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Conserved domains on  [gi|64762445|ref|NP_001018063|]
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 isoform b [Homo sapiens]

Protein Classification

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase( domain architecture ID 11122785)

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase catalyzes synthesis and degradation of fructose 2,6-bisphosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
26-249 3.94e-135

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: 388.23  E-value: 3.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445    26 KKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQC 105
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   106 ALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNREN 185
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 64762445   186 VMEDFLKRIECYKVTYRPLDpDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQP 249
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
252-435 1.73e-54

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: 180.48  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   252 IYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILN 325
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   326 EIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYF 402
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 64762445   403 LDKGADELPYLRCPLHTIFKLTPVAYGCKVETI 435
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLL 191
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
26-249 3.94e-135

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: 388.23  E-value: 3.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445    26 KKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQC 105
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   106 ALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNREN 185
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 64762445   186 VMEDFLKRIECYKVTYRPLDpDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQP 249
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
252-435 1.73e-54

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: 180.48  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   252 IYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILN 325
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   326 EIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYF 402
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 64762445   403 LDKGADELPYLRCPLHTIFKLTPVAYGCKVETI 435
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLL 191
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
40-446 1.40e-47

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 173.93  E-value: 1.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   40 LIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCAlvalEDVKAYLTE 119
Cdd:PTZ00322 217 IVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRLERRGGAVSSPTGAAEVEFRIAKAIA----HDMTTFICK 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  120 ENGqIAVFDATNTTRERRDMILNFAEQ----NSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERnrenVMEDFLKRIE 195
Cdd:PTZ00322 293 TDG-VAVLDGTNTTHARRMALLRAIREtgliRMTRVVFVEVVNNNSETIRRNVLRAKEMFPGAPED----FVDRYYEVIE 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  196 CYKVTYRPLDPDNyDKDLSFIKVINvGQRFLVNRVQDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLS 275
Cdd:PTZ00322 368 QLEAVYKSLNPVT-DCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLT 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  276 VRGKQFAQAL-RKFLEEQEITDLKVWTSQLKRTIQTAE---------------------SLGVPYEQWKILNEIDAGVCE 333
Cdd:PTZ00322 446 ERGRAYSRALfEYFQKEISTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYFPTLDDINHGDCE 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  334 EMTYAEIEKRYPEEFALRDQEKYLYRYPGGE-SYQDLVQRLEPVIMELERQGN-VLVISHQAVMRCLLAYFLDKGADELP 411
Cdd:PTZ00322 526 GQLLSDVRRTMPNTLQSMKADPYYTAWPNGEcIHQVFNARLEPHIHDIQASTTpVLVVSHLHLLQGLYSYFVTDGDNIVA 605
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 64762445  412 -----YLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHR 446
Cdd:PTZ00322 606 pqnayKIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQ 645
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
249-416 1.95e-46

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 159.72  E-value: 1.95e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 249 PRTIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWK 322
Cdd:COG0406   1 MTRLYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEalaeALGLPVEVDP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 323 ILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLL 399
Cdd:COG0406  79 RLREIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARhpgGTVLVVTHGGVIRALL 158
                       170
                ....*....|....*..
gi 64762445 400 AYFLDKGADELPYLRCP 416
Cdd:COG0406 159 AHLLGLPLEAFWRLRID 175
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
251-398 3.47e-41

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: 144.53  E-value: 3.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445    251 TIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFL-EEQEITDLKVWTSQLKRTIQTAESLGVPYEQWkILNEI 327
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLP-GLRER 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 64762445    328 DAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRY---PGGESYQDLVQRLEPVIMELERQ-----GNVLVISHQAVMRCL 398
Cdd:smart00855  80 DFGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPpapPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
251-437 1.15e-34

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: 126.67  E-value: 1.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 251 TIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESL-----GVPYEQWKI 323
Cdd:cd07067   1 RLYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIIleelpGLPVEVDPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 324 LNEidagvceemtyaeiekrypeefalrdqekylyrypggesyqdlvQRLEPVIMELERQ---GNVLVISHQAVMRCLLA 400
Cdd:cd07067  81 LRE--------------------------------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLA 116
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 64762445 401 YFLDKGADELPYLRCPLHTIFKLTPVAYGCKVETIKL 437
Cdd:cd07067 117 YLLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
252-430 3.32e-30

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: 115.41  E-value: 3.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   252 IYLCRHGESEFNLLGKIG-GDSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAESLGVPyEQWKI-----LN 325
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILAER-RGLPIikddrLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   326 EIDAGVCEEMTYAEIEKRYPEefalrdQEKYL-----YRYPGGESYQDLVQRLEPV---IMELERQGNVLVISHQAVMRC 397
Cdd:TIGR03162  78 EMDFGDWEGRSWDEIPEAYPE------LDAWAadwqhARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRA 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 64762445   398 LLAYFLDKGADELPYLrcplhtifkltPVAYGC 430
Cdd:TIGR03162 152 LLAHLLGLPLEQWWSF-----------AVEYGS 173
PRK13463 PRK13463
phosphoserine phosphatase 1;
251-402 2.34e-17

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 80.48  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  251 TIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAESL----GVPYEQWKIL 324
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLGERMKDLSIH--AIYSSPSERTLHTAELIkgerDIPIIADEHF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  325 NEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQR-LEPVIMELERQG--NVLVISHQAVMRCLLAY 401
Cdd:PRK13463  82 YEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHKgeSILIVSHAAAAKLLVGH 161

                 .
gi 64762445  402 F 402
Cdd:PRK13463 162 F 162
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
40-207 1.19e-08

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 54.15  E-value: 1.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  40 LIVMIGLPARGKTYVSKKLTRYLNWIgvptkvfnlgVYRREAVKSY---KSYDFFRHDNEEAMKIRKQCALVALEDVKAy 116
Cdd:COG0645   1 LILVCGLPGSGKSTLARALAERLGAV----------RLRSDVVRKRlfgAGLAPLERSPEATARTYARLLALARELLAA- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 117 lteenGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVEsvCD-DPDVIAANILevkvsspdypERNRENVMEDF-LKRI 194
Cdd:COG0645  70 -----GRSVILDATFLRRAQREAFRALAEEAGAPFVLIW--LDaPEEVLRERLE----------ARNAEGGDSDAtWEVL 132
                       170
                ....*....|...
gi 64762445 195 ECYKVTYRPLDPD 207
Cdd:COG0645 133 ERQLAFEEPLTED 145
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
26-249 3.94e-135

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: 388.23  E-value: 3.94e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445    26 KKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQC 105
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   106 ALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNREN 185
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 64762445   186 VMEDFLKRIECYKVTYRPLDpDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQP 249
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
252-435 1.73e-54

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: 180.48  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   252 IYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILN 325
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   326 EIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLLAYF 402
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 64762445   403 LDKGADELPYLRCPLHTIFKLTPVAYGCKVETI 435
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLL 191
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
40-446 1.40e-47

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 173.93  E-value: 1.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   40 LIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCAlvalEDVKAYLTE 119
Cdd:PTZ00322 217 IVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRLERRGGAVSSPTGAAEVEFRIAKAIA----HDMTTFICK 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  120 ENGqIAVFDATNTTRERRDMILNFAEQ----NSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERnrenVMEDFLKRIE 195
Cdd:PTZ00322 293 TDG-VAVLDGTNTTHARRMALLRAIREtgliRMTRVVFVEVVNNNSETIRRNVLRAKEMFPGAPED----FVDRYYEVIE 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  196 CYKVTYRPLDPDNyDKDLSFIKVINvGQRFLVNRVQDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLS 275
Cdd:PTZ00322 368 QLEAVYKSLNPVT-DCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLT 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  276 VRGKQFAQAL-RKFLEEQEITDLKVWTSQLKRTIQTAE---------------------SLGVPYEQWKILNEIDAGVCE 333
Cdd:PTZ00322 446 ERGRAYSRALfEYFQKEISTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYFPTLDDINHGDCE 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  334 EMTYAEIEKRYPEEFALRDQEKYLYRYPGGE-SYQDLVQRLEPVIMELERQGN-VLVISHQAVMRCLLAYFLDKGADELP 411
Cdd:PTZ00322 526 GQLLSDVRRTMPNTLQSMKADPYYTAWPNGEcIHQVFNARLEPHIHDIQASTTpVLVVSHLHLLQGLYSYFVTDGDNIVA 605
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 64762445  412 -----YLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHR 446
Cdd:PTZ00322 606 pqnayKIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQ 645
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
249-416 1.95e-46

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 159.72  E-value: 1.95e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 249 PRTIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWK 322
Cdd:COG0406   1 MTRLYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEalaeALGLPVEVDP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 323 ILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMRCLL 399
Cdd:COG0406  79 RLREIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARhpgGTVLVVTHGGVIRALL 158
                       170
                ....*....|....*..
gi 64762445 400 AYFLDKGADELPYLRCP 416
Cdd:COG0406 159 AHLLGLPLEAFWRLRID 175
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
251-398 3.47e-41

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: 144.53  E-value: 3.47e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445    251 TIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFL-EEQEITDLKVWTSQLKRTIQTAESLGVPYEQWkILNEI 327
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLP-GLRER 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 64762445    328 DAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRY---PGGESYQDLVQRLEPVIMELERQ-----GNVLVISHQAVMRCL 398
Cdd:smart00855  80 DFGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPpapPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
251-437 1.15e-34

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: 126.67  E-value: 1.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 251 TIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESL-----GVPYEQWKI 323
Cdd:cd07067   1 RLYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIIleelpGLPVEVDPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 324 LNEidagvceemtyaeiekrypeefalrdqekylyrypggesyqdlvQRLEPVIMELERQ---GNVLVISHQAVMRCLLA 400
Cdd:cd07067  81 LRE--------------------------------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLA 116
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 64762445 401 YFLDKGADELPYLRCPLHTIFKLTPVAYGCKVETIKL 437
Cdd:cd07067 117 YLLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
252-430 3.32e-30

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: 115.41  E-value: 3.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   252 IYLCRHGESEFNLLGKIG-GDSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAESLGVPyEQWKI-----LN 325
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILAER-RGLPIikddrLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445   326 EIDAGVCEEMTYAEIEKRYPEefalrdQEKYL-----YRYPGGESYQDLVQRLEPV---IMELERQGNVLVISHQAVMRC 397
Cdd:TIGR03162  78 EMDFGDWEGRSWDEIPEAYPE------LDAWAadwqhARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRA 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 64762445   398 LLAYFLDKGADELPYLrcplhtifkltPVAYGC 430
Cdd:TIGR03162 152 LLAHLLGLPLEQWWSF-----------AVEYGS 173
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
251-424 2.31e-25

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: 101.34  E-value: 2.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 251 TIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESlgvpyeqwkILNEID 328
Cdd:cd07040   1 VLYLVRHGEREPNAEGRFTGwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEI---------ILEGLF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 329 AGVceeMTYAEIEKRYpeefalrdqekylyrypggesYQDLVQRLEPvimELERQGNVLVISHQAVMRCLLAYFLDKGAD 408
Cdd:cd07040  72 EGL---PVEVDPRARV---------------------LNALLELLAR---HLLDGKNVLIVSHGGTIRALLAALLGLSDE 124
                       170
                ....*....|....*.
gi 64762445 409 ELPYLRCPLHTIFKLT 424
Cdd:cd07040 125 EILSLNLPNGSILVLE 140
PRK13463 PRK13463
phosphoserine phosphatase 1;
251-402 2.34e-17

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 80.48  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  251 TIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAESL----GVPYEQWKIL 324
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLGERMKDLSIH--AIYSSPSERTLHTAELIkgerDIPIIADEHF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  325 NEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQR-LEPVIMELERQG--NVLVISHQAVMRCLLAY 401
Cdd:PRK13463  82 YEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHKgeSILIVSHAAAAKLLVGH 161

                 .
gi 64762445  402 F 402
Cdd:PRK13463 162 F 162
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
252-404 4.72e-16

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 76.63  E-value: 4.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  252 IYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLeeQEITDLKVWTSQLKRTIQTAE----SLGVPYEQWKILN 325
Cdd:PRK15004   3 LWLVRHGETQANVDGLYSGhaPTPLTARGIEQAQNLHTLL--RDVPFDLVLCSELERAQHTARlvlsDRQLPVHIIPELN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  326 EIDAGvceemtyaEIEKRYPEEFALRDQEKYL-----YRY---PGGESYQDLVQRLEPVIMEL---ERQGNVLVISHQAV 394
Cdd:PRK15004  81 EMFFG--------DWEMRHHRDLMQEDAENYAawcndWQHaipTNGEGFQAFSQRVERFIARLsafQHYQNLLIVSHQGV 152
                        170
                 ....*....|
gi 64762445  395 MRCLLAYFLD 404
Cdd:PRK15004 153 LSLLIARLLG 162
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
248-410 2.91e-14

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 73.86  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  248 QPRTIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLkVWTSQLKRTIQTA----ESLGVPYEQW 321
Cdd:PRK07238 170 TPTRLLLLRHGQTELSVQRRYSGrgNPELTEVGRRQAAAAARYLAARGGIDA-VVSSPLQRARDTAaaaaKALGLDVTVD 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  322 KILNEIDAGVCEEMTYAEIEKRYPEEFA--LRDQEkylYRYPGGESYQDLVQRLEPVIMELERQ---GNVLVISHQAVMR 396
Cdd:PRK07238 249 DDLIETDFGAWEGLTFAEAAERDPELHRawLADTS---VAPPGGESFDAVARRVRRARDRLIAEypgATVLVVSHVTPIK 325
                        170
                 ....*....|....
gi 64762445  397 CLLAYFLDKGADEL 410
Cdd:PRK07238 326 TLLRLALDAGPGVL 339
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
252-403 4.35e-13

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 68.22  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  252 IYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITdlKVWTSQLKRTIQTAE----SLGVPYEQWKILN 325
Cdd:PRK03482   4 VYLVRHGETQWNAERRIQGqsDSPLTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAEiiaqACGCDIIFDPRLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  326 EIDAGVCEEMtyaEIEKRYPEEFALRDQekyLY------RYPGGESYQDLVQRLEPVI---MELERQGNVLVISHQAVMR 396
Cdd:PRK03482  82 ELNMGVLEKR---HIDSLTEEEEGWRRQ---LVngtvdgRIPEGESMQELSDRMHAALescLELPQGSRPLLVSHGIALG 155

                 ....*..
gi 64762445  397 CLLAYFL 403
Cdd:PRK03482 156 CLVSTIL 162
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
254-409 6.77e-10

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-dependent) is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440353  Cd Length: 229  Bit Score: 58.94  E-value: 6.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 254 LCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEIT-DLkVWTSQLKRTIQTA----ESLG---VP-YEQWK 322
Cdd:COG0588   5 LLRHGESEWNLENRFTGwtDVDLSEKGRAEAKRAGRLLKEAGFLfDV-AYTSVLKRAIRTLwivlDEMDrlwIPvEKSWR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 323 iLNEIDAGVCEEMTYAEIEKRYPEE--------FALR------DQEKYLY---RY--------PGGESYQDLVQRLEP-- 375
Cdd:COG0588  84 -LNERHYGALQGLNKAETAAKYGEEqvhiwrrsYDVPpppldpDDPRHPGndpRYadlppaelPLTESLKDTVARVLPyw 162
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 64762445 376 --VIM-ELERQGNVLVISHQAVMRCLLAYfLDKGADE 409
Cdd:COG0588 163 eeEIApALKAGKRVLIAAHGNSLRALVKH-LDGISDE 198
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
252-392 1.13e-08

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 54.11  E-value: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 252 IYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGvpyEQWKILNEIDagV 331
Cdd:COG2062   1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILA---EALGLPPKVE--V 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 64762445 332 CEEMTYAEIEkrypeefalrdqekylyrypggesyqDLVQRLEpvimELERQGNVLVISHQ 392
Cdd:COG2062  76 EDELYDADPE--------------------------DLLDLLR----ELDDGETVLLVGHN 106
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
40-207 1.19e-08

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 54.15  E-value: 1.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  40 LIVMIGLPARGKTYVSKKLTRYLNWIgvptkvfnlgVYRREAVKSY---KSYDFFRHDNEEAMKIRKQCALVALEDVKAy 116
Cdd:COG0645   1 LILVCGLPGSGKSTLARALAERLGAV----------RLRSDVVRKRlfgAGLAPLERSPEATARTYARLLALARELLAA- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 117 lteenGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVEsvCD-DPDVIAANILevkvsspdypERNRENVMEDF-LKRI 194
Cdd:COG0645  70 -----GRSVILDATFLRRAQREAFRALAEEAGAPFVLIW--LDaPEEVLRERLE----------ARNAEGGDSDAtWEVL 132
                       170
                ....*....|...
gi 64762445 195 ECYKVTYRPLDPD 207
Cdd:COG0645 133 ERQLAFEEPLTED 145
PRK13462 PRK13462
acid phosphatase; Provisional
254-404 1.20e-08

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 54.84  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  254 LCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPY-EQWKILNEIDAG 330
Cdd:PRK13462  10 LLRHGETEWSKSGRHTGrtELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKLAGLTVdEVSGLLAEWDYG 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 64762445  331 VCEEMTYAEIEKRYPEEFAlrdqekYLYRYPGGESYQDLVQRLEPVI---MELERQGNVLVISHQAVMRCLLAYFLD 404
Cdd:PRK13462  90 SYEGLTTPQIRESEPDWLV------WTHGCPGGESVAQVNERADRAValaLEHMESRDVVFVSHGHFSRAVITRWVE 160
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
40-195 1.22e-07

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 50.77  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445    40 LIVMIGLPARGKTYVSKKLTRYLNWIGVptkvfNLGVYRREAVKSYksydffRHDNEEAMKIRKQCALVALEDVKAYLTE 119
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAVRL-----SSDDERKRLFGEG------RPSISYYTDATDRTYERLHELARIALRA 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 64762445   120 enGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVesVCD-DPDVIAANILEVKVSSPDYPERNREnVMEDFLKRIE 195
Cdd:pfam13671  70 --GRPVILDATNLRRDERARLLALAREYGVPVRIV--VFEaPEEVLRERLAARARAGGDPSDVPEE-VLDRQKARFE 141
PRK01295 PRK01295
phosphoglyceromutase; Provisional
249-399 1.33e-07

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 52.00  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  249 PRTIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTA----ESLG---VPYE 319
Cdd:PRK01295   2 SRTLVLVRHGQSEWNLKNLFTGwrDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCqlilEELGqpgLETI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  320 QWKILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQD--------LVQRLEPVIMELERqgnVLVISH 391
Cdd:PRK01295  82 RDQALNERDYGDLSGLNKDDARAKWGEEQVHIWRRSYDVPPPGGESLKDtgarvlpyYLQEILPRVLRGER---VLVAAH 158

                 ....*...
gi 64762445  392 QAVMRCLL 399
Cdd:PRK01295 159 GNSLRALV 166
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
263-409 1.56e-07

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 52.35  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  263 NLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTA----ESLGVPY----EQWKiLNEIDAGVC 332
Cdd:PTZ00123   2 NKENRFTGwtDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAwivlEELGQLHvpviKSWR-LNERHYGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  333 EEMTYAEIEKRYPEE--------FALR--DQEKYLYRYPG---------------GESYQDLVQRLEP----VIMELERQ 383
Cdd:PTZ00123  81 QGLNKSETAEKHGEEqvkiwrrsYDIPppPLEKSDERYPGndpvykdipkdalpnTECLKDTVERVLPywedHIAPDILA 160
                        170       180
                 ....*....|....*....|....*..
gi 64762445  384 G-NVLVISHQAVMRCLLAYfLDKGADE 409
Cdd:PTZ00123 161 GkKVLVAAHGNSLRALVKY-LDKMSEE 186
gpmA PRK14120
phosphoglyceromutase; Provisional
249-409 1.75e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 52.35  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  249 PRTIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQT-------AESLGVPYE 319
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNLFTGwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTanlaldaADRLWIPVR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  320 Q-WKiLNEIDAGVCEEMTYAEIEKRYPEE---------------------FALRDQEKY--LYRYPGGESYQDLVQRLEP 375
Cdd:PRK14120  84 RsWR-LNERHYGALQGKDKAETKAEYGEEqfmlwrrsydtppppiedgseYSQDNDPRYadLGVGPRTECLKDVVARFLP 162
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 64762445  376 -----VIMELERQGNVLVISHQAVMRCLLAYfLDKGADE 409
Cdd:PRK14120 163 yweddIVPDLKAGKTVLIAAHGNSLRALVKH-LDGISDE 200
COG4639 COG4639
Predicted kinase [General function prediction only];
38-195 1.15e-06

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 47.90  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  38 PTLIVMIGLPARGKTYVSKKLTRylnwigvPTKVFNLGVYRREavksyksydffRHDNEEAMKIRKQCALVALEDVKAYL 117
Cdd:COG4639   2 LSLVVLIGLPGSGKSTFARRLFA-------PTEVVSSDDIRAL-----------LGGDENDQSAWGDVFQLAHEIARARL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445 118 teENGQIAVFDATNTTRERRDMILNFAeqNSFKVFFVESVCDDPDVIAAnilevkvsspdypERNR-------ENVMEDF 190
Cdd:COG4639  64 --RAGRLTVVDATNLQREARRRLLALA--RAYGALVVAVVLDVPLEVCL-------------ARNAardrqvpEEVIRRM 126

                ....*
gi 64762445 191 LKRIE 195
Cdd:COG4639 127 LRRLR 131
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
250-409 3.64e-06

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 48.32  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  250 RTIYLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQT-------AESLGVPYEQ 320
Cdd:PRK14115   1 TKLVLIRHGESQWNKENRFTGwtDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTlwivldeLDQMWLPVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  321 -WKiLNEIDAGVCEEMTYAEIEKRYPEE--------FALR------DQEKYLY---RY--------PGGESYQDLVQRLE 374
Cdd:PRK14115  81 sWR-LNERHYGALQGLNKAETAAKYGDEqvkiwrrsYDVPppalekDDERYPGhdpRYaklpeeelPLTESLKDTIARVL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 64762445  375 P----VIMELERQGN-VLVISHQAVMRCLLAYfLDKGADE 409
Cdd:PRK14115 160 PywneTIAPQLKSGKrVLIAAHGNSLRALVKY-LDNISDE 198
gpmA PRK14119
phosphoglyceromutase; Provisional
249-409 6.68e-06

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 47.19  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  249 PRTIyLCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQT-----AES--LGVP-Y 318
Cdd:PRK14119   2 PKLI-LCRHGQSEWNAKNLFTGweDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTthyilTESkqQWIPvY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  319 EQWKiLNEIDAGVCEEMTYAEIEKRYPEE--------FALR-------DQEKYL----YRY------PGGESYQDLVQRL 373
Cdd:PRK14119  81 KSWR-LNERHYGGLQGLNKDDARKEFGEEqvhiwrrsYDVKppaeteeQREAYLadrrYNHldkrmmPYSESLKDTLVRV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 64762445  374 EP-----VIMELERQGNVLVISHQAVMRCLLAYfLDKGADE 409
Cdd:PRK14119 160 IPfwtdhISQYLLDGQTVLVSAHGNSIRALIKY-LEDVSDE 199
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
254-401 1.08e-05

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 46.45  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  254 LCRHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQT-------AESLGVP-YEQWKi 323
Cdd:PRK14116   6 LIRHGQSEWNLSNQFTGwvDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTlhyaleeSDQLWIPeTKTWR- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  324 LNEIDAGVCEEMTYAEIEKRYPEE----------------------FALRDQekylyRY--------PGGESYQDLVQRL 373
Cdd:PRK14116  85 LNERHYGALQGLNKKETAEKYGDEqvhiwrrsydvlpplldaddegSAAKDR-----RYanldpriiPGGENLKVTLERV 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 64762445  374 EP-----VIMELERQGNVLVISHQAVMRCLLAY 401
Cdd:PRK14116 160 IPfwedhIAPDLLDGKNVIIAAHGNSLRALTKY 192
gpmA PRK14117
phosphoglyceromutase; Provisional
256-347 5.25e-05

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 44.63  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  256 RHGESEFNLLGKIGG--DSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQT-------AESLGVPYEQ-WKiLN 325
Cdd:PRK14117   8 RHGESEWNKANLFTGwaDVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTtnlaleaSDQLWVPVEKsWR-LN 86
                         90       100
                 ....*....|....*....|..
gi 64762445  326 EIDAGVCEEMTYAEIEKRYPEE 347
Cdd:PRK14117  87 ERHYGGLTGKNKAEAAEQFGDE 108
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
37-184 2.20e-04

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 42.02  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64762445  37 SPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRReavkSYKSYDFFRHDNEE-AMKIRKQCAlvaledvKA 115
Cdd:COG4088   3 SPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRR----FLVNESFPKETYEEvVEDVRTTTA-------DN 71
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 64762445 116 YLTeeNGQIAVFDATNTTRERRDMILNFAEQNSfKVFFVesVCDDPDVIAAnilevkvsspdypERNRE 184
Cdd:COG4088  72 ALD--NGYSVIVDGTFYYRSWQRDFRNLAKHKA-PIHII--YLKAPLETAL-------------RRNRE 122
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
252-315 5.98e-03

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 37.51  E-value: 5.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 64762445   252 IYLCRHGESEfnLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLG 315
Cdd:TIGR00249   3 LFIMRHGDAA--LDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVG 64
 
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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