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Conserved domains on  [gi|1730762|sp|P53929|]
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RecName: Full=Uncharacterized protein YNL108C

Protein Classification

phosphoglycerate mutase family protein( domain architecture ID 10162637)

phosphoglycerate mutase family protein belonging to the histidine phosphatase superfamily, contains a conserved His residue that is transiently phosphorylated during the catalytic cycle; similar to Saccharomyces cerevisiae phosphoglycerate mutase PMU1 that may have a function related to the manipulation of phosphate groups on carbohydrates

CATH:  3.40.50.1240
PubMed:  18092946|2543188
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-203 1.14e-19

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: 83.14  E-value: 1.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    5 NIYIARHGyRSNWlpkgpYPPPPTGIDNDVPLSEHGVEQAHELANYISKLDVKPEMIFSSPFYRCLETSKPTVEAL-KIP 83
Cdd:cd07067   1 RLYLVRHG-ESEW-----NAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELpGLP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762   84 LYVDRGVGEwykpdrpiipepathevmskffpsmispdwepsiipsnkgeteedifERCHKFWpvfiDRVERKFPNvKTI 163
Cdd:cd07067  75 VEVDPRLRE-----------------------------------------------ARVLPAL----EELIAPHDG-KNV 102

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1730762  164 MIVTHAATKSALGMNLLKFSSAKEPIDNkgtfIRNGSCAI 203
Cdd:cd07067 103 LIVSHGGVLRALLAYLLGLSDEDILRLN----LPNGSISV 138
 
Name Accession Description Interval E-value
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-203 1.14e-19

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: 83.14  E-value: 1.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    5 NIYIARHGyRSNWlpkgpYPPPPTGIDNDVPLSEHGVEQAHELANYISKLDVKPEMIFSSPFYRCLETSKPTVEAL-KIP 83
Cdd:cd07067   1 RLYLVRHG-ESEW-----NAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELpGLP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762   84 LYVDRGVGEwykpdrpiipepathevmskffpsmispdwepsiipsnkgeteedifERCHKFWpvfiDRVERKFPNvKTI 163
Cdd:cd07067  75 VEVDPRLRE-----------------------------------------------ARVLPAL----EELIAPHDG-KNV 102

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1730762  164 MIVTHAATKSALGMNLLKFSSAKEPIDNkgtfIRNGSCAI 203
Cdd:cd07067 103 LIVSHGGVLRALLAYLLGLSDEDILRLN----LPNGSISV 138
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-171 6.44e-19

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: 81.87  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762      6 IYIARHGyRSNWlpkgpYPPPPTGIDNDVPLSEHGVEQAHELANYISklDVKPEMIFSSPFYRCLETSKPTVEALKIPLY 85
Cdd:pfam00300   1 LYLVRHG-ETEW-----NLEGRFQGRTDSPLTELGREQAEALAERLA--GEPFDAIYSSPLKRARQTAEIIAEALGLPVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762     86 VDRGVGEWykpDRPIIPEPATHEVMSKF--FPSMISPDWEPSIIPsnKGETEEDIFERCHKfwpvFIDRVERKFPNvKTI 163
Cdd:pfam00300  73 IDPRLREI---DFGDWEGLTFEEIAERYpeEYDAWLADPADYRPP--GGESLADVRARVRA----ALEELAARHPG-KTV 142


                  ....*...
gi 1730762    164 MIVTHAAT 171
Cdd:pfam00300 143 LVVSHGGV 150
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
6-191 2.34e-18

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 80.37  E-value: 2.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    6 IYIARHGyRSNWlpkgPYPPPPTGIDnDVPLSEHGVEQAHELANYISklDVKPEMIFSSPFYRCLETSKPTVEALKIPLY 85
Cdd:COG0406   4 LYLVRHG-ETEW----NAEGRLQGRL-DVPLTELGRAQARALAERLA--DIPFDAVYSSPLQRARQTAEALAEALGLPVE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762   86 VDRGVGEWykpDRPIIPEPATHEVMSKFFPSMISPDWEPSIIPSNKGETEEDIFERCHKFWpvfiDRVERKFPNvKTIMI 165
Cdd:COG0406  76 VDPRLREI---DFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAAL----EELLARHPG-GTVLV 147

                       170       180       190
                ....*....|....*....|....*....|.
gi 1730762  166 VTHAAT-----KSALGMNLLKFssAKEPIDN 191
Cdd:COG0406 148 VTHGGVirallAHLLGLPLEAF--WRLRIDN 176
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 6-171 6.01e-18

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: 78.66  E-value: 6.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762       6 IYIARHGyRSNWlpkgPYPPPPTGiDNDVPLSEHGVEQAHELANYISKL-DVKPEMIFSSPFYRCLETSKPTVEALKIPL 84
Cdd:smart00855   2 LYLIRHG-ETEW----NREGRLYG-DTDVPLTELGRAQAEALGRLLASLlLPRFDVVYSSPLKRARQTAEALAIALGLPG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762      85 YVDRGVGEWykpdrpiipEPATHEVMSKFFPSMISPDWEPSIIPSN----KGETEEDIFERCHKFWpvfIDRVERKFPNV 160
Cdd:smart00855  76 LRERDFGAW---------EGLTWDEIAAKYPEEYLAAWRDPYDPAPpappGGESLADLVERVEPAL---DELIATADASG 143

                          170
                   ....*....|.
gi 1730762     161 KTIMIVTHAAT 171
Cdd:smart00855 144 QNVLIVSHGGV 154
PRK13463 PRK13463
phosphoserine phosphatase 1;
6-212 5.12e-08

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 51.97  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762     6 IYIARHGyRSNWlpkgPYPPPPTGIDNDVpLSEHGVEQAHELANYISKLDVkpEMIFSSPFYRCLETSKPTVEALKIPLY 85
Cdd:PRK13463   5 VYVTRHG-ETEW----NVAKRMQGRKNSA-LTENGILQAKQLGERMKDLSI--HAIYSSPSERTLHTAELIKGERDIPII 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    86 VDR-----GVGEWykpdrpiipEPATHEVMSKFFPSMISPDW-EPSIIPSNKGETEEDIFERCHKFWPVFIDRVERkfpn 159
Cdd:PRK13463  77 ADEhfyeiNMGIW---------EGQTIDDIERQYPDDIQLFWnEPHLFQSTSGENFEAVHKRVIEGMQLLLEKHKG---- 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1730762   160 vKTIMIVTHAAtksalGMNLLKFSSAKEPIDN--KGTFIRNGSCAIDKFELVKGE 212
Cdd:PRK13463 144 -ESILIVSHAA-----AAKLLVGHFAGIEIENvwDDPFMHSASLSIIEFEDGKGE 192
 
Name Accession Description Interval E-value
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 5-203 1.14e-19

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: 83.14  E-value: 1.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    5 NIYIARHGyRSNWlpkgpYPPPPTGIDNDVPLSEHGVEQAHELANYISKLDVKPEMIFSSPFYRCLETSKPTVEAL-KIP 83
Cdd:cd07067   1 RLYLVRHG-ESEW-----NAEGRFQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELpGLP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762   84 LYVDRGVGEwykpdrpiipepathevmskffpsmispdwepsiipsnkgeteedifERCHKFWpvfiDRVERKFPNvKTI 163
Cdd:cd07067  75 VEVDPRLRE-----------------------------------------------ARVLPAL----EELIAPHDG-KNV 102

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1730762  164 MIVTHAATKSALGMNLLKFSSAKEPIDNkgtfIRNGSCAI 203
Cdd:cd07067 103 LIVSHGGVLRALLAYLLGLSDEDILRLN----LPNGSISV 138
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 6-171 6.44e-19

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: 81.87  E-value: 6.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762      6 IYIARHGyRSNWlpkgpYPPPPTGIDNDVPLSEHGVEQAHELANYISklDVKPEMIFSSPFYRCLETSKPTVEALKIPLY 85
Cdd:pfam00300   1 LYLVRHG-ETEW-----NLEGRFQGRTDSPLTELGREQAEALAERLA--GEPFDAIYSSPLKRARQTAEIIAEALGLPVE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762     86 VDRGVGEWykpDRPIIPEPATHEVMSKF--FPSMISPDWEPSIIPsnKGETEEDIFERCHKfwpvFIDRVERKFPNvKTI 163
Cdd:pfam00300  73 IDPRLREI---DFGDWEGLTFEEIAERYpeEYDAWLADPADYRPP--GGESLADVRARVRA----ALEELAARHPG-KTV 142


                  ....*...
gi 1730762    164 MIVTHAAT 171
Cdd:pfam00300 143 LVVSHGGV 150
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
6-191 2.34e-18

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 80.37  E-value: 2.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    6 IYIARHGyRSNWlpkgPYPPPPTGIDnDVPLSEHGVEQAHELANYISklDVKPEMIFSSPFYRCLETSKPTVEALKIPLY 85
Cdd:COG0406   4 LYLVRHG-ETEW----NAEGRLQGRL-DVPLTELGRAQARALAERLA--DIPFDAVYSSPLQRARQTAEALAEALGLPVE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762   86 VDRGVGEWykpDRPIIPEPATHEVMSKFFPSMISPDWEPSIIPSNKGETEEDIFERCHKFWpvfiDRVERKFPNvKTIMI 165
Cdd:COG0406  76 VDPRLREI---DFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAAL----EELLARHPG-GTVLV 147

                       170       180       190
                ....*....|....*....|....*....|.
gi 1730762  166 VTHAAT-----KSALGMNLLKFssAKEPIDN 191
Cdd:COG0406 148 VTHGGVirallAHLLGLPLEAF--WRLRIDN 176
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 6-171 6.01e-18

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: 78.66  E-value: 6.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762       6 IYIARHGyRSNWlpkgPYPPPPTGiDNDVPLSEHGVEQAHELANYISKL-DVKPEMIFSSPFYRCLETSKPTVEALKIPL 84
Cdd:smart00855   2 LYLIRHG-ETEW----NREGRLYG-DTDVPLTELGRAQAEALGRLLASLlLPRFDVVYSSPLKRARQTAEALAIALGLPG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762      85 YVDRGVGEWykpdrpiipEPATHEVMSKFFPSMISPDWEPSIIPSN----KGETEEDIFERCHKFWpvfIDRVERKFPNV 160
Cdd:smart00855  76 LRERDFGAW---------EGLTWDEIAAKYPEEYLAAWRDPYDPAPpappGGESLADLVERVEPAL---DELIATADASG 143

                          170
                   ....*....|.
gi 1730762     161 KTIMIVTHAAT 171
Cdd:smart00855 144 QNVLIVSHGGV 154
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 6-216 5.45e-17

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: 75.91  E-value: 5.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    6 IYIARHGYRSNWLPKGpyppppTGIDNDVPLSEHGVEQAHELANYISKLDVKPEMIFSSPFYRCLETSKPTVEALKIPLy 85
Cdd:cd07040   2 LYLVRHGEREPNAEGR------FTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGL- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762   86 vdrgvgewykpdrPIIPEPAthevmskffpsmispdwepsiipsnkgeteedifERCHKFWpvfIDRVERKFPNVKTIMI 165
Cdd:cd07040  75 -------------PVEVDPR----------------------------------ARVLNAL---LELLARHLLDGKNVLI 104

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 1730762  166 VTHAATKSALGMNLLKFSSAKEPIDNkgtfIRNGSCAIdkFELVKGENESI 216
Cdd:cd07040 105 VSHGGTIRALLAALLGLSDEEILSLN----LPNGSILV--LELDECGGKYV 149
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
6-86 1.05e-10

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 58.73  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    6 IYIARHG---YRSNWLPkgpypppptgiDNDVPLSEHGVEQAHELANYISKLDVKPEMIFSSPFYRCLETSKPTVEALKI 82
Cdd:COG2062   1 LILVRHAkaeWRAPGGD-----------DFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGL 69


                ....
gi 1730762   83 PLYV 86
Cdd:COG2062  70 PPKV 73
PRK13463 PRK13463
phosphoserine phosphatase 1;
6-212 5.12e-08

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 51.97  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762     6 IYIARHGyRSNWlpkgPYPPPPTGIDNDVpLSEHGVEQAHELANYISKLDVkpEMIFSSPFYRCLETSKPTVEALKIPLY 85
Cdd:PRK13463   5 VYVTRHG-ETEW----NVAKRMQGRKNSA-LTENGILQAKQLGERMKDLSI--HAIYSSPSERTLHTAELIKGERDIPII 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    86 VDR-----GVGEWykpdrpiipEPATHEVMSKFFPSMISPDW-EPSIIPSNKGETEEDIFERCHKFWPVFIDRVERkfpn 159
Cdd:PRK13463  77 ADEhfyeiNMGIW---------EGQTIDDIERQYPDDIQLFWnEPHLFQSTSGENFEAVHKRVIEGMQLLLEKHKG---- 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1730762   160 vKTIMIVTHAAtksalGMNLLKFSSAKEPIDN--KGTFIRNGSCAIDKFELVKGE 212
Cdd:PRK13463 144 -ESILIVSHAA-----AAKLLVGHFAGIEIENvwDDPFMHSASLSIIEFEDGKGE 192
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 33-168 4.03e-07

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 50.36  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730762    33 DVPLSEHGVEQAHELANYISKLDvKPEMIFSSPFYRCLETSKPTVEALKIPLYVDRGV-----GEWykpdrpiipEPATH 107
Cdd:PRK07238 195 NPELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALGLDVTVDDDLietdfGAW---------EGLTF 264

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730762   108 -EVMSKFfpsmisPD------WEPSIIPSNkGETEEDIFERCHKfwpvFIDRVERKFPNvKTIMIVTH 168
Cdd:PRK07238 265 aEAAERD------PElhrawlADTSVAPPG-GESFDAVARRVRR----ARDRLIAEYPG-ATVLVVSH 320
 
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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