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Conserved domains on  [gi|1169081142|gb|ARB46182|]
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histidine phosphatase [Alloalcanivorax xenomutans]

Protein Classification

SixA phosphatase family protein( domain architecture ID 10788349)

SixA phosphatase family protein belongs to the histidine phosphatase superfamily, members of which contain a conserved His residue that is transiently phosphorylated during the catalytic cycle

CATH:  3.40.50.1240
EC:  3.1.3.-
Gene Ontology:  GO:0016791
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-120 2.68e-30

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


:

Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 107.27  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   3 VYLCRHGEAVAKAP--TDAERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCIAQAFGG-MEQESCGYLV 79
Cdd:COG2062     1 LILVRHAKAEWRAPggDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLpPKVEVEDELY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169081142  80 pEAQPERFLEWLMLQPKQENLVLVSHMPLVSLLTATWIGEP 120
Cdd:COG2062    81 -DADPEDLLDLLRELDDGETVLLVGHNPGLSELAALLAGGE 120
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-120 2.68e-30

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 107.27  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   3 VYLCRHGEAVAKAP--TDAERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCIAQAFGG-MEQESCGYLV 79
Cdd:COG2062     1 LILVRHAKAEWRAPggDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLpPKVEVEDELY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169081142  80 pEAQPERFLEWLMLQPKQENLVLVSHMPLVSLLTATWIGEP 120
Cdd:COG2062    81 -DADPEDLLDLLRELDDGETVLLVGHNPGLSELAALLAGGE 120
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 2-120 3.43e-23

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: 88.92  E-value: 3.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   2 RVYLCRHGEAVAKAP----TDAERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCIAQAFGGMEQEscgy 77
Cdd:cd07067     1 RLYLVRHGESEWNAEgrfqGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVE---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169081142  78 LVP---EAQPERFLEWLMLQPKQENLVLVSHMPLVSLLTATWIGEP 120
Cdd:cd07067    77 VDPrlrEARVLPALEELIAPHDGKNVLIVSHGGVLRALLAYLLGLS 122
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 1-114 5.24e-19

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 78.34  E-value: 5.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   1 MRVYLCRHGEAVAKAPTDAERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCIAQAFGGMEQ-ESCGYLV 79
Cdd:TIGR00249   1 MQLFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLNLPSSaEVLEGLT 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169081142  80 PEAQPERFLEWL--MLQPKQENLVLVSHMPLVSLLTA 114
Cdd:TIGR00249  81 PCGDIGLVSDYLeaLTNEGVASVLLVSHLPLVGYLVA 117
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 3-68 1.12e-09

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: 54.52  E-value: 1.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169081142   3 VYLCRHGEAVAKA------PTDAerPLTERGRAEVLSLWQTLREEGVSVgrLVASPYRRAQQTALCIAQAFG 68
Cdd:pfam00300   1 LYLVRHGETEWNLegrfqgRTDS--PLTELGREQAEALAERLAGEPFDA--IYSSPLKRARQTAEIIAEALG 68
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 2-68 1.14e-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: 53.62  E-value: 1.14e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169081142    2 RVYLCRHGEAVAKA----PTDAERPLTERGRAEVLSLWQTLREEG-VSVGRLVASPYRRAQQTALCIAQAFG 68
Cdd:smart00855   1 RLYLIRHGETEWNRegrlYGDTDVPLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALG 72
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
1-120 2.71e-06

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 45.04  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   1 MRVYLCRHGEAVA--------KAPTdaerPLTERGRAEVLSLWQTLReeGVSVGRLVASPYRRAQQTALCIAQA------ 66
Cdd:PRK15004    1 MRLWLVRHGETQAnvdglysgHAPT----PLTARGIEQAQNLHTLLR--DVPFDLVLCSELERAQHTARLVLSDrqlpvh 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142  67 ---------FGGME----------------------QESC-----GYLVPEAQPERFLEWLMLQPKQENLVLVSHMPLVS 110
Cdd:PRK15004   75 iipelnemfFGDWEmrhhrdlmqedaenyaawcndwQHAIptngeGFQAFSQRVERFIARLSAFQHYQNLLIVSHQGVLS 154

                         170
                  ....*....|
gi 1169081142 111 LLTATWIGEP 120
Cdd:PRK15004  155 LLIARLLGMP 164
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
3-120 2.68e-30

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 107.27  E-value: 2.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   3 VYLCRHGEAVAKAP--TDAERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCIAQAFGG-MEQESCGYLV 79
Cdd:COG2062     1 LILVRHAKAEWRAPggDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLpPKVEVEDELY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1169081142  80 pEAQPERFLEWLMLQPKQENLVLVSHMPLVSLLTATWIGEP 120
Cdd:COG2062    81 -DADPEDLLDLLRELDDGETVLLVGHNPGLSELAALLAGGE 120
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 2-120 3.43e-23

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: 88.92  E-value: 3.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   2 RVYLCRHGEAVAKAP----TDAERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCIAQAFGGMEQEscgy 77
Cdd:cd07067     1 RLYLVRHGESEWNAEgrfqGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVE---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169081142  78 LVP---EAQPERFLEWLMLQPKQENLVLVSHMPLVSLLTATWIGEP 120
Cdd:cd07067    77 VDPrlrEARVLPALEELIAPHDGKNVLIVSHGGVLRALLAYLLGLS 122
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 1-114 5.24e-19

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 78.34  E-value: 5.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   1 MRVYLCRHGEAVAKAPTDAERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCIAQAFGGMEQ-ESCGYLV 79
Cdd:TIGR00249   1 MQLFIMRHGDAALDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVGDCLNLPSSaEVLEGLT 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1169081142  80 PEAQPERFLEWL--MLQPKQENLVLVSHMPLVSLLTA 114
Cdd:TIGR00249  81 PCGDIGLVSDYLeaLTNEGVASVLLVSHLPLVGYLVA 117
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 2-120 3.94e-18

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: 3.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   2 RVYLCRHGEAVAKAP----TDAERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCIAQAFG-GMEQEscg 76
Cdd:cd07040     1 VLYLVRHGEREPNAEgrftGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFeGLPVE--- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1169081142  77 yLVPEAQPERFLEWLMLQ--PKQENLVLVSHMPLVSLLTATWIGEP 120
Cdd:cd07040    78 -VDPRARVLNALLELLARhlLDGKNVLIVSHGGTIRALLAALLGLS 122
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-68 2.76e-11

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 58.80  E-value: 2.76e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169081142   1 MRVYLCRHGEAVAKAP----TDAERPLTERGRAEVLSLWQTLREEGVSvgRLVASPYRRAQQTALCIAQAFG 68
Cdd:COG0406     2 TRLYLVRHGETEWNAEgrlqGRLDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALAEALG 71
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 3-68 1.12e-09

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: 54.52  E-value: 1.12e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169081142   3 VYLCRHGEAVAKA------PTDAerPLTERGRAEVLSLWQTLREEGVSVgrLVASPYRRAQQTALCIAQAFG 68
Cdd:pfam00300   1 LYLVRHGETEWNLegrfqgRTDS--PLTELGREQAEALAERLAGEPFDA--IYSSPLKRARQTAEIIAEALG 68
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 2-68 1.14e-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: 53.62  E-value: 1.14e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169081142    2 RVYLCRHGEAVAKA----PTDAERPLTERGRAEVLSLWQTLREEG-VSVGRLVASPYRRAQQTALCIAQAFG 68
Cdd:smart00855   1 RLYLIRHGETEWNRegrlYGDTDVPLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALG 72
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
1-120 2.71e-06

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 45.04  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142   1 MRVYLCRHGEAVA--------KAPTdaerPLTERGRAEVLSLWQTLReeGVSVGRLVASPYRRAQQTALCIAQA------ 66
Cdd:PRK15004    1 MRLWLVRHGETQAnvdglysgHAPT----PLTARGIEQAQNLHTLLR--DVPFDLVLCSELERAQHTARLVLSDrqlpvh 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142  67 ---------FGGME----------------------QESC-----GYLVPEAQPERFLEWLMLQPKQENLVLVSHMPLVS 110
Cdd:PRK15004   75 iipelnemfFGDWEmrhhrdlmqedaenyaawcndwQHAIptngeGFQAFSQRVERFIARLSAFQHYQNLLIVSHQGVLS 154

                         170
                  ....*....|
gi 1169081142 111 LLTATWIGEP 120
Cdd:PRK15004  155 LLIARLLGMP 164
PRK06193 PRK06193
hypothetical protein; Provisional
 19-105 3.50e-04

hypothetical protein; Provisional


Pssm-ID: 235734  Cd Length: 206  Bit Score: 39.28  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169081142  19 AERPLTERGRAEVLSLWQTLREEGVSVGRLVASPYRRAQQTALCiaqAFGGMEQES------CGYLVPEAQPE---RFLE 89
Cdd:PRK06193   70 TQRNLSEEGREQARAIGEAFRALAIPVGKVISSPYCRAWETAQL---AFGRHEKEIrlnflnSEPVPAERNALlkaGLRP 146

                          90
                  ....*....|....*..
gi 1169081142  90 WLMLQPKQ-ENLVLVSH 105
Cdd:PRK06193  147 LLTTPPDPgTNTVLVGH 163
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-68 4.81e-04

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 38.94  E-value: 4.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169081142   1 MRVYLCRHGEAVAKAPT----DAERPLTERGRAEVLSLWQTLREEGVSvgRLVASPYRRAQQTALCIAQAFG 68
Cdd:PRK03482    2 LQVYLVRHGETQWNAERriqgQSDSPLTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAEIIAQACG 71
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 2-68 6.11e-03

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 35.72  E-value: 6.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169081142   2 RVYLCRHGEAvakaPTDAER--------PLTERGRAEVLSLWQTLREEGvSVGRLVASPYRRAQQTALCIAQAFG 68
Cdd:PRK07238  173 RLLLLRHGQT----ELSVQRrysgrgnpELTEVGRRQAAAAARYLAARG-GIDAVVSSPLQRARDTAAAAAKALG 242
 
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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