLISiDNQPQLIVSSPLYRCLQTSEPIADLLELPIYFDRGL-----GEWykpdrdiipEPAS 107
Cdd:PRK07238  194 GNPELTEVGRRQAAAAARYLAA-RGGIDAVVSSPLQRARDTAAAAAKALGLDVTVDDDLietdfGAW---------EGLT 263

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953602848 108 YDILNNFFPGkLKSEW---PHSAIPSnkGETEEEIFERCKKfwpvFIKTVEERFPEvETILLVTH 169
Cdd:PRK07238  264 FAEAAERDPE-LHRAWladTSVAPPG--GESFDAVARRVRR----ARDRLIAEYPG-ATVLVVSH 320
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
33-169 4.35e-07

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 50.05  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  33 SDVPLAPHGIEQARELAHYL--ISIDnqpqLIVSSPLYRCLQTSEPIADLLELPIYFDRGL-----GEW-YKPDRDIIPE 104
Cdd:PRK15004   23 APTPLTARGIEQAQNLHTLLrdVPFD----LVLCSELERAQHTARLVLSDRQLPVHIIPELnemffGDWeMRHHRDLMQE 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953602848 105 -PASYDILNNffpgklksEWPHsAIPSNkGETEEEIFERCKKfwpvFIKTVEErFPEVETILLVTH 169
Cdd:PRK15004   99 dAENYAAWCN--------DWQH-AIPTN-GEGFQAFSQRVER----FIARLSA-FQHYQNLLIVSH 149
PRK13463 PRK13463
phosphoserine phosphatase 1;
5-177 2.44e-05

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 45.04  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848   5 TIYIARHGyRSNWLPTPPAHPAPptgvNSdvPLAPHGIEQARELAHYLIsiDNQPQLIVSSPLYRCLQTSEPIADLLELP 84
Cdd:PRK13463    4 TVYVTRHG-ETEWNVAKRMQGRK----NS--ALTENGILQAKQLGERMK--DLSIHAIYSSPSERTLHTAELIKGERDIP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953602848  85 I-----YFDRGLGEWykpdrdiipEPASYDILNNFFPGKLKSEW--PHsAIPSNKGETEEEIFERCKKfwpvFIKTVEER 157
Cdd:PRK13463   75 IiadehFYEINMGIW---------EGQTIDDIERQYPDDIQLFWnePH-LFQSTSGENFEAVHKRVIE----GMQLLLEK 140

                         170       180
                  ....*....|....*....|.
gi 1953602848 158 FpEVETILLVTH-AATKIALG 177
Cdd:PRK13463  141 H-KGESILIVSHaAAAKLLVG 160
 
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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