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Conserved domains on  [gi|161078566|ref|NP_001097896|]
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ecdysteroid phosphate phosphatase, isoform B [Drosophila melanogaster]

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];
53-289 1.28e-21

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


:

Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 90.39  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  53 RKIYIMRHGErvdftfgtwipycfdefgnymrkdlnmpkTLPRRKNSPEGWQnDSPLTNVGVYQANLIGQALleAQVQID 132
Cdd:COG0406    2 TRLYLVRHGE-----------------------------TEWNAEGRLQGRL-DVPLTELGRAQARALAERL--ADIPFD 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 133 HVYCSPSYRCIQTCTSALEGLKLTgkqkIKLEPGLFEWmawypsGVPDW--LTKNELTEAKFDVDLDYEpvqpASELTAR 210
Cdd:COG0406   50 AVYSSPLQRARQTAEALAEALGLP----VEVDPRLREI------DFGDWegLTFAELEARYPEALAAWL----ADPAEFR 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 211 LK--ESTEQFYERNHDVILQLLEQTTG-NILVVAHATTLDTCSRQLTGGVPRSTNELRqvihkIPYCSLATVEQVDGVWK 287
Cdd:COG0406  116 PPggESLADVQARVRAALEELLARHPGgTVLVVTHGGVIRALLAHLLGLPLEAFWRLR-----IDNASVTVLEFDDGRWR 190

                 ..
gi 161078566 288 LV 289
Cdd:COG0406  191 LV 192
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
53-289 1.28e-21

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 90.39  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  53 RKIYIMRHGErvdftfgtwipycfdefgnymrkdlnmpkTLPRRKNSPEGWQnDSPLTNVGVYQANLIGQALleAQVQID 132
Cdd:COG0406    2 TRLYLVRHGE-----------------------------TEWNAEGRLQGRL-DVPLTELGRAQARALAERL--ADIPFD 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 133 HVYCSPSYRCIQTCTSALEGLKLTgkqkIKLEPGLFEWmawypsGVPDW--LTKNELTEAKFDVDLDYEpvqpASELTAR 210
Cdd:COG0406   50 AVYSSPLQRARQTAEALAEALGLP----VEVDPRLREI------DFGDWegLTFAELEARYPEALAAWL----ADPAEFR 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 211 LK--ESTEQFYERNHDVILQLLEQTTG-NILVVAHATTLDTCSRQLTGGVPRSTNELRqvihkIPYCSLATVEQVDGVWK 287
Cdd:COG0406  116 PPggESLADVQARVRAALEELLARHPGgTVLVVTHGGVIRALLAHLLGLPLEAFWRLR-----IDNASVTVLEFDDGRWR 190

                 ..
gi 161078566 288 LV 289
Cdd:COG0406  191 LV 192
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
55-289 8.93e-21

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: 88.04  E-value: 8.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566   55 IYIMRHGErvdftfgtwipycfdefgnymrkdlnmpkTLPRRKNSPEGWqNDSPLTNVGVYQANLIGQALleAQVQIDHV 134
Cdd:pfam00300   1 LYLVRHGE-----------------------------TEWNLEGRFQGR-TDSPLTELGREQAEALAERL--AGEPFDAI 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  135 YCSPSYRCIQTCTSALEGLKLTgkqkIKLEPGLFEWMAwypsGVPDWLTKNELTE------AKFDVDLDYEPVQPAselt 208
Cdd:pfam00300  49 YSSPLKRARQTAEIIAEALGLP----VEIDPRLREIDF----GDWEGLTFEEIAErypeeyDAWLADPADYRPPGG---- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  209 arlkESTEQFYERNHDVILQLLEQTTG-NILVVAHATTLDTCSRQLTgGVPRStnELRQviHKIPYCSLATVEQVDGVWK 287
Cdd:pfam00300 117 ----ESLADVRARVRAALEELAARHPGkTVLVVSHGGVIRALLAHLL-GLPLE--ALRR--FPLDNASLSILEFDGGGWV 187

                  ..
gi 161078566  288 LV 289
Cdd:pfam00300 188 LV 189
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
54-280 1.77e-19

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 83.14  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  54 KIYIMRHGERVDftfgtwipycfdefgnymrkdlnmpktlpRRKNSPEGWqNDSPLTNVGVYQANLIGQALLEAQVQIDH 133
Cdd:cd07067    1 RLYLVRHGESEW-----------------------------NAEGRFQGW-TDVPLTEKGREQARALGKRLKELGIKFDR 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 134 VYCSPSYRCIQTCTSALEGLkltGKQKIKLEPGLFEwmawypsgvpdwltknelteakfdvdldyepvqpaseltarlke 213
Cdd:cd07067   51 IYSSPLKRAIQTAEIILEEL---PGLPVEVDPRLRE-------------------------------------------- 83
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161078566 214 steqfyERNHDVILQLLEQTTG-NILVVAHATTLDTCSRQLTGGVPRSTNELRqvihkIPYCSLATVE 280
Cdd:cd07067   84 ------ARVLPALEELIAPHDGkNVLIVSHGGVLRALLAYLLGLSDEDILRLN-----LPNGSISVLE 140
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
54-246 2.91e-14

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: 69.03  E-value: 2.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566    54 KIYIMRHGErvdftfgtwipycfdefgnymrkdlnmpkTLPRRKNSPEGWqNDSPLTNVGVYQANLIGQALLEA-QVQID 132
Cdd:smart00855   1 RLYLIRHGE-----------------------------TEWNREGRLYGD-TDVPLTELGRAQAEALGRLLASLlLPRFD 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566   133 HVYCSPSYRCIQTCTSALEGLKLtgkqkiklePGLFEWmawypsGVPDW--LTKNELTEAKFDVDLDY-EPVQPASELTA 209
Cdd:smart00855  51 VVYSSPLKRARQTAEALAIALGL---------PGLRER------DFGAWegLTWDEIAAKYPEEYLAAwRDPYDPAPPAP 115
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 161078566   210 RLKESTEQFYERNHDVILQLLE---QTTGNILVVAHATTL 246
Cdd:smart00855 116 PGGESLADLVERVEPALDELIAtadASGQNVLIVSHGGVI 155
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
104-243 4.69e-06

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: 46.08  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  104 QNDSPLTNVGVYQANLIGQALleAQVQIDHVYCSPSYRCIQTCTSALEGLKLtgkqKIKLEPGLFEwMAWypsGvpDW-- 181
Cdd:TIGR03162  19 QTDVPLAESGEEQAAALREKL--ADVPFDAVYSSPLSRCRELAEILAERRGL----PIIKDDRLRE-MDF---G--DWeg 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161078566  182 LTKNELTEAKFDVDLDYEPVQpaselTARL--KESTEQFYERNHDVILQLLE-QTTGNILVVAHA 243
Cdd:TIGR03162  87 RSWDEIPEAYPELDAWAADWQ-----HARPpgGESFADFYQRVSEFLEELLKaHEGDNVLIVTHG 146
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
96-153 7.52e-05

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 43.11  E-value: 7.52e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161078566  96 RKNSPEGWQnDSPLTNVGVYQANLIGQALLEAQVQIDHVYCSPSYRCIQTCTSALEGL 153
Cdd:PTZ00123   3 KENRFTGWT-DVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAWIVLEEL 59
 
Name Accession Description Interval E-value
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
53-289 1.28e-21

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 90.39  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  53 RKIYIMRHGErvdftfgtwipycfdefgnymrkdlnmpkTLPRRKNSPEGWQnDSPLTNVGVYQANLIGQALleAQVQID 132
Cdd:COG0406    2 TRLYLVRHGE-----------------------------TEWNAEGRLQGRL-DVPLTELGRAQARALAERL--ADIPFD 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 133 HVYCSPSYRCIQTCTSALEGLKLTgkqkIKLEPGLFEWmawypsGVPDW--LTKNELTEAKFDVDLDYEpvqpASELTAR 210
Cdd:COG0406   50 AVYSSPLQRARQTAEALAEALGLP----VEVDPRLREI------DFGDWegLTFAELEARYPEALAAWL----ADPAEFR 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 211 LK--ESTEQFYERNHDVILQLLEQTTG-NILVVAHATTLDTCSRQLTGGVPRSTNELRqvihkIPYCSLATVEQVDGVWK 287
Cdd:COG0406  116 PPggESLADVQARVRAALEELLARHPGgTVLVVTHGGVIRALLAHLLGLPLEAFWRLR-----IDNASVTVLEFDDGRWR 190

                 ..
gi 161078566 288 LV 289
Cdd:COG0406  191 LV 192
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
55-289 8.93e-21

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: 88.04  E-value: 8.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566   55 IYIMRHGErvdftfgtwipycfdefgnymrkdlnmpkTLPRRKNSPEGWqNDSPLTNVGVYQANLIGQALleAQVQIDHV 134
Cdd:pfam00300   1 LYLVRHGE-----------------------------TEWNLEGRFQGR-TDSPLTELGREQAEALAERL--AGEPFDAI 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  135 YCSPSYRCIQTCTSALEGLKLTgkqkIKLEPGLFEWMAwypsGVPDWLTKNELTE------AKFDVDLDYEPVQPAselt 208
Cdd:pfam00300  49 YSSPLKRARQTAEIIAEALGLP----VEIDPRLREIDF----GDWEGLTFEEIAErypeeyDAWLADPADYRPPGG---- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  209 arlkESTEQFYERNHDVILQLLEQTTG-NILVVAHATTLDTCSRQLTgGVPRStnELRQviHKIPYCSLATVEQVDGVWK 287
Cdd:pfam00300 117 ----ESLADVRARVRAALEELAARHPGkTVLVVSHGGVIRALLAHLL-GLPLE--ALRR--FPLDNASLSILEFDGGGWV 187

                  ..
gi 161078566  288 LV 289
Cdd:pfam00300 188 LV 189
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
54-280 1.77e-19

Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Subgroup of the catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This subgroup contains cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example, F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG.


Pssm-ID: 132718 [Multi-domain]  Cd Length: 153  Bit Score: 83.14  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  54 KIYIMRHGERVDftfgtwipycfdefgnymrkdlnmpktlpRRKNSPEGWqNDSPLTNVGVYQANLIGQALLEAQVQIDH 133
Cdd:cd07067    1 RLYLVRHGESEW-----------------------------NAEGRFQGW-TDVPLTEKGREQARALGKRLKELGIKFDR 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 134 VYCSPSYRCIQTCTSALEGLkltGKQKIKLEPGLFEwmawypsgvpdwltknelteakfdvdldyepvqpaseltarlke 213
Cdd:cd07067   51 IYSSPLKRAIQTAEIILEEL---PGLPVEVDPRLRE-------------------------------------------- 83
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161078566 214 steqfyERNHDVILQLLEQTTG-NILVVAHATTLDTCSRQLTGGVPRSTNELRqvihkIPYCSLATVE 280
Cdd:cd07067   84 ------ARVLPALEELIAPHDGkNVLIVSHGGVLRALLAYLLGLSDEDILRLN-----LPNGSISVLE 140
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
54-280 4.43e-15

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: 71.29  E-value: 4.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  54 KIYIMRHGERVdftfgtwipycfdefgnymrkdlnmpktlPRRKNSPEGWqNDSPLTNVGVYQANLIGQALLEAQVQIDH 133
Cdd:cd07040    1 VLYLVRHGERE-----------------------------PNAEGRFTGW-GDGPLTEKGRQQARELGKALRERYIKFDR 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 134 VYCSPSYRCIQTCTSALEGLKLtgKQKIKLEPGlfewmawypsgvpdwltknelteakfdvdldyepvqpaseltarlke 213
Cdd:cd07040   51 IYSSPLKRAIQTAEIILEGLFE--GLPVEVDPR----------------------------------------------- 81
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 214 steqfyERNHDVILQLLEQTT---GNILVVAHATTLDTCSRQLTGGvprstNELRQVIHKIPYCSLATVE 280
Cdd:cd07040   82 ------ARVLNALLELLARHLldgKNVLIVSHGGTIRALLAALLGL-----SDEEILSLNLPNGSILVLE 140
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
54-246 2.91e-14

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: 69.03  E-value: 2.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566    54 KIYIMRHGErvdftfgtwipycfdefgnymrkdlnmpkTLPRRKNSPEGWqNDSPLTNVGVYQANLIGQALLEA-QVQID 132
Cdd:smart00855   1 RLYLIRHGE-----------------------------TEWNREGRLYGD-TDVPLTELGRAQAEALGRLLASLlLPRFD 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566   133 HVYCSPSYRCIQTCTSALEGLKLtgkqkiklePGLFEWmawypsGVPDW--LTKNELTEAKFDVDLDY-EPVQPASELTA 209
Cdd:smart00855  51 VVYSSPLKRARQTAEALAIALGL---------PGLRER------DFGAWegLTWDEIAAKYPEEYLAAwRDPYDPAPPAP 115
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 161078566   210 RLKESTEQFYERNHDVILQLLE---QTTGNILVVAHATTL 246
Cdd:smart00855 116 PGGESLADLVERVEPALDELIAtadASGQNVLIVSHGGVI 155
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
55-280 2.35e-10

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 57.96  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  55 IYIMRHGERVDftfgtwipycfdefgnymrkdlnmpktlprrknsPEGWQNDS--PLTNVGVYQANLIGQALLEAQVQID 132
Cdd:COG2062    1 LILVRHAKAEW----------------------------------RAPGGDDFdrPLTERGRRQARAMARWLAALGLKPD 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566 133 HVYCSPSYRCIQTCTSALEGLKLtgKQKIKLEPGLfewmawYPSGVPDWLtknelteakfdvdldyepvqpaseltarlk 212
Cdd:COG2062   47 RILSSPALRARQTAEILAEALGL--PPKVEVEDEL------YDADPEDLL------------------------------ 88
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161078566 213 esteqfyernhDVILQLleQTTGNILVVAHATTLDTCSRQLTGGVPrstnelrqvIHKIPYCSLATVE 280
Cdd:COG2062   89 -----------DLLREL--DDGETVLLVGHNPGLSELAALLAGGEP---------LDGFPTGGLAVLE 134
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
104-243 4.69e-06

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: 46.08  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161078566  104 QNDSPLTNVGVYQANLIGQALleAQVQIDHVYCSPSYRCIQTCTSALEGLKLtgkqKIKLEPGLFEwMAWypsGvpDW-- 181
Cdd:TIGR03162  19 QTDVPLAESGEEQAAALREKL--ADVPFDAVYSSPLSRCRELAEILAERRGL----PIIKDDRLRE-MDF---G--DWeg 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161078566  182 LTKNELTEAKFDVDLDYEPVQpaselTARL--KESTEQFYERNHDVILQLLE-QTTGNILVVAHA 243
Cdd:TIGR03162  87 RSWDEIPEAYPELDAWAADWQ-----HARPpgGESFADFYQRVSEFLEELLKaHEGDNVLIVTHG 146
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
96-153 7.52e-05

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 43.11  E-value: 7.52e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161078566  96 RKNSPEGWQnDSPLTNVGVYQANLIGQALLEAQVQIDHVYCSPSYRCIQTCTSALEGL 153
Cdd:PTZ00123   3 KENRFTGWT-DVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAWIVLEEL 59
 
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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