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Conserved domains on  [gi|446130463|ref|WP_000208318|]
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MULTISPECIES: histidine phosphatase family protein [Acinetobacter]

Protein Classification

histidine phosphatase family protein( domain architecture ID 10001383)

histidine phosphatase family protein is a probable phosphatase that may catalyze the dephosphorylation of a phosphorylated substrate involving a conserved catalytic histidine residue which becomes phosphorylated during the reaction

CATH:  3.40.50.1240
Gene Ontology:  GO:0016791
PubMed:  18092946
SCOP:  3000781

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-216 2.19e-31

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 113.89  E-value: 2.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   1 MTTIYLVRHGQASFGKSNY------DELSENGEAQATLLGQYFKKIlkEQPYVVAGTMQRHEQTAQLALKECFPDAVIHH 74
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRlqgrldVPLTELGRAQARALAERLADI--PFDAVYSSPLQRARQTAEALAEALGLPVEVDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463  75 NnlWNEFNhqqvFARYEPRfeqpellkadvakehnPRAYLAKIFEGAIERWTEGDFHHEYD--ESWPHFKNRVETALQQL 152
Cdd:COG0406   79 R--LREID----FGDWEGL----------------TFAELEARYPEALAAWLADPAEFRPPggESLADVQARVRAALEEL 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446130463 153 cdeLAKTKPRYAVVFTSGGVISVAIGKLLELSPNRTFalNWAITNTSLTTLRLVGNEAQVLSLN 216
Cdd:COG0406  137 ---LARHPGGTVLVVTHGGVIRALLAHLLGLPLEAFW--RLRIDNASVTVLEFDDGRWRLVALN 195
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-216 2.19e-31

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 113.89  E-value: 2.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   1 MTTIYLVRHGQASFGKSNY------DELSENGEAQATLLGQYFKKIlkEQPYVVAGTMQRHEQTAQLALKECFPDAVIHH 74
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRlqgrldVPLTELGRAQARALAERLADI--PFDAVYSSPLQRARQTAEALAEALGLPVEVDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463  75 NnlWNEFNhqqvFARYEPRfeqpellkadvakehnPRAYLAKIFEGAIERWTEGDFHHEYD--ESWPHFKNRVETALQQL 152
Cdd:COG0406   79 R--LREID----FGDWEGL----------------TFAELEARYPEALAAWLADPAEFRPPggESLADVQARVRAALEEL 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446130463 153 cdeLAKTKPRYAVVFTSGGVISVAIGKLLELSPNRTFalNWAITNTSLTTLRLVGNEAQVLSLN 216
Cdd:COG0406  137 ---LARHPGGTVLVVTHGGVIRALLAHLLGLPLEAFW--RLRIDNASVTVLEFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-217 3.91e-22

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: 89.58  E-value: 3.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463    4 IYLVRHGQASF-------GKSNYDeLSENGEAQATLLGQYFKKIlkEQPYVVAGTMQRHEQTAQLALKECfpDAVIHHNN 76
Cdd:pfam00300   1 LYLVRHGETEWnlegrfqGRTDSP-LTELGREQAEALAERLAGE--PFDAIYSSPLKRARQTAEIIAEAL--GLPVEIDP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   77 LWNEFNhqqvFARYEprfeqpELLKADVAKEHnPRAYLAKIFEGAIERWTEGdfhheydESWPHFKNRVETALQQLCdel 156
Cdd:pfam00300  76 RLREID----FGDWE------GLTFEEIAERY-PEEYDAWLADPADYRPPGG-------ESLADVRARVRAALEELA--- 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446130463  157 AKTKPRYAVVFTSGGVISVAIGKLLELSPnrTFALNWAITNTSLTTLRLVGNEAQVLSLNE 217
Cdd:pfam00300 135 ARHPGKTVLVVSHGGVIRALLAHLLGLPL--EALRRFPLDNASLSILEFDGGGWVLVLLND 193
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-176 1.35e-15

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: 71.34  E-value: 1.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463     3 TIYLVRHGQASFGKSNY------DELSENGEAQATLLGQYFKKILKEQP-YVVAGTMQRHEQTAQLALKEcfpdaviHHN 75
Cdd:smart00855   1 RLYLIRHGETEWNREGRlygdtdVPLTELGRAQAEALGRLLASLLLPRFdVVYSSPLKRARQTAEALAIA-------LGL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463    76 NLWNEFNhqqvFARYEprfeqpELLKADVAKEHnPRAYLAKIFEGAIERwtegDFHHEYDESWPHFKNRVETALQQLCDE 155
Cdd:smart00855  74 PGLRERD----FGAWE------GLTWDEIAAKY-PEEYLAAWRDPYDPA----PPAPPGGESLADLVERVEPALDELIAT 138

                          170       180
                   ....*....|....*....|.
gi 446130463   156 LAKtKPRYAVVFTSGGVISVA 176
Cdd:smart00855 139 ADA-SGQNVLIVSHGGVIRAL 158
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-73 2.58e-12

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: 62.43  E-value: 2.58e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446130463   3 TIYLVRHGQASFGKSN------YDELSENGEAQATLLGQYFKKILKEQPYVVAGTMQRHEQTAQLALKECFPDAVIH 73
Cdd:cd07040    1 VLYLVRHGEREPNAEGrftgwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVE 77
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-203 2.29e-09

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


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 54.94  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463    4 IYLVRHGQ-ASFGKSNY----DELSENGEAQATLLGQYFKKILKEQpyVVAGTMQRHEQTAQLALKECfpDAVIHHNNLW 78
Cdd:TIGR03162   1 LYLIRHGEtDVNAGLCYgqtdVPLAESGEEQAAALREKLADVPFDA--VYSSPLSRCRELAEILAERR--GLPIIKDDRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   79 NEFNhqqvFARYEPRfEQPELlkadvakehnPRAYlakifeGAIERWTEGDFHHEY--DESWPHFKNRVETALQQLcdeL 156
Cdd:TIGR03162  77 REMD----FGDWEGR-SWDEI----------PEAY------PELDAWAADWQHARPpgGESFADFYQRVSEFLEEL---L 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446130463  157 AKTKPRYAVVFTSGGVISVAIGKLLELSPNRTFAlnWAITNTSLTTL 203
Cdd:TIGR03162 133 KAHEGDNVLIVTHGGVIRALLAHLLGLPLEQWWS--FAVEYGSITLI 177
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 4-70 9.96e-06

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 45.57  E-value: 9.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446130463   4 IYLVRHGQASFGKSNYDE---LSENGEAQATLLGQYFKKILKEQPY------VVAGTMQRHEQTAQLALkECFPDA 70
Cdd:PTZ00122 105 IILVRHGQYINESSNDDNikrLTELGKEQARITGKYLKEQFGEILVdkkvkaIYHSDMTRAKETAEIIS-EAFPGV 179
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-216 2.19e-31

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 113.89  E-value: 2.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   1 MTTIYLVRHGQASFGKSNY------DELSENGEAQATLLGQYFKKIlkEQPYVVAGTMQRHEQTAQLALKECFPDAVIHH 74
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRlqgrldVPLTELGRAQARALAERLADI--PFDAVYSSPLQRARQTAEALAEALGLPVEVDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463  75 NnlWNEFNhqqvFARYEPRfeqpellkadvakehnPRAYLAKIFEGAIERWTEGDFHHEYD--ESWPHFKNRVETALQQL 152
Cdd:COG0406   79 R--LREID----FGDWEGL----------------TFAELEARYPEALAAWLADPAEFRPPggESLADVQARVRAALEEL 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446130463 153 cdeLAKTKPRYAVVFTSGGVISVAIGKLLELSPNRTFalNWAITNTSLTTLRLVGNEAQVLSLN 216
Cdd:COG0406  137 ---LARHPGGTVLVVTHGGVIRALLAHLLGLPLEAFW--RLRIDNASVTVLEFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-217 3.91e-22

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: 89.58  E-value: 3.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463    4 IYLVRHGQASF-------GKSNYDeLSENGEAQATLLGQYFKKIlkEQPYVVAGTMQRHEQTAQLALKECfpDAVIHHNN 76
Cdd:pfam00300   1 LYLVRHGETEWnlegrfqGRTDSP-LTELGREQAEALAERLAGE--PFDAIYSSPLKRARQTAEIIAEAL--GLPVEIDP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   77 LWNEFNhqqvFARYEprfeqpELLKADVAKEHnPRAYLAKIFEGAIERWTEGdfhheydESWPHFKNRVETALQQLCdel 156
Cdd:pfam00300  76 RLREID----FGDWE------GLTFEEIAERY-PEEYDAWLADPADYRPPGG-------ESLADVRARVRAALEELA--- 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446130463  157 AKTKPRYAVVFTSGGVISVAIGKLLELSPnrTFALNWAITNTSLTTLRLVGNEAQVLSLNE 217
Cdd:pfam00300 135 ARHPGKTVLVVSHGGVIRALLAHLLGLPL--EALRRFPLDNASLSILEFDGGGWVLVLLND 193
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-176 1.35e-15

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: 71.34  E-value: 1.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463     3 TIYLVRHGQASFGKSNY------DELSENGEAQATLLGQYFKKILKEQP-YVVAGTMQRHEQTAQLALKEcfpdaviHHN 75
Cdd:smart00855   1 RLYLIRHGETEWNREGRlygdtdVPLTELGRAQAEALGRLLASLLLPRFdVVYSSPLKRARQTAEALAIA-------LGL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463    76 NLWNEFNhqqvFARYEprfeqpELLKADVAKEHnPRAYLAKIFEGAIERwtegDFHHEYDESWPHFKNRVETALQQLCDE 155
Cdd:smart00855  74 PGLRERD----FGAWE------GLTWDEIAAKY-PEEYLAAWRDPYDPA----PPAPPGGESLADLVERVEPALDELIAT 138

                          170       180
                   ....*....|....*....|.
gi 446130463   156 LAKtKPRYAVVFTSGGVISVA 176
Cdd:smart00855 139 ADA-SGQNVLIVSHGGVIRAL 158
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-73 2.58e-12

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: 62.43  E-value: 2.58e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446130463   3 TIYLVRHGQASFGKSN------YDELSENGEAQATLLGQYFKKILKEQPYVVAGTMQRHEQTAQLALKECFPDAVIH 73
Cdd:cd07040    1 VLYLVRHGEREPNAEGrftgwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVE 77
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-77 2.22e-09

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: 54.25  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   3 TIYLVRHGQASFGKSN-----YD-ELSENGEAQATLLGQYFKKILKEQPYVVAGTMQRHEQTAQLALKECFPDAVIHHNN 76
Cdd:cd07067    1 RLYLVRHGESEWNAEGrfqgwTDvPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVDPR 80


                 .
gi 446130463  77 L 77
Cdd:cd07067   81 L 81
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-203 2.29e-09

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


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 54.94  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463    4 IYLVRHGQ-ASFGKSNY----DELSENGEAQATLLGQYFKKILKEQpyVVAGTMQRHEQTAQLALKECfpDAVIHHNNLW 78
Cdd:TIGR03162   1 LYLIRHGEtDVNAGLCYgqtdVPLAESGEEQAAALREKLADVPFDA--VYSSPLSRCRELAEILAERR--GLPIIKDDRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   79 NEFNhqqvFARYEPRfEQPELlkadvakehnPRAYlakifeGAIERWTEGDFHHEY--DESWPHFKNRVETALQQLcdeL 156
Cdd:TIGR03162  77 REMD----FGDWEGR-SWDEI----------PEAY------PELDAWAADWQHARPpgGESFADFYQRVSEFLEEL---L 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446130463  157 AKTKPRYAVVFTSGGVISVAIGKLLELSPNRTFAlnWAITNTSLTTL 203
Cdd:TIGR03162 133 KAHEGDNVLIVTHGGVIRALLAHLLGLPLEQWWS--FAVEYGSITLI 177
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 4-70 9.96e-06

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 45.57  E-value: 9.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446130463   4 IYLVRHGQASFGKSNYDE---LSENGEAQATLLGQYFKKILKEQPY------VVAGTMQRHEQTAQLALkECFPDA 70
Cdd:PTZ00122 105 IILVRHGQYINESSNDDNikrLTELGKEQARITGKYLKEQFGEILVdkkvkaIYHSDMTRAKETAEIIS-EAFPGV 179
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-79 1.73e-05

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 43.32  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463   4 IYLVRHGQASFGKSNYD----ELSENGEAQATLLGQYFKKILKEQPYVVAGTMQRHEQTAQLALKEC-FPDAVIHHNNLW 78
Cdd:COG2062    1 LILVRHAKAEWRAPGGDdfdrPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALgLPPKVEVEDELY 80


                 .
gi 446130463  79 N 79
Cdd:COG2062   81 D 81
PRK13462 PRK13462
acid phosphatase; Provisional
 6-62 2.04e-04

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 40.97  E-value: 2.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446130463   6 LVRHGQASFGKSNYD------ELSENGEAQATLLGQYFKKILKEQPYVVAGTMQRHEQTAQLA 62
Cdd:PRK13462  10 LLRHGETEWSKSGRHtgrtelELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKLA 72
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 4-60 5.22e-04

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 39.05  E-value: 5.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446130463    4 IYLVRHGQASFgKSNYD---ELSENGEAQATLLGQYFKKILKEQPYVVAGTMQRHEQTAQ 60
Cdd:TIGR00249   3 LFIMRHGDAAL-DAASDsvrPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAE 61
gpmA PRK14120
phosphoglyceromutase; Provisional
 1-65 2.85e-03

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 37.71  E-value: 2.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446130463   1 MTTIYLVRHGQASFGKSNY-----D-ELSENGEAQATLLGQyfkkILKEQ---PYVVAGTMQRHE-QTAQLALKE 65
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNLftgwvDvDLTEKGEAEAKRGGE----LLAEAgvlPDVVYTSLLRRAiRTANLALDA 74
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-66 4.31e-03

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 37.01  E-value: 4.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446130463   1 MTTIYLVRHGQASF-------GKSNyDELSENGEAQATLLGQYFKKIlkEQPYVVAGTMQRHEQTAQLALKEC 66
Cdd:PRK03482   1 MLQVYLVRHGETQWnaerriqGQSD-SPLTAKGEQQAMQVAERAKEL--GITHIISSDLGRTRRTAEIIAQAC 70
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 2-66 7.50e-03

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: 36.60  E-value: 7.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446130463   2 TTIYLVRHGQASFGKSN-----YD-ELSENGEAQATLLGqyfkKILKEQPYV--VAGT--MQRHEQTAQLALKEC 66
Cdd:COG0588    1 YKLVLLRHGESEWNLENrftgwTDvDLSEKGRAEAKRAG----RLLKEAGFLfdVAYTsvLKRAIRTLWIVLDEM 71
 
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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