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Conserved domains on  [gi|491088349|ref|WP_004949960|]
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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 3.68e-34

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 121.20  E-value: 3.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   1 MTTIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFfkhtLKEHPL--VLAGSMQRHQQTAQLALAQSfdDAPI 72
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQgrldvpLTELGRAQARALAER----LADIPFdaVYSSPLQRARQTAEALAEAL--GLPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349  73 HTESAWNEFDhqqvfakyderFNQPELLkqdvelianPRAYLAKIFDGAIERWIGEQYDHEYH--ETWLGFQTRVEGALH 150
Cdd:COG0406   75 EVDPRLREID-----------FGDWEGL---------TFAELEARYPEALAAWLADPAEFRPPggESLADVQARVRAALE 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491088349 151 GLcqhIDATQPRQAVVFSSGGVISVAVGKVLGLNAKQIFalNWSIANASITTLRWTDGRLQLLSFN 216
Cdd:COG0406  135 EL---LARHPGGTVLVVTHGGVIRALLAHLLGLPLEAFW--RLRIDNASVTVLEFDDGRWRLVALN 195
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-216 3.68e-34

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 121.20  E-value: 3.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   1 MTTIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFfkhtLKEHPL--VLAGSMQRHQQTAQLALAQSfdDAPI 72
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQgrldvpLTELGRAQARALAER----LADIPFdaVYSSPLQRARQTAEALAEAL--GLPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349  73 HTESAWNEFDhqqvfakyderFNQPELLkqdvelianPRAYLAKIFDGAIERWIGEQYDHEYH--ETWLGFQTRVEGALH 150
Cdd:COG0406   75 EVDPRLREID-----------FGDWEGL---------TFAELEARYPEALAAWLADPAEFRPPggESLADVQARVRAALE 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491088349 151 GLcqhIDATQPRQAVVFSSGGVISVAVGKVLGLNAKQIFalNWSIANASITTLRWTDGRLQLLSFN 216
Cdd:COG0406  135 EL---LARHPGGTVLVVTHGGVIRALLAHLLGLPLEAFW--RLRIDNASVTVLEFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-217 5.72e-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: 89.19  E-value: 5.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349    4 IYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFfkhtLKEHPL--VLAGSMQRHQQTAQLALAQSfdDAPIHTE 75
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQgrtdspLTELGREQAEALAER----LAGEPFdaIYSSPLKRARQTAEIIAEAL--GLPVEID 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   76 SAWNEFDhqqvFAKYDERfnqpellkqdvelianPRAYLAKIFDGAIERWIGEQYDHEYH--ETWLGFQTRVEGALHGLC 153
Cdd:pfam00300  75 PRLREID----FGDWEGL----------------TFEEIAERYPEEYDAWLADPADYRPPggESLADVRARVRAALEELA 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491088349  154 QhidATQPRQAVVFSSGGVISVAVGKVLGLNAKQIFalNWSIANASITTLRWTDGRLQLLSFNE 217
Cdd:pfam00300 135 A---RHPGKTVLVVSHGGVIRALLAHLLGLPLEALR--RFPLDNASLSILEFDGGGWVLVLLND 193
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-176 9.52e-13

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: 63.63  E-value: 9.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349     3 TIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFFKHTLKEHP-LVLAGSMQRHQQTAQLALAQSFDDapihte 75
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYgdtdvpLTELGRAQAEALGRLLASLLLPRFdVVYSSPLKRARQTAEALAIALGLP------ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349    76 sAWNEFDhqqvFAKYDERfnqpellkqdvelianPRAYLAKIFDGAIERWIGEQYDHEYH-----ETWLGFQTRVEGALH 150
Cdd:smart00855  75 -GLRERD----FGAWEGL----------------TWDEIAAKYPEEYLAAWRDPYDPAPPappggESLADLVERVEPALD 133

                          170       180
                   ....*....|....*....|....*.
gi 491088349   151 GLCQHiDATQPRQAVVFSSGGVISVA 176
Cdd:smart00855 134 ELIAT-ADASGQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-80 3.04e-12

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: 62.34  E-value: 3.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   3 TIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFFKHTLKEHPLVLAGSMQRHQQTAQLaLAQSFDDAPIHTES 76
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQgwtdvpLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEI-ILEELPGLPVEVDP 79


                 ....
gi 491088349  77 AWNE 80
Cdd:cd07067   80 RLRE 83
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-203 5.36e-07

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: 48.00  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349    4 IYLVRHGQ-ASFGAASYDQ----LSAKGEQQAQVVGDFFKHTLKEhpLVLAGSMQRHQQTAQLALAQsfDDAPIHTESAW 78
Cdd:TIGR03162   1 LYLIRHGEtDVNAGLCYGQtdvpLAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILAER--RGLPIIKDDRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   79 NEFDhqqvFAKYDerfNQP--ELLKQDVELIANPRAYLAKIFDGAierwigeqydheyhETWLGFQTRVEGALHGLcqhI 156
Cdd:TIGR03162  77 REMD----FGDWE---GRSwdEIPEAYPELDAWAADWQHARPPGG--------------ESFADFYQRVSEFLEEL---L 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 491088349  157 DATQPRQAVVFSSGGVISVAVGKVLGLNAKQifALNWSIANASITTL 203
Cdd:TIGR03162 133 KAHEGDNVLIVTHGGVIRALLAHLLGLPLEQ--WWSFAVEYGSITLI 177
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-61 1.20e-05

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 44.72  E-value: 1.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491088349   1 MTTIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFFKHTLKEHplVLAGSMQRHQQTAQL 61
Cdd:PRK03482   1 MLQVYLVRHGETQWNAERRIQgqsdspLTAKGEQQAMQVAERAKELGITH--IISSDLGRTRRTAEI 65
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
1-216 3.68e-34

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 121.20  E-value: 3.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   1 MTTIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFfkhtLKEHPL--VLAGSMQRHQQTAQLALAQSfdDAPI 72
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQgrldvpLTELGRAQARALAER----LADIPFdaVYSSPLQRARQTAEALAEAL--GLPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349  73 HTESAWNEFDhqqvfakyderFNQPELLkqdvelianPRAYLAKIFDGAIERWIGEQYDHEYH--ETWLGFQTRVEGALH 150
Cdd:COG0406   75 EVDPRLREID-----------FGDWEGL---------TFAELEARYPEALAAWLADPAEFRPPggESLADVQARVRAALE 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491088349 151 GLcqhIDATQPRQAVVFSSGGVISVAVGKVLGLNAKQIFalNWSIANASITTLRWTDGRLQLLSFN 216
Cdd:COG0406  135 EL---LARHPGGTVLVVTHGGVIRALLAHLLGLPLEAFW--RLRIDNASVTVLEFDDGRWRLVALN 195
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 4-217 5.72e-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: 89.19  E-value: 5.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349    4 IYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFfkhtLKEHPL--VLAGSMQRHQQTAQLALAQSfdDAPIHTE 75
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQgrtdspLTELGREQAEALAER----LAGEPFdaIYSSPLKRARQTAEIIAEAL--GLPVEID 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   76 SAWNEFDhqqvFAKYDERfnqpellkqdvelianPRAYLAKIFDGAIERWIGEQYDHEYH--ETWLGFQTRVEGALHGLC 153
Cdd:pfam00300  75 PRLREID----FGDWEGL----------------TFEEIAERYPEEYDAWLADPADYRPPggESLADVRARVRAALEELA 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491088349  154 QhidATQPRQAVVFSSGGVISVAVGKVLGLNAKQIFalNWSIANASITTLRWTDGRLQLLSFNE 217
Cdd:pfam00300 135 A---RHPGKTVLVVSHGGVIRALLAHLLGLPLEALR--RFPLDNASLSILEFDGGGWVLVLLND 193
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 3-176 9.52e-13

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: 63.63  E-value: 9.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349     3 TIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFFKHTLKEHP-LVLAGSMQRHQQTAQLALAQSFDDapihte 75
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYgdtdvpLTELGRAQAEALGRLLASLLLPRFdVVYSSPLKRARQTAEALAIALGLP------ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349    76 sAWNEFDhqqvFAKYDERfnqpellkqdvelianPRAYLAKIFDGAIERWIGEQYDHEYH-----ETWLGFQTRVEGALH 150
Cdd:smart00855  75 -GLRERD----FGAWEGL----------------TWDEIAAKYPEEYLAAWRDPYDPAPPappggESLADLVERVEPALD 133

                          170       180
                   ....*....|....*....|....*.
gi 491088349   151 GLCQHiDATQPRQAVVFSSGGVISVA 176
Cdd:smart00855 134 ELIAT-ADASGQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 3-80 3.04e-12

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: 62.34  E-value: 3.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   3 TIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFFKHTLKEHPLVLAGSMQRHQQTAQLaLAQSFDDAPIHTES 76
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQgwtdvpLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEI-ILEELPGLPVEVDP 79


                 ....
gi 491088349  77 AWNE 80
Cdd:cd07067   80 RLRE 83
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 3-77 4.75e-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: 61.66  E-value: 4.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   3 TIYLVRHGQAS------FGAASYDQLSAKGEQQAQVVGDFFKHTLKEHPLVLAGSMQRHQQTAQLALAQSFDDAPIHTES 76
Cdd:cd07040    1 VLYLVRHGEREpnaegrFTGWGDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEVDP 80


                 .
gi 491088349  77 A 77
Cdd:cd07040   81 R 81
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
4-88 2.05e-08

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 51.80  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   4 IYLVRHGQASFGAASYD----QLSAKGEQQAQVVGDFFKHTLKEHPLVLAGSMQRHQQTAQLALAQSFDDAPIHTESAWN 79
Cdd:COG2062    1 LILVRHAKAEWRAPGGDdfdrPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAEALGLPPKVEVEDELY 80


                 ....*....
gi 491088349  80 EFDHQQVFA 88
Cdd:COG2062   81 DADPEDLLD 89
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 4-203 5.36e-07

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: 48.00  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349    4 IYLVRHGQ-ASFGAASYDQ----LSAKGEQQAQVVGDFFKHTLKEhpLVLAGSMQRHQQTAQLALAQsfDDAPIHTESAW 78
Cdd:TIGR03162   1 LYLIRHGEtDVNAGLCYGQtdvpLAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILAER--RGLPIIKDDRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   79 NEFDhqqvFAKYDerfNQP--ELLKQDVELIANPRAYLAKIFDGAierwigeqydheyhETWLGFQTRVEGALHGLcqhI 156
Cdd:TIGR03162  77 REMD----FGDWE---GRSwdEIPEAYPELDAWAADWQHARPPGG--------------ESFADFYQRVSEFLEEL---L 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 491088349  157 DATQPRQAVVFSSGGVISVAVGKVLGLNAKQifALNWSIANASITTL 203
Cdd:TIGR03162 133 KAHEGDNVLIVTHGGVIRALLAHLLGLPLEQ--WWSFAVEYGSITLI 177
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 4-71 9.72e-06

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 44.06  E-value: 9.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349    4 IYLVRHGQASFGAAS--YDQLSAKGEQQAQVVGDFFKHTLKEHPLVLAGSMQRHQQTAQLaLAQSFDDAP 71
Cdd:TIGR00249   3 LFIMRHGDAALDAASdsVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEI-VGDCLNLPS 71
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
1-61 1.20e-05

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 44.72  E-value: 1.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491088349   1 MTTIYLVRHGQASFGAASYDQ------LSAKGEQQAQVVGDFFKHTLKEHplVLAGSMQRHQQTAQL 61
Cdd:PRK03482   1 MLQVYLVRHGETQWNAERRIQgqsdspLTAKGEQQAMQVAERAKELGITH--IISSDLGRTRRTAEI 65
PTZ00122 PTZ00122
phosphoglycerate mutase; Provisional
 4-107 2.86e-04

phosphoglycerate mutase; Provisional


Pssm-ID: 240279  Cd Length: 299  Bit Score: 40.94  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   4 IYLVRHGQASFGAASYDQ---LSAKGEQQAQVVGDFFKHTLKE-----HPLVLAGS-MQRHQQTAQLALaQSFDDAPIHT 74
Cdd:PTZ00122 105 IILVRHGQYINESSNDDNikrLTELGKEQARITGKYLKEQFGEilvdkKVKAIYHSdMTRAKETAEIIS-EAFPGVRLIE 183

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491088349  75 ESAWNE--------------FDHQQ----------VFAKYderFNQPELLKQDVELI 107
Cdd:PTZ00122 184 DPNLAEgvpcapdppsrgfkPTIEEiledmkrieaAFEKY---FHRPVEDEDSVEII 237
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
4-75 4.41e-03

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 36.95  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491088349   4 IYLVRHGQAS------FGAASYDQLSAKGEQQAQVVGdffkHTLKEHP--LVLAGSMQRHQQTAQLALAQSFDDAPIHTE 75
Cdd:PRK15004   3 LWLVRHGETQanvdglYSGHAPTPLTARGIEQAQNLH----TLLRDVPfdLVLCSELERAQHTARLVLSDRQLPVHIIPE 78
 
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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