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Conserved domains on  [gi|224282149|ref|NP_001138915|]
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 isoform 2 [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, ...
4-226 3.15e-142

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: 407.49  E-value: 3.15e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149    4 RKACGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCA 83
Cdd:pfam01591   2 RGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQCA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149   84 LAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEA 163
Cdd:pfam01591  82 LAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEEA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224282149  164 MDDFMKRISCYEASYQPLDpDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQP 226
Cdd:pfam01591 162 IDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
229-415 4.08e-51

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: 172.39  E-value: 4.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  229 IYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKdlRVWTSQLKSTIQTAE----ALRLPYEQWKALN 302
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  303 EIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLRCLLAYF 379
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 224282149  380 LDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLN 415
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
4-226 3.15e-142

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: 407.49  E-value: 3.15e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149    4 RKACGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCA 83
Cdd:pfam01591   2 RGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQCA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149   84 LAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEA 163
Cdd:pfam01591  82 LAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEEA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224282149  164 MDDFMKRISCYEASYQPLDpDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQP 226
Cdd:pfam01591 162 IDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
229-415 4.08e-51

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: 172.39  E-value: 4.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  229 IYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKdlRVWTSQLKSTIQTAE----ALRLPYEQWKALN 302
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  303 EIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLRCLLAYF 379
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 224282149  380 LDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLN 415
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
17-431 4.49e-47

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 173.16  E-value: 4.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  17 VIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCAlaalRDVKSYLAK 96
Cdd:PTZ00322 217 IVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRLERRGGAVSSPTGAAEVEFRIAKAIA----HDMTTFICK 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  97 EGGqIAVFDATNTTRERRHMILHFAKE----NDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDcnsaEAMDDFMKRIS 172
Cdd:PTZ00322 293 TDG-VAVLDGTNTTHARRMALLRAIREtgliRMTRVVFVEVVNNNSETIRRNVLRAKEMFPGAPE----DFVDRYYEVIE 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 173 CYEASYQPLDPdKCDRDLSLIKVIDvGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLS 252
Cdd:PTZ00322 368 QLEAVYKSLNP-VTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLT 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 253 SRGKKFASALSK-FVEEQNLKDLRVWTSQLKSTIQTAE---------------------ALRLPYEQWKALNEIDAGVCE 310
Cdd:PTZ00322 446 ERGRAYSRALFEyFQKEISTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYFPTLDDINHGDCE 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 311 ELTYEEIRDTYPEEYALREQDKYYYRYPTGE-SYQDLVQRLEPVIMELE-RQENVLVICHQAVLRCLLAYFLDKS----A 384
Cdd:PTZ00322 526 GQLLSDVRRTMPNTLQSMKADPYYTAWPNGEcIHQVFNARLEPHIHDIQaSTTPVLVVSHLHLLQGLYSYFVTDGdnivA 605
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 224282149 385 EEMPY-LKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKK 431
Cdd:PTZ00322 606 PQNAYkIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQSRTGLVTK 653
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
226-393 3.97e-41

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 145.86  E-value: 3.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 226 PRTIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFveeqnLKDL---RVWTSQLKSTIQTAEALR----LPYE 296
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAER-----LADIpfdAVYSSPLQRARQTAEALAealgLPVE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 297 QWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLR 373
Cdd:COG0406   76 VDPRLREIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARhpgGTVLVVTHGGVIR 155
                        170       180
                 ....*....|....*....|
gi 224282149 374 CLLAYFLDKSAEEMPYLKCP 393
Cdd:COG0406  156 ALLAHLLGLPLEAFWRLRID 175
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
228-375 9.68e-37

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: 132.97  E-value: 9.68e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149   228 TIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFV-EEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWkALNEI 304
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLP-GLRER 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224282149   305 DAGVCEELTYEEIRDTYPEEYA---LREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ-----ENVLVICHQAVLRCL 375
Cdd:smart00855  80 DFGAWEGLTWDEIAAKYPEEYLaawRDPYDPAPPAPPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
228-414 3.79e-33

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: 123.20  E-value: 3.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 228 TIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALR-----LPYEQWKA 300
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILeelpgLPVEVDPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 301 LNEidagvceeltyeeirdtypeeyalreqdkyyyryptgesyqdlvQRLEPVIMELERQ---ENVLVICHQAVLRCLLA 377
Cdd:cd07067   81 LRE--------------------------------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLA 116
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 224282149 378 YFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYL 414
Cdd:cd07067  117 YLLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
229-407 5.40e-28

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: 109.63  E-value: 5.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  229 IYLCRHGENEHNLQGRIG-GDSGLSSRGKKFASALSkfveeQNLKDL---RVWTSQLKSTIQTAEAL----RLPYEQWKA 300
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALR-----EKLADVpfdAVYSSPLSRCRELAEILaerrGLPIIKDDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  301 LNEIDAGVCEELTYEEIRDTYPeEYALREQDKYYYRYPTGESYQDLVQRLEPV---IMELERQENVLVICHQAVLRCLLA 377
Cdd:TIGR03162  76 LREMDFGDWEGRSWDEIPEAYP-ELDAWAADWQHARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRALLA 154
                         170       180       190
                  ....*....|....*....|....*....|
gi 224282149  378 YFLDKSAEEMPYLkcplhtvlkltPVAYGC 407
Cdd:TIGR03162 155 HLLGLPLEQWWSF-----------AVEYGS 173
PRK13463 PRK13463
phosphoserine phosphatase 1;
228-379 1.08e-14

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 72.77  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 228 TIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSkfveeQNLKDLR---VWTSQLKSTIQTAEALR----LPYEQW 298
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLG-----ERMKDLSihaIYSSPSERTLHTAELIKgerdIPIIAD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 299 KALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQR-LEPVIMELERQ--ENVLVICHQAVLRCL 375
Cdd:PRK13463  79 EHFYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHkgESILIVSHAAAAKLL 158

                 ....
gi 224282149 376 LAYF 379
Cdd:PRK13463 159 VGHF 162
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
14-122 1.85e-05

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: 45.10  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  14 SPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRReavkQYSSYNFFRPDNEE-AMKVRKQCALAALrdvks 92
Cdd:COG4088    3 SPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRR----FLVNESFPKETYEEvVEDVRTTTADNAL----- 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 224282149  93 ylakEGGQIAVFDATNTTRERRHMILHFAK 122
Cdd:COG4088   74 ----DNGYSVIVDGTFYYRSWQRDFRNLAK 99
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
4-226 3.15e-142

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: 407.49  E-value: 3.15e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149    4 RKACGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCA 83
Cdd:pfam01591   2 RGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQCA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149   84 LAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEA 163
Cdd:pfam01591  82 LAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEEA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224282149  164 MDDFMKRISCYEASYQPLDpDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQP 226
Cdd:pfam01591 162 IDDFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
229-415 4.08e-51

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: 172.39  E-value: 4.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  229 IYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKdlRVWTSQLKSTIQTAE----ALRLPYEQWKALN 302
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  303 EIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLRCLLAYF 379
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 224282149  380 LDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLN 415
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
17-431 4.49e-47

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 173.16  E-value: 4.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  17 VIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCAlaalRDVKSYLAK 96
Cdd:PTZ00322 217 IVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRLERRGGAVSSPTGAAEVEFRIAKAIA----HDMTTFICK 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  97 EGGqIAVFDATNTTRERRHMILHFAKE----NDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDcnsaEAMDDFMKRIS 172
Cdd:PTZ00322 293 TDG-VAVLDGTNTTHARRMALLRAIREtgliRMTRVVFVEVVNNNSETIRRNVLRAKEMFPGAPE----DFVDRYYEVIE 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 173 CYEASYQPLDPdKCDRDLSLIKVIDvGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLS 252
Cdd:PTZ00322 368 QLEAVYKSLNP-VTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLT 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 253 SRGKKFASALSK-FVEEQNLKDLRVWTSQLKSTIQTAE---------------------ALRLPYEQWKALNEIDAGVCE 310
Cdd:PTZ00322 446 ERGRAYSRALFEyFQKEISTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYFPTLDDINHGDCE 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 311 ELTYEEIRDTYPEEYALREQDKYYYRYPTGE-SYQDLVQRLEPVIMELE-RQENVLVICHQAVLRCLLAYFLDKS----A 384
Cdd:PTZ00322 526 GQLLSDVRRTMPNTLQSMKADPYYTAWPNGEcIHQVFNARLEPHIHDIQaSTTPVLVVSHLHLLQGLYSYFVTDGdnivA 605
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 224282149 385 EEMPY-LKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKK 431
Cdd:PTZ00322 606 PQNAYkIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQSRTGLVTK 653
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
226-393 3.97e-41

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 145.86  E-value: 3.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 226 PRTIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFveeqnLKDL---RVWTSQLKSTIQTAEALR----LPYE 296
Cdd:COG0406    1 MTRLYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAER-----LADIpfdAVYSSPLQRARQTAEALAealgLPVE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 297 QWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLR 373
Cdd:COG0406   76 VDPRLREIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARhpgGTVLVVTHGGVIR 155
                        170       180
                 ....*....|....*....|
gi 224282149 374 CLLAYFLDKSAEEMPYLKCP 393
Cdd:COG0406  156 ALLAHLLGLPLEAFWRLRID 175
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
228-375 9.68e-37

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: 132.97  E-value: 9.68e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149   228 TIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFV-EEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWkALNEI 304
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLP-GLRER 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224282149   305 DAGVCEELTYEEIRDTYPEEYA---LREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ-----ENVLVICHQAVLRCL 375
Cdd:smart00855  80 DFGAWEGLTWDEIAAKYPEEYLaawRDPYDPAPPAPPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
228-414 3.79e-33

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: 123.20  E-value: 3.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 228 TIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALR-----LPYEQWKA 300
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILeelpgLPVEVDPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 301 LNEidagvceeltyeeirdtypeeyalreqdkyyyryptgesyqdlvQRLEPVIMELERQ---ENVLVICHQAVLRCLLA 377
Cdd:cd07067   81 LRE--------------------------------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLA 116
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 224282149 378 YFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYL 414
Cdd:cd07067  117 YLLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
229-407 5.40e-28

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: 109.63  E-value: 5.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  229 IYLCRHGENEHNLQGRIG-GDSGLSSRGKKFASALSkfveeQNLKDL---RVWTSQLKSTIQTAEAL----RLPYEQWKA 300
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALR-----EKLADVpfdAVYSSPLSRCRELAEILaerrGLPIIKDDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  301 LNEIDAGVCEELTYEEIRDTYPeEYALREQDKYYYRYPTGESYQDLVQRLEPV---IMELERQENVLVICHQAVLRCLLA 377
Cdd:TIGR03162  76 LREMDFGDWEGRSWDEIPEAYP-ELDAWAADWQHARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRALLA 154
                         170       180       190
                  ....*....|....*....|....*....|
gi 224282149  378 YFLDKSAEEMPYLkcplhtvlkltPVAYGC 407
Cdd:TIGR03162 155 HLLGLPLEQWWSF-----------AVEYGS 173
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
228-401 8.52e-23

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: 94.40  E-value: 8.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 228 TIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEID 305
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTGwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEVDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 306 AgvceeltyeeirdtypeeyalreqdkyyyryptgesyqdlvQRLEPVIMELERQ-----ENVLVICHQAVLRCLLAYFL 380
Cdd:cd07040   81 R-----------------------------------------ARVLNALLELLARhlldgKNVLIVSHGGTIRALLAALL 119
                        170       180
                 ....*....|....*....|.
gi 224282149 381 DKSAEEMPYLKCPLHTVLKLT 401
Cdd:cd07040  120 GLSDEEILSLNLPNGSILVLE 140
PRK13463 PRK13463
phosphoserine phosphatase 1;
228-379 1.08e-14

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 72.77  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 228 TIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSkfveeQNLKDLR---VWTSQLKSTIQTAEALR----LPYEQW 298
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLG-----ERMKDLSihaIYSSPSERTLHTAELIKgerdIPIIAD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 299 KALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQR-LEPVIMELERQ--ENVLVICHQAVLRCL 375
Cdd:PRK13463  79 EHFYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHkgESILIVSHAAAAKLL 158

                 ....
gi 224282149 376 LAYF 379
Cdd:PRK13463 159 VGHF 162
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
229-387 1.41e-14

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 72.39  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 229 IYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVeeQNLKDLRVWTSQLKSTIQTAE----ALRLPYEQWKALN 302
Cdd:PRK15004   3 LWLVRHGETQANVDGLYSGhaPTPLTARGIEQAQNLHTLL--RDVPFDLVLCSELERAQHTARlvlsDRQLPVHIIPELN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 303 EIDAGVCE-----ELTYEEirdtyPEEYALREQDkYYYRYPT-GESYQDLVQRLEPVIMEL---ERQENVLVICHQAVLR 373
Cdd:PRK15004  81 EMFFGDWEmrhhrDLMQED-----AENYAAWCND-WQHAIPTnGEGFQAFSQRVERFIARLsafQHYQNLLIVSHQGVLS 154
                        170
                 ....*....|....
gi 224282149 374 CLLAYFLDKSAEEM 387
Cdd:PRK15004 155 LLIARLLGMPAEAM 168
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
225-385 3.40e-11

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 64.61  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 225 QPRTIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLrVWTSQLKSTIQTA----EALRLPYEQW 298
Cdd:PRK07238 170 TPTRLLLLRHGQTELSVQRRYSGrgNPELTEVGRRQAAAAARYLAARGGIDA-VVSSPLQRARDTAaaaaKALGLDVTVD 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 299 KALNEIDAGVCEELTYEEIRDTYPEEYA--LREQDkyyYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLR 373
Cdd:PRK07238 249 DDLIETDFGAWEGLTFAEAAERDPELHRawLADTS---VAPPGGESFDAVARRVRRARDRLIAEypgATVLVVSHVTPIK 325
                        170
                 ....*....|..
gi 224282149 374 CLLAYFLDKSAE 385
Cdd:PRK07238 326 TLLRLALDAGPG 337
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
229-380 9.34e-11

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 61.67  E-value: 9.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 229 IYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKdlRVWTSQLKSTIQTAE----ALRLPYEQWKALN 302
Cdd:PRK03482   4 VYLVRHGETQWNAERRIQGqsDSPLTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAEiiaqACGCDIIFDPRLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 303 EIDAGVCEEltyEEIRDTYPEEYALREQ------DKyyyRYPTGESYQDLVQRLEPVI---MELERQENVLVICHQAVLR 373
Cdd:PRK03482  82 ELNMGVLEK---RHIDSLTEEEEGWRRQlvngtvDG---RIPEGESMQELSDRMHAALescLELPQGSRPLLVSHGIALG 155

                 ....*..
gi 224282149 374 CLLAYFL 380
Cdd:PRK03482 156 CLVSTIL 162
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
240-393 1.74e-08

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 55.05  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 240 NLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTA----EALRLPY----EQWKaLNEIDAGVC 309
Cdd:PTZ00123   2 NKENRFTGwtDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAwivlEELGQLHvpviKSWR-LNERHYGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 310 EELTYEEIRDTYPEE--------Y-----ALREQDKYY----YRY--------PTGESYQDLVQRLEP-----VIMELER 359
Cdd:PTZ00123  81 QGLNKSETAEKHGEEqvkiwrrsYdipppPLEKSDERYpgndPVYkdipkdalPNTECLKDTVERVLPywedhIAPDILA 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 224282149 360 QENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCP 393
Cdd:PTZ00123 161 GKKVLVAAHGNSLRALVKYLDKMSEEDILELNIP 194
PRK01295 PRK01295
phosphoglyceromutase; Provisional
226-388 9.01e-08

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 52.38  E-value: 9.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 226 PRTIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEAL-------RLPYE 296
Cdd:PRK01295   2 SRTLVLVRHGQSEWNLKNLFTGwrDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLIleelgqpGLETI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 297 QWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIME-----LERQENVLVICHQAV 371
Cdd:PRK01295  82 RDQALNERDYGDLSGLNKDDARAKWGEEQVHIWRRSYDVPPPGGESLKDTGARVLPYYLQeilprVLRGERVLVAAHGNS 161
                        170
                 ....*....|....*...
gi 224282149 372 LRCLLAyFLDK-SAEEMP 388
Cdd:PRK01295 162 LRALVM-VLDGlTPEQIL 178
gpmA PRK14119
phosphoglyceromutase; Provisional
226-387 1.53e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 52.20  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 226 PRTIyLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQT-------AEALRLP-Y 295
Cdd:PRK14119   2 PKLI-LCRHGQSEWNAKNLFTGweDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTthyilteSKQQWIPvY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 296 EQWKaLNEIDAGVCEELTYEEIRDTYPEE--------YALR------EQDKYY-----YRY------PTGESYQDLVQRL 350
Cdd:PRK14119  81 KSWR-LNERHYGGLQGLNKDDARKEFGEEqvhiwrrsYDVKppaeteEQREAYladrrYNHldkrmmPYSESLKDTLVRV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 224282149 351 EP-----VIMELERQENVLVICHQAVLRCLLAYFLDKSAEEM 387
Cdd:PRK14119 160 IPfwtdhISQYLLDGQTVLVSAHGNSIRALIKYLEDVSDEDI 201
gpmA PRK14120
phosphoglyceromutase; Provisional
226-393 1.12e-06

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 50.04  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 226 PRTIYLCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTA-----EALRL--PYE 296
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNLFTGwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTAnlaldAADRLwiPVR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 297 Q-WKaLNEIDAGVCEELTYEEIRDTYPEE--------YA-----LREQDKYYY----RY------PTGESYQDLVQRLEP 352
Cdd:PRK14120  84 RsWR-LNERHYGALQGKDKAETKAEYGEEqfmlwrrsYDtppppIEDGSEYSQdndpRYadlgvgPRTECLKDVVARFLP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 224282149 353 -----VIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCP 393
Cdd:PRK14120 163 yweddIVPDLKAGKTVLIAAHGNSLRALVKHLDGISDEDIAGLNIP 208
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
14-122 1.85e-05

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: 45.10  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  14 SPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRReavkQYSSYNFFRPDNEE-AMKVRKQCALAALrdvks 92
Cdd:COG4088    3 SPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRR----FLVNESFPKETYEEvVEDVRTTTADNAL----- 73
                         90       100       110
                 ....*....|....*....|....*....|
gi 224282149  93 ylakEGGQIAVFDATNTTRERRHMILHFAK 122
Cdd:COG4088   74 ----DNGYSVIVDGTFYYRSWQRDFRNLAK 99
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
229-369 3.54e-05

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 44.09  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 229 IYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRlpyEQWKALNEIDagV 308
Cdd:COG2062    1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILA---EALGLPPKVE--V 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224282149 309 CEELtyeeirdtypeeyalreqdkyyyryptgesYQDLVQRLEPVIMELERQENVLVICHQ 369
Cdd:COG2062   76 EDEL------------------------------YDADPEDLLDLLRELDDGETVLLVGHN 106
COG4639 COG4639
Predicted kinase [General function prediction only];
15-125 4.74e-05

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 43.28  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149  15 PTVIVMVGLPARGKTYISKKLTRylnwigvPTKVFNVGEYRREAvkqYSSYNFFRPdNEEAMKVRKQCALAALRDvksyl 94
Cdd:COG4639    2 LSLVVLIGLPGSGKSTFARRLFA-------PTEVVSSDDIRALL---GGDENDQSA-WGDVFQLAHEIARARLRA----- 65
                         90       100       110
                 ....*....|....*....|....*....|.
gi 224282149  95 akegGQIAVFDATNTTRERRHMILHFAKEND 125
Cdd:COG4639   66 ----GRLTVVDATNLQREARRRLLALARAYG 92
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
17-127 1.79e-04

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: 41.53  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149   17 VIVMVGLPARGKTYISKKLTRYLNWIGVptkvfNVGEYRR----EAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVks 92
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAVRL-----SSDDERKrlfgEGRPSISYYTDATDRTYERLHELARIALRAGRPV-- 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 224282149   93 ylakeggqiaVFDATNTTRERRHMILHFAKENDFK 127
Cdd:pfam13671  74 ----------ILDATNLRRDERARLLALAREYGVP 98
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
231-387 2.73e-04

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 42.59  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 231 LCRHGENEHNLQGRIGG--DSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQT-------AEALRLP-YEQWKa 300
Cdd:PRK14116   6 LIRHGQSEWNLSNQFTGwvDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTlhyaleeSDQLWIPeTKTWR- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224282149 301 LNEIDAGVCEELTYEEIRDTYPEEY-------------ALREQDKYYY----RY--------PTGESYQDLVQRLEP--- 352
Cdd:PRK14116  85 LNERHYGALQGLNKKETAEKYGDEQvhiwrrsydvlppLLDADDEGSAakdrRYanldpriiPGGENLKVTLERVIPfwe 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 224282149 353 --VIMELERQENVLVICHQAVLRCLLAYFLDKSAEEM 387
Cdd:PRK14116 165 dhIAPDLLDGKNVIIAAHGNSLRALTKYIENISDEDI 201
 
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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