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Conserved domains on  [gi|787738487|ref|WP_045757435|]
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histidine phosphatase family protein [Xanthomonas albilineans]

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];
4-158 6.62e-50

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


:

Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 156.96  E-value: 6.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487   4 VILLRHAHAEPADTGQADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAILGLTGYVEQ-RLEPCIY 82
Cdd:COG2062    1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKvEVEDELY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 787738487  83 EATSGTLADLLDGHRDVERLLLVGHNPGMERLVALMHSGQsgDYRGMPTASIAVLAVPQEApIEPGVARLNAFWWP 158
Cdd:COG2062   81 DADPEDLLDLLRELDDGETVLLVGHNPGLSELAALLAGGE--PLDGFPTGGLAVLEFDIDD-LGPGKGRLVWFLTP 153
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-158 6.62e-50

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 156.96  E-value: 6.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487   4 VILLRHAHAEPADTGQADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAILGLTGYVEQ-RLEPCIY 82
Cdd:COG2062    1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKvEVEDELY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 787738487  83 EATSGTLADLLDGHRDVERLLLVGHNPGMERLVALMHSGQsgDYRGMPTASIAVLAVPQEApIEPGVARLNAFWWP 158
Cdd:COG2062   81 DADPEDLLDLLRELDDGETVLLVGHNPGLSELAALLAGGE--PLDGFPTGGLAVLEFDIDD-LGPGKGRLVWFLTP 153
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-137 3.63e-27

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: 99.32  E-value: 3.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487   3 EVILLRHAHAEPADTG--QADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAILGLTGYVEQRLEPC 80
Cdd:cd07067    1 RLYLVRHGESEWNAEGrfQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487  81 IYEA-TSGTLADLLDGHRDvERLLLVGHNPGMERLVALM--HSGQSGDYRGMPTASIAVL 137
Cdd:cd07067   81 LREArVLPALEELIAPHDG-KNVLIVSHGGVLRALLAYLlgLSDEDILRLNLPNGSISVL 139
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 3-123 6.19e-13

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 62.55  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487    3 EVILLRHAHAEPADTgqADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAI---LGLTGYVE--QRL 77
Cdd:TIGR00249   2 QLFIMRHGDAALDAA--SDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVgdcLNLPSSAEvlEGL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 787738487   78 EPCiyeATSGTLADLLDG--HRDVERLLLVGHNPGMERLVALMHSGQS 123
Cdd:TIGR00249  80 TPC---GDIGLVSDYLEAltNEGVASVLLVSHLPLVGYLVAELCPGEN 124
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-72 5.70e-12

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: 59.78  E-value: 5.70e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 787738487     3 EVILLRHAHAE--PADTGQADFDRPLSPHGLAEADAAGRWLLEQRLV-PDRVLCSPARRARETLEAILGLTGY 72
Cdd:smart00855   1 RLYLIRHGETEwnREGRLYGDTDVPLTELGRAQAEALGRLLASLLLPrFDVVYSSPLKRARQTAEALAIALGL 73
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-71 6.21e-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: 52.21  E-value: 6.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487    4 VILLRHAHAEPADTG--QADFDRPLSPHGLAEADAAGRWLleQRLVPDRVLCSPARRARETLEAILGLTG 71
Cdd:pfam00300   1 LYLVRHGETEWNLEGrfQGRTDSPLTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALG 68
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-62 2.21e-05

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 42.72  E-value: 2.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 787738487   1 MREVILLRHAHAEPADTGQadF----DRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARET 62
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNL--FtgwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRT 67
 
Name Accession Description Interval E-value
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-158 6.62e-50

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 156.96  E-value: 6.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487   4 VILLRHAHAEPADTGQADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAILGLTGYVEQ-RLEPCIY 82
Cdd:COG2062    1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKvEVEDELY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 787738487  83 EATSGTLADLLDGHRDVERLLLVGHNPGMERLVALMHSGQsgDYRGMPTASIAVLAVPQEApIEPGVARLNAFWWP 158
Cdd:COG2062   81 DADPEDLLDLLRELDDGETVLLVGHNPGLSELAALLAGGE--PLDGFPTGGLAVLEFDIDD-LGPGKGRLVWFLTP 153
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-137 3.63e-27

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: 99.32  E-value: 3.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487   3 EVILLRHAHAEPADTG--QADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAILGLTGYVEQRLEPC 80
Cdd:cd07067    1 RLYLVRHGESEWNAEGrfQGWTDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487  81 IYEA-TSGTLADLLDGHRDvERLLLVGHNPGMERLVALM--HSGQSGDYRGMPTASIAVL 137
Cdd:cd07067   81 LREArVLPALEELIAPHDG-KNVLIVSHGGVLRALLAYLlgLSDEDILRLNLPNGSISVL 139
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 4-137 3.05e-20

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: 81.31  E-value: 3.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487   4 VILLRHAHAEPADTG--QADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAIL-GLTGYVEQRLEPC 80
Cdd:cd07040    2 LYLVRHGEREPNAEGrfTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILeGLFEGLPVEVDPR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487  81 iyEATSGTLADLLDGH-RDVERLLLVGHNPGMERLVALM--HSGQSGDYRGMPTASIAVL 137
Cdd:cd07040   82 --ARVLNALLELLARHlLDGKNVLIVSHGGTIRALLAALlgLSDEEILSLNLPNGSILVL 139
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 3-123 6.19e-13

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 62.55  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487    3 EVILLRHAHAEPADTgqADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAI---LGLTGYVE--QRL 77
Cdd:TIGR00249   2 QLFIMRHGDAALDAA--SDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVgdcLNLPSSAEvlEGL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 787738487   78 EPCiyeATSGTLADLLDG--HRDVERLLLVGHNPGMERLVALMHSGQS 123
Cdd:TIGR00249  80 TPC---GDIGLVSDYLEAltNEGVASVLLVSHLPLVGYLVAELCPGEN 124
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-77 2.49e-12

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 61.50  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487   1 MREVILLRHAHAEPADTG--QADFDRPLSPHGLAEADAAGRWLleQRLVPDRVLCSPARRARETLEAI---LGLTGYVEQ 75
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGrlQGRLDVPLTELGRAQARALAERL--ADIPFDAVYSSPLQRARQTAEALaeaLGLPVEVDP 78


                 ..
gi 787738487  76 RL 77
Cdd:COG0406   79 RL 80
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-72 5.70e-12

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: 59.78  E-value: 5.70e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 787738487     3 EVILLRHAHAE--PADTGQADFDRPLSPHGLAEADAAGRWLLEQRLV-PDRVLCSPARRARETLEAILGLTGY 72
Cdd:smart00855   1 RLYLIRHGETEwnREGRLYGDTDVPLTELGRAQAEALGRLLASLLLPrFDVVYSSPLKRARQTAEALAIALGL 73
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-71 6.21e-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: 52.21  E-value: 6.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 787738487    4 VILLRHAHAEPADTG--QADFDRPLSPHGLAEADAAGRWLleQRLVPDRVLCSPARRARETLEAILGLTG 71
Cdd:pfam00300   1 LYLVRHGETEWNLEGrfQGRTDSPLTELGREQAEALAERL--AGEPFDAIYSSPLKRARQTAEIIAEALG 68
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 4-67 7.35e-07

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: 47.00  E-value: 7.35e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 787738487   4 VILLRHAH----AEPADTGQADFDrpLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAIL 67
Cdd:COG0588    3 LVLLRHGEsewnLENRFTGWTDVD--LSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLWIVL 68
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-62 2.21e-05

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 42.72  E-value: 2.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 787738487   1 MREVILLRHAHAEPADTGQadF----DRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARET 62
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNL--FtgwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRT 67
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 2-71 1.13e-04

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 40.44  E-value: 1.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 787738487   2 REVILLRHAHAE----PADTGQADFDrpLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEAILGLTG 71
Cdd:PRK01295   3 RTLVLVRHGQSEwnlkNLFTGWRDPD--LTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLILEELG 74
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
23-68 1.87e-04

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 40.03  E-value: 1.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 787738487  23 DRPLSPHGLAEADAAGRWLleqRLVP-DRVLCSPARRARETLEAILG 68
Cdd:PRK15004  24 PTPLTARGIEQAQNLHTLL---RDVPfDLVLCSELERAQHTARLVLS 67
PRK13462 PRK13462
acid phosphatase; Provisional
 4-70 1.88e-04

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 39.81  E-value: 1.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 787738487   4 VILLRHAHAEPADTGQ--ADFDRPLSPHGLAEADAAGRWLLEQRLVPDRVLCSPARRARETLEaILGLT 70
Cdd:PRK13462   8 LLLLRHGETEWSKSGRhtGRTELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAK-LAGLT 75
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 23-69 5.35e-03

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 36.11  E-value: 5.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 787738487  23 DRPLSPHGLAEADAAGRWLlEQRLVPDRVLCSPARRARETLEAI---LGL 69
Cdd:PRK07238 195 NPELTEVGRRQAAAAARYL-AARGGIDAVVSSPLQRARDTAAAAakaLGL 243
 
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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