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Conserved domains on  [gi|855311642|ref|XP_012897562|]
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uncharacterized protein [Blastocystis hominis]

Protein Classification

bifunctional nucleoside/nucleotide kinase/histidine phosphatase family protein( domain architecture ID 10988806)

bifunctional nucleoside/nucleotide kinase (NK)/histidine phosphatase (HP) family protein contains an N-terminal NK domain that may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars, and a C-terminal HP domain that contains a conserved His residue that is transiently phosphorylated during the catalytic cycle; similar to Schizosaccharomyces pombe 6-phosphofructo-2-kinase C222.13c

CATH:  3.40.50.1240|3.40.50.300
EC:  2.7.1.-|3.1.3.-
Gene Ontology:  GO:0016773|GO:0005524|GO:0016791
PubMed:  18092946|14568537
SCOP:  3000781|3002021

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 1-148 2.38e-50

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member pfam01591:

Pssm-ID: 450170  Cd Length: 223  Bit Score: 167.13  E-value: 2.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642    1 MELRAYYASLALEELISFLL-EGGDVALLDATNSNVDRRNYIASRCSSLGFHVLYLESICDDPELIHKNCLSKLQN-PDY 78
Cdd:pfam01591  74 MKIREQCALAALKDVLAYLNeESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSsPDY 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642   79 KDRSPDEALADFYQRLENYKLNYEPLDKERDRESSYIRLFNVGEYIVANHCNGVLESDVVSYLLNTHLVP 148
Cdd:pfam01591 154 KGKPPEEAIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 151-328 3.67e-38

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: 134.64  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  151 IWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDnvTILCDRSLRVAQTVRPLAG----DYNRCTLLR 224
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEIIAEalglPVEIDPRLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  225 ELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVS--CRDNVLIVGHVAVIRILLAYF 302
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAArhPGKTVLVVSHGGVIRALLAHL 158

                         170       180
                  ....*....|....*....|....*.
gi 855311642  303 MDKPIASIPDMEVKMHTVYELDPTAY 328
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGG 184
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 1-148 2.38e-50

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 167.13  E-value: 2.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642    1 MELRAYYASLALEELISFLL-EGGDVALLDATNSNVDRRNYIASRCSSLGFHVLYLESICDDPELIHKNCLSKLQN-PDY 78
Cdd:pfam01591  74 MKIREQCALAALKDVLAYLNeESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSsPDY 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642   79 KDRSPDEALADFYQRLENYKLNYEPLDKERDRESSYIRLFNVGEYIVANHCNGVLESDVVSYLLNTHLVP 148
Cdd:pfam01591 154 KGKPPEEAIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 151-328 3.67e-38

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: 134.64  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  151 IWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDnvTILCDRSLRVAQTVRPLAG----DYNRCTLLR 224
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEIIAEalglPVEIDPRLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  225 ELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVS--CRDNVLIVGHVAVIRILLAYF 302
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAArhPGKTVLVVSHGGVIRALLAHL 158

                         170       180
                  ....*....|....*....|....*.
gi 855311642  303 MDKPIASIPDMEVKMHTVYELDPTAY 328
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGG 184
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
148-324 9.85e-32

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 117.74  E-value: 9.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 148 PRKIWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDnvTILCDRSLRVAQTVRPLAG----DYNRCT 221
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALAEalglPVEVDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 222 LLRELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVSCRD--NVLIVGHVAVIRILL 299
Cdd:COG0406   79 RLREIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARHPggTVLVVTHGGVIRALL 158

                        170       180
                 ....*....|....*....|....*
gi 855311642 300 AYFMDKPIASIPDMEVKMHTVYELD 324
Cdd:COG0406  159 AHLLGLPLEAFWRLRIDNASVTVLE 183
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 150-298 3.79e-26

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: 101.77  E-value: 3.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642   150 KIWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDNVT-ILCDRSLRVAQTVRPLAGDYNRCtLLREL 226
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLASLLLPRFDvVYSSPLKRARQTAEALAIALGLP-GLRER 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 855311642   227 NGGDYARMTYQEIKERYPEEYMKRKRNKLEYRY---PDGESYLDVKDRLSPVIMKIVS----CRDNVLIVGHVAVIRIL 298
Cdd:smart00855  80 DFGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPpapPGGESLADLVERVEPALDELIAtadaSGQNVLIVSHGGVIRAL 158
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 151-317 4.70e-22

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: 91.14  E-value: 4.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  151 IWLCIHGETDfTRRGILGG--DPPLNQNGAEFARKLHDfiRSRGKDNVTILCDRSLRVAQTVRPLAGDY----NRCTLLR 224
Cdd:TIGR03162   1 LYLIRHGETD-VNAGLCYGqtDVPLAESGEEQAAALRE--KLADVPFDAVYSSPLSRCRELAEILAERRglpiIKDDRLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  225 ELNGGDYARMTYQEIKERYPEeYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVSCR--DNVLIVGHVAVIRILLAYF 302
Cdd:TIGR03162  78 EMDFGDWEGRSWDEIPEAYPE-LDAWAADWQHARPPGGESFADFYQRVSEFLEELLKAHegDNVLIVTHGGVIRALLAHL 156

                         170
                  ....*....|....*
gi 855311642  303 MDKPIASIPDMEVKM 317
Cdd:TIGR03162 157 LGLPLEQWWSFAVEY 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1-305 2.02e-17

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 83.02  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642   1 MELRAyyASLALEELISFLLEGGDVALLDATNSNVDRRNYIASRCSSLGF----HVLYLESICDDPELIHKNCL-SKLQN 75
Cdd:PTZ00322 274 VEFRI--AKAIAHDMTTFICKTDGVAVLDGTNTTHARRMALLRAIRETGLirmtRVVFVEVVNNNSETIRRNVLrAKEMF 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  76 PDYKDRSPDEaladFYQRLENYKLNYEPLDKERDRESSYIRLFNvGEYIVANHCNGVLESDVVSYLLNTHLVPRKIWLCI 155
Cdd:PTZ00322 352 PGAPEDFVDR----YYEVIEQLEAVYKSLNPVTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTR 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 156 HGETDFTRRGILGGDPPLNQNGAEFARKLHD-FIRSRGKDNVTILCDRSLRVAQTVRPLA-------GDYN--------- 218
Cdd:PTZ00322 427 AGEYVDLLSGRIGGNSRLTERGRAYSRALFEyFQKEISTTSFTVMSSCAKRCTETVHYFAeesilqqSTASaassqspsl 506

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 219 RCTL-----LRELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDV-KDRLSPVIMKIVSCRDNVLIVGHV 292
Cdd:PTZ00322 507 NCRVlyfptLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGECIHQVfNARLEPHIHDIQASTTPVLVVSHL 586

                        330
                 ....*....|...
gi 855311642 293 AVIRILLAYFMDK 305
Cdd:PTZ00322 587 HLLQGLYSYFVTD 599
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 150-325 7.45e-16

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: 73.90  E-value: 7.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 150 KIWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDNVTILCDRSLRVAQTVRPLAGDYNRCTLLREln 227
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVD-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 228 ggdyarmtyQEIKErypeeymkrkrnkleyrypdgesyldvkDRLSPVIMKIVSCRD--NVLIVGHVAVIRILLAYFMDK 305
Cdd:cd07067   79 ---------PRLRE----------------------------ARVLPALEELIAPHDgkNVLIVSHGGVLRALLAYLLGL 121

                        170       180
                 ....*....|....*....|..
gi 855311642 306 PIASIPDMEVKMH--TVYELDP 325
Cdd:cd07067  122 SDEDILRLNLPNGsiSVLELDE 143
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 1-148 2.38e-50

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 167.13  E-value: 2.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642    1 MELRAYYASLALEELISFLL-EGGDVALLDATNSNVDRRNYIASRCSSLGFHVLYLESICDDPELIHKNCLSKLQN-PDY 78
Cdd:pfam01591  74 MKIREQCALAALKDVLAYLNeESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSsPDY 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642   79 KDRSPDEALADFYQRLENYKLNYEPLDKERDRESSYIRLFNVGEYIVANHCNGVLESDVVSYLLNTHLVP 148
Cdd:pfam01591 154 KGKPPEEAIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 151-328 3.67e-38

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: 134.64  E-value: 3.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  151 IWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDnvTILCDRSLRVAQTVRPLAG----DYNRCTLLR 224
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEIIAEalglPVEIDPRLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  225 ELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVS--CRDNVLIVGHVAVIRILLAYF 302
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAArhPGKTVLVVSHGGVIRALLAHL 158

                         170       180
                  ....*....|....*....|....*.
gi 855311642  303 MDKPIASIPDMEVKMHTVYELDPTAY 328
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGG 184
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
148-324 9.85e-32

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 117.74  E-value: 9.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 148 PRKIWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDnvTILCDRSLRVAQTVRPLAG----DYNRCT 221
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALAEalglPVEVDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 222 LLRELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVSCRD--NVLIVGHVAVIRILL 299
Cdd:COG0406   79 RLREIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARHPggTVLVVTHGGVIRALL 158

                        170       180
                 ....*....|....*....|....*
gi 855311642 300 AYFMDKPIASIPDMEVKMHTVYELD 324
Cdd:COG0406  159 AHLLGLPLEAFWRLRIDNASVTVLE 183
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 150-298 3.79e-26

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: 101.77  E-value: 3.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642   150 KIWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDNVT-ILCDRSLRVAQTVRPLAGDYNRCtLLREL 226
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLASLLLPRFDvVYSSPLKRARQTAEALAIALGLP-GLRER 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 855311642   227 NGGDYARMTYQEIKERYPEEYMKRKRNKLEYRY---PDGESYLDVKDRLSPVIMKIVS----CRDNVLIVGHVAVIRIL 298
Cdd:smart00855  80 DFGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPpapPGGESLADLVERVEPALDELIAtadaSGQNVLIVSHGGVIRAL 158
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 151-317 4.70e-22

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: 91.14  E-value: 4.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  151 IWLCIHGETDfTRRGILGG--DPPLNQNGAEFARKLHDfiRSRGKDNVTILCDRSLRVAQTVRPLAGDY----NRCTLLR 224
Cdd:TIGR03162   1 LYLIRHGETD-VNAGLCYGqtDVPLAESGEEQAAALRE--KLADVPFDAVYSSPLSRCRELAEILAERRglpiIKDDRLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  225 ELNGGDYARMTYQEIKERYPEeYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVSCR--DNVLIVGHVAVIRILLAYF 302
Cdd:TIGR03162  78 EMDFGDWEGRSWDEIPEAYPE-LDAWAADWQHARPPGGESFADFYQRVSEFLEELLKAHegDNVLIVTHGGVIRALLAHL 156

                         170
                  ....*....|....*
gi 855311642  303 MDKPIASIPDMEVKM 317
Cdd:TIGR03162 157 LGLPLEQWWSFAVEY 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1-305 2.02e-17

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 83.02  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642   1 MELRAyyASLALEELISFLLEGGDVALLDATNSNVDRRNYIASRCSSLGF----HVLYLESICDDPELIHKNCL-SKLQN 75
Cdd:PTZ00322 274 VEFRI--AKAIAHDMTTFICKTDGVAVLDGTNTTHARRMALLRAIRETGLirmtRVVFVEVVNNNSETIRRNVLrAKEMF 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642  76 PDYKDRSPDEaladFYQRLENYKLNYEPLDKERDRESSYIRLFNvGEYIVANHCNGVLESDVVSYLLNTHLVPRKIWLCI 155
Cdd:PTZ00322 352 PGAPEDFVDR----YYEVIEQLEAVYKSLNPVTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTR 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 156 HGETDFTRRGILGGDPPLNQNGAEFARKLHD-FIRSRGKDNVTILCDRSLRVAQTVRPLA-------GDYN--------- 218
Cdd:PTZ00322 427 AGEYVDLLSGRIGGNSRLTERGRAYSRALFEyFQKEISTTSFTVMSSCAKRCTETVHYFAeesilqqSTASaassqspsl 506

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 219 RCTL-----LRELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDV-KDRLSPVIMKIVSCRDNVLIVGHV 292
Cdd:PTZ00322 507 NCRVlyfptLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGECIHQVfNARLEPHIHDIQASTTPVLVVSHL 586

                        330
                 ....*....|...
gi 855311642 293 AVIRILLAYFMDK 305
Cdd:PTZ00322 587 HLLQGLYSYFVTD 599
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 150-325 7.45e-16

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: 73.90  E-value: 7.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 150 KIWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDNVTILCDRSLRVAQTVRPLAGDYNRCTLLREln 227
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILEELPGLPVEVD-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 228 ggdyarmtyQEIKErypeeymkrkrnkleyrypdgesyldvkDRLSPVIMKIVSCRD--NVLIVGHVAVIRILLAYFMDK 305
Cdd:cd07067   79 ---------PRLRE----------------------------ARVLPALEELIAPHDgkNVLIVSHGGVLRALLAYLLGL 121

                        170       180
                 ....*....|....*....|..
gi 855311642 306 PIASIPDMEVKMH--TVYELDP 325
Cdd:cd07067  122 SDEDILRLNLPNGsiSVLELDE 143
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 150-325 1.07e-13

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: 67.82  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 150 KIWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDNVTILCDRSLRVAQTVRPLagdynrctllreln 227
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTGwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEII-------------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 228 ggdyarmtyqeikerypeeymkrkrnkLEYRYPDGESYLDVKDRLSPVIMKIV----SCRDNVLIVGHVAVIRILLAYFM 303
Cdd:cd07040   67 ---------------------------LEGLFEGLPVEVDPRARVLNALLELLarhlLDGKNVLIVSHGGTIRALLAALL 119

                        170       180
                 ....*....|....*....|....
gi 855311642 304 DKPIASIPDMEVKMH--TVYELDP 325
Cdd:cd07040  120 GLSDEEILSLNLPNGsiLVLELDE 143
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
150-310 6.61e-13

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 66.61  E-value: 6.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 150 KIWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDNVtiLCDRSLRVAQTVRPLAGD----YNRCTLL 223
Cdd:PRK15004   2 RLWLVRHGETQANVDGLYSGhaPTPLTARGIEQAQNLHTLLRDVPFDLV--LCSELERAQHTARLVLSDrqlpVHIIPEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 224 RELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVSCR--DNVLIVGHVAVIRILLAY 301
Cdd:PRK15004  80 NEMFFGDWEMRHHRDLMQEDAENYAAWCNDWQHAIPTNGEGFQAFSQRVERFIARLSAFQhyQNLLIVSHQGVLSLLIAR 159


                 ....*....
gi 855311642 302 FMDKPIASI 310
Cdd:PRK15004 160 LLGMPAEAM 168
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 148-318 1.81e-09

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 58.45  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 148 PRKIWLCIHGETDFT--RRGILGGDPPLNQNGAEFARKLHDFIRSRGKDNVtILCD---RSLRVAQTV-RPLAGDYNRCT 221
Cdd:PRK07238 171 PTRLLLLRHGQTELSvqRRYSGRGNPELTEVGRRQAAAAARYLAARGGIDA-VVSSplqRARDTAAAAaKALGLDVTVDD 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 222 LLRELNGGDYARMTYQEIKERYPEEyMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVS--CRDNVLIVGHVAVIRILL 299
Cdd:PRK07238 250 DLIETDFGAWEGLTFAEAAERDPEL-HRAWLADTSVAPPGGESFDAVARRVRRARDRLIAeyPGATVLVVSHVTPIKTLL 328

                        170
                 ....*....|....*....
gi 855311642 300 AYFMDKPiasiPDMEVKMH 318
Cdd:PRK07238 329 RLALDAG----PGVLYRLH 343
PRK13463 PRK13463
phosphoserine phosphatase 1;
151-324 8.60e-04

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 40.03  E-value: 8.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 151 IWLCIHGETDFTRRGILGG--DPPLNQNGAEFARKLHDFIRSRGKDNV-TILCDRSLRVAQTVR-----PLAGDYNrctl 222
Cdd:PRK13463   5 VYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLGERMKDLSIHAIySSPSERTLHTAELIKgerdiPIIADEH---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 855311642 223 LRELNGGDYARMTYQEIKERYPEEYMKRKRNKLEYRYPDGESYLDVKDRLSPVIMKIVSCR--DNVLIVGHVAVIRILLA 300
Cdd:PRK13463  81 FYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRVIEGMQLLLEKHkgESILIVSHAAAAKLLVG 160

                        170       180
                 ....*....|....*....|....*..
gi 855311642 301 YFMDKPIASI---PDMEVKMHTVYELD 324
Cdd:PRK13463 161 HFAGIEIENVwddPFMHSASLSIIEFE 187
 
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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