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Conserved domains on  [gi|295293217|ref|NP_001171228|]
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 isoform 7 [Mus musculus]

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, ...
26-246 6.33e-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: 6.33e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217   26 SCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCALA 105
Cdd:pfam01591   4 STGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQCALA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  106 ALRDVKSYLTKEGGQIAVFDATNTTRERRHMILNFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMD 185
Cdd:pfam01591  84 ALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEEAID 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295293217  186 DFMKRINCYEASYQPLDpDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQP 246
Cdd:pfam01591 164 DFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
249-435 1.09e-50

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centers 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: 425591 [Multi-domain]  Cd Length: 194  Bit Score: 172.01  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  249 IYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKdlRVWTSQLKSTIQTAE----ALRLPYEQWKALN 322
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  323 EIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLRCLLAYF 399
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 295293217  400 LDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLN 435
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, ...
26-246 6.33e-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: 6.33e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217   26 SCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCALA 105
Cdd:pfam01591   4 STGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQCALA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  106 ALRDVKSYLTKEGGQIAVFDATNTTRERRHMILNFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMD 185
Cdd:pfam01591  84 ALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEEAID 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295293217  186 DFMKRINCYEASYQPLDpDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQP 246
Cdd:pfam01591 164 DFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
249-435 1.09e-50

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centers 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: 425591 [Multi-domain]  Cd Length: 194  Bit Score: 172.01  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  249 IYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKdlRVWTSQLKSTIQTAE----ALRLPYEQWKALN 322
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  323 EIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLRCLLAYF 399
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 295293217  400 LDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLN 435
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
37-451 1.27e-47

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 175.47  E-value: 1.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  37 VIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCAlaalRDVKSYLTK 116
Cdd:PTZ00322 217 IVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRLERRGGAVSSPTGAAEVEFRIAKAIA----HDMTTFICK 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 117 EGGqIAVFDATNTTRERRHMILNFAKE----NDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDcnsaEAMDDFMKRIN 192
Cdd:PTZ00322 293 TDG-VAVLDGTNTTHARRMALLRAIREtgliRMTRVVFVEVVNNNSETIRRNVLRAKEMFPGAPE----DFVDRYYEVIE 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 193 CYEASYQPLDPdKCDRDLSLIKVIDvGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEYNLQGKIGGDSGLS 272
Cdd:PTZ00322 368 QLEAVYKSLNP-VTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLT 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 273 SRGKKFANALSK-FVEEQNLKDLRVWTSQLKSTIQTAE---------------------ALRLPYEQWKALNEIDAGVCE 330
Cdd:PTZ00322 446 ERGRAYSRALFEyFQKEISTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYFPTLDDINHGDCE 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 331 ELTYEEIRDTYPEEYALREQDKYYYRYPTGE-SYQDLVQRLEPVIMELE-RQENVLVICHQAVLRCLLAYFLDKS----A 404
Cdd:PTZ00322 526 GQLLSDVRRTMPNTLQSMKADPYYTAWPNGEcIHQVFNARLEPHIHDIQaSTTPVLVVSHLHLLQGLYSYFVTDGdnivA 605
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 295293217 405 EEMPY-LKCPLHTVLKLTPVAYGCRVESIYLNVESVSTHRERSEDAKK 451
Cdd:PTZ00322 606 PQNAYkIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQSRTGLVTK 653
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
245-420 1.86e-44

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 223483 [Multi-domain]  Cd Length: 208  Bit Score: 155.72  E-value: 1.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 245 QPRTIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAE----ALRLPYEQW 318
Cdd:COG0406    1 MMMRLYLVRHGETEWNVEGRLQGwtDSPLTEEGRAQAEALAERLAARDIGFDAIYSSPLKRAQQTAEplaeELGLPLEVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 319 KALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLRCL 395
Cdd:COG0406   81 DRLREIDFGDWEGLTIDELAEEPPEELAAWLADPYLAPPPGGESLADVSKRVVAALAELLRSppgNNVLVVSHGGVIRAL 160
                        170       180
                 ....*....|....*....|....*
gi 295293217 396 LAYFLDKSAEEMPYLKCPLHTVLKL 420
Cdd:COG0406  161 LAYLLGLDLEELWRLRLDNASVTVL 185
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
248-395 1.74e-36

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: 132.58  E-value: 1.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217   248 TIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFV-EEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWkALNEI 324
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLP-GLRER 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295293217   325 DAGVCEELTYEEIRDTYPEEYA---LREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ-----ENVLVICHQAVLRCL 395
Cdd:smart00855  80 DFGAWEGLTWDEIAAKYPEEYLaawRDPYDPAPPAPPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
248-434 2.94e-32

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: 120.89  E-value: 2.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 248 TIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEALR-----LPYEQWKA 320
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILeelpgLPVEVDPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 321 LNEidagvceeltyeeirdtypeeyalreqdkyyyryptgesyqdlvQRLEPVIMELERQ---ENVLVICHQAVLRCLLA 397
Cdd:cd07067   81 LRE--------------------------------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLA 116
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 295293217 398 YFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYL 434
Cdd:cd07067  117 YLLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
249-427 4.28e-27

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: 107.32  E-value: 4.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  249 IYLCRHGENEYNLQGKIG-GDSGLSSRGKKFANALSkfveeQNLKDL---RVWTSQLKSTIQTAEAL----RLPYEQWKA 320
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALR-----EKLADVpfdAVYSSPLSRCRELAEILaerrGLPIIKDDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  321 LNEIDAGVCEELTYEEIRDTYPeEYALREQDKYYYRYPTGESYQDLVQRLEPV---IMELERQENVLVICHQAVLRCLLA 397
Cdd:TIGR03162  76 LREMDFGDWEGRSWDEIPEAYP-ELDAWAADWQHARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRALLA 154
                         170       180       190
                  ....*....|....*....|....*....|
gi 295293217  398 YFLDKSAEEMPYLkcplhtvlkltPVAYGC 427
Cdd:TIGR03162 155 HLLGLPLEQWWSF-----------AVEYGS 173
PRK13463 PRK13463
phosphoserine phosphatase 1;
248-399 8.37e-15

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 73.16  E-value: 8.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 248 TIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSkfveeQNLKDLR---VWTSQLKSTIQTAEALR----LPYEQW 318
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLG-----ERMKDLSihaIYSSPSERTLHTAELIKgerdIPIIAD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 319 KALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQR-LEPVIMELERQ--ENVLVICHQAVLRCL 395
Cdd:PRK13463  79 EHFYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHkgESILIVSHAAAAKLL 158

                 ....
gi 295293217 396 LAYF 399
Cdd:PRK13463 159 VGHF 162
COG4639 COG4639
Predicted kinase [General function prediction only];
36-152 6.16e-03

Predicted kinase [General function prediction only];


Pssm-ID: 226986 [Multi-domain]  Cd Length: 168  Bit Score: 37.83  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  36 TVIVMVGLPARGK-TYISKKLtrylnwigVPTKVFNVGEYRREAVKQYSSYNFFRPDneeamrvrkqcaLAALRDVKSYL 114
Cdd:COG4639    3 ILVVLRGASGSGKsTFAKENF--------LQNYVLSLDDLRLLLGVSASKENSQKND------------ELVWDILYKQL 62
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 295293217 115 TK--EGGQIAVFDATNTTRERRHMILNFAKENDFKAFFIE 152
Cdd:COG4639   63 EQrlRRGKFTIIDATNLRREDRRKLIDLAKAYGYKIYAIV 102
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
26-246 6.33e-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: 6.33e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217   26 SCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCALA 105
Cdd:pfam01591   4 STGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVKAYSNYEFFRPDNPEAMKIREQCALA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  106 ALRDVKSYLTKEGGQIAVFDATNTTRERRHMILNFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMD 185
Cdd:pfam01591  84 ALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEEAID 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295293217  186 DFMKRINCYEASYQPLDpDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQP 246
Cdd:pfam01591 164 DFMKRLECYEKQYEPLD-DEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
249-435 1.09e-50

Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so named because catalysis centers 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: 425591 [Multi-domain]  Cd Length: 194  Bit Score: 172.01  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  249 IYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKdlRVWTSQLKSTIQTAE----ALRLPYEQWKALN 322
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  323 EIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLRCLLAYF 399
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 295293217  400 LDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLN 435
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
37-451 1.27e-47

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 175.47  E-value: 1.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  37 VIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMRVRKQCAlaalRDVKSYLTK 116
Cdd:PTZ00322 217 IVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRLERRGGAVSSPTGAAEVEFRIAKAIA----HDMTTFICK 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 117 EGGqIAVFDATNTTRERRHMILNFAKE----NDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDcnsaEAMDDFMKRIN 192
Cdd:PTZ00322 293 TDG-VAVLDGTNTTHARRMALLRAIREtgliRMTRVVFVEVVNNNSETIRRNVLRAKEMFPGAPE----DFVDRYYEVIE 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 193 CYEASYQPLDPdKCDRDLSLIKVIDvGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEYNLQGKIGGDSGLS 272
Cdd:PTZ00322 368 QLEAVYKSLNP-VTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLT 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 273 SRGKKFANALSK-FVEEQNLKDLRVWTSQLKSTIQTAE---------------------ALRLPYEQWKALNEIDAGVCE 330
Cdd:PTZ00322 446 ERGRAYSRALFEyFQKEISTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYFPTLDDINHGDCE 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 331 ELTYEEIRDTYPEEYALREQDKYYYRYPTGE-SYQDLVQRLEPVIMELE-RQENVLVICHQAVLRCLLAYFLDKS----A 404
Cdd:PTZ00322 526 GQLLSDVRRTMPNTLQSMKADPYYTAWPNGEcIHQVFNARLEPHIHDIQaSTTPVLVVSHLHLLQGLYSYFVTDGdnivA 605
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 295293217 405 EEMPY-LKCPLHTVLKLTPVAYGCRVESIYLNVESVSTHRERSEDAKK 451
Cdd:PTZ00322 606 PQNAYkIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQSRTGLVTK 653
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
245-420 1.86e-44

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 223483 [Multi-domain]  Cd Length: 208  Bit Score: 155.72  E-value: 1.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 245 QPRTIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAE----ALRLPYEQW 318
Cdd:COG0406    1 MMMRLYLVRHGETEWNVEGRLQGwtDSPLTEEGRAQAEALAERLAARDIGFDAIYSSPLKRAQQTAEplaeELGLPLEVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 319 KALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLRCL 395
Cdd:COG0406   81 DRLREIDFGDWEGLTIDELAEEPPEELAAWLADPYLAPPPGGESLADVSKRVVAALAELLRSppgNNVLVVSHGGVIRAL 160
                        170       180
                 ....*....|....*....|....*
gi 295293217 396 LAYFLDKSAEEMPYLKCPLHTVLKL 420
Cdd:COG0406  161 LAYLLGLDLEELWRLRLDNASVTVL 185
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
248-395 1.74e-36

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: 132.58  E-value: 1.74e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217   248 TIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFV-EEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWkALNEI 324
Cdd:smart00855   1 RLYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLaSLLLPRFDVVYSSPLKRARQTAEALAIALGLP-GLRER 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295293217   325 DAGVCEELTYEEIRDTYPEEYA---LREQDKYYYRYPTGESYQDLVQRLEPVIMELERQ-----ENVLVICHQAVLRCL 395
Cdd:smart00855  80 DFGAWEGLTWDEIAAKYPEEYLaawRDPYDPAPPAPPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
248-434 2.94e-32

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: 120.89  E-value: 2.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 248 TIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEALR-----LPYEQWKA 320
Cdd:cd07067    1 RLYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIILeelpgLPVEVDPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 321 LNEidagvceeltyeeirdtypeeyalreqdkyyyryptgesyqdlvQRLEPVIMELERQ---ENVLVICHQAVLRCLLA 397
Cdd:cd07067   81 LRE--------------------------------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLA 116
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 295293217 398 YFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYL 434
Cdd:cd07067  117 YLLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
249-427 4.28e-27

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: 107.32  E-value: 4.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  249 IYLCRHGENEYNLQGKIG-GDSGLSSRGKKFANALSkfveeQNLKDL---RVWTSQLKSTIQTAEAL----RLPYEQWKA 320
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALR-----EKLADVpfdAVYSSPLSRCRELAEILaerrGLPIIKDDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  321 LNEIDAGVCEELTYEEIRDTYPeEYALREQDKYYYRYPTGESYQDLVQRLEPV---IMELERQENVLVICHQAVLRCLLA 397
Cdd:TIGR03162  76 LREMDFGDWEGRSWDEIPEAYP-ELDAWAADWQHARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRALLA 154
                         170       180       190
                  ....*....|....*....|....*....|
gi 295293217  398 YFLDKSAEEMPYLkcplhtvlkltPVAYGC 427
Cdd:TIGR03162 155 HLLGLPLEQWWSF-----------AVEYGS 173
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
248-421 2.97e-22

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: 92.86  E-value: 2.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 248 TIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEID 325
Cdd:cd07040    1 VLYLVRHGEREPNAEGRFTGwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEVDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 326 AgvceeltyeeirdtypeeyalreqdkyyyryptgesyqdlvQRLEPVIMELERQ-----ENVLVICHQAVLRCLLAYFL 400
Cdd:cd07040   81 R-----------------------------------------ARVLNALLELLARhlldgKNVLIVSHGGTIRALLAALL 119
                        170       180
                 ....*....|....*....|.
gi 295293217 401 DKSAEEMPYLKCPLHTVLKLT 421
Cdd:cd07040  120 GLSDEEILSLNLPNGSILVLE 140
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism];
247-406 8.31e-15

Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism];


Pssm-ID: 223661  Cd Length: 230  Bit Score: 73.85  E-value: 8.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 247 RTIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTA-----EALRL---PYE 316
Cdd:COG0588    2 MKLVLLRHGQSEWNKENLFTGwvDVDLTEKGISEAKAAGKLLKEEGLEFDIAYTSVLKRAIKTLnivleESDQLwipVIK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 317 QWKaLNEIDAGVCEELTYEEIRDTYPEEY-------------ALREQDKYY------YRY------PTGESYQDLVQRLE 371
Cdd:COG0588   82 SWR-LNERHYGALQGLNKAETAAKYGEEQvliwrrsydipppKLEKDDERSphrdrrYAHldigglPLTESLKDTVERVL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 295293217 372 P----VIM-ELERQENVLVICHQAVLRCLLAYFLDKSAEE 406
Cdd:COG0588  161 PywedDIApNLKSGKNVLIVAHGNSLRALIKYLEGISDED 200
PRK13463 PRK13463
phosphoserine phosphatase 1;
248-399 8.37e-15

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 73.16  E-value: 8.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 248 TIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSkfveeQNLKDLR---VWTSQLKSTIQTAEALR----LPYEQW 318
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLG-----ERMKDLSihaIYSSPSERTLHTAELIKgerdIPIIAD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 319 KALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQR-LEPVIMELERQ--ENVLVICHQAVLRCL 395
Cdd:PRK13463  79 EHFYEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHkgESILIVSHAAAAKLL 158

                 ....
gi 295293217 396 LAYF 399
Cdd:PRK13463 159 VGHF 162
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
249-407 1.54e-14

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 72.39  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 249 IYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVeeQNLKDLRVWTSQLKSTIQTAE----ALRLPYEQWKALN 322
Cdd:PRK15004   3 LWLVRHGETQANVDGLYSGhaPTPLTARGIEQAQNLHTLL--RDVPFDLVLCSELERAQHTARlvlsDRQLPVHIIPELN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 323 EIDAGVCE-----ELTYEEirdtyPEEYALREQDkYYYRYPT-GESYQDLVQRLEPVIMEL---ERQENVLVICHQAVLR 393
Cdd:PRK15004  81 EMFFGDWEmrhhrDLMQED-----AENYAAWCND-WQHAIPTnGEGFQAFSQRVERFIARLsafQHYQNLLIVSHQGVLS 154
                        170
                 ....*....|....
gi 295293217 394 CLLAYFLDKSAEEM 407
Cdd:PRK15004 155 LLIARLLGMPAEAM 168
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
245-405 5.99e-11

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 64.23  E-value: 5.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 245 QPRTIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLrVWTSQLKSTIQTA----EALRLPYEQW 318
Cdd:PRK07238 170 TPTRLLLLRHGQTELSVQRRYSGrgNPELTEVGRRQAAAAARYLAARGGIDA-VVSSPLQRARDTAaaaaKALGLDVTVD 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 319 KALNEIDAGVCEELTYEEIRDTYPEEYA--LREQDkyyYRYPTGESYQDLVQRLEPVIMELERQ---ENVLVICHQAVLR 393
Cdd:PRK07238 249 DDLIETDFGAWEGLTFAEAAERDPELHRawLADTS---VAPPGGESFDAVARRVRRARDRLIAEypgATVLVVSHVTPIK 325
                        170
                 ....*....|..
gi 295293217 394 CLLAYFLDKSAE 405
Cdd:PRK07238 326 TLLRLALDAGPG 337
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
249-400 1.60e-10

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 60.90  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 249 IYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKdlRVWTSQLKSTIQTAE----ALRLPYEQWKALN 322
Cdd:PRK03482   4 VYLVRHGETQWNAERRIQGqsDSPLTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAEiiaqACGCDIIFDPRLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 323 EIDAGVCEEltyEEIRDTYPEEYALREQ------DKyyyRYPTGESYQDLVQRLEPVI---MELERQENVLVICHQAVLR 393
Cdd:PRK03482  82 ELNMGVLEK---RHIDSLTEEEEGWRRQlvngtvDG---RIPEGESMQELSDRMHAALescLELPQGSRPLLVSHGIALG 155

                 ....*..
gi 295293217 394 CLLAYFL 400
Cdd:PRK03482 156 CLVSTIL 162
PRK01295 PRK01295
phosphoglyceromutase; Provisional
246-408 1.13e-08

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 55.08  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 246 PRTIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEAL-------RLPYE 316
Cdd:PRK01295   2 SRTLVLVRHGQSEWNLKNLFTGwrDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCQLIleelgqpGLETI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 317 QWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIME-----LERQENVLVICHQAV 391
Cdd:PRK01295  82 RDQALNERDYGDLSGLNKDDARAKWGEEQVHIWRRSYDVPPPGGESLKDTGARVLPYYLQeilprVLRGERVLVAAHGNS 161
                        170
                 ....*....|....*...
gi 295293217 392 LRCLLAyFLDK-SAEEMP 408
Cdd:PRK01295 162 LRALVM-VLDGlTPEQIL 178
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
259-413 4.44e-08

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 53.89  E-value: 4.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 259 YNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTA----EALRLPY----EQWKaLNEIDAGV 328
Cdd:PTZ00123   1 WNKENRFTGwtDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAwivlEELGQLHvpviKSWR-LNERHYGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 329 CEELTYEEIRDTYPEE--------Y-----ALREQDKYY----YRY--------PTGESYQDLVQRLEP-----VIMELE 378
Cdd:PTZ00123  80 LQGLNKSETAEKHGEEqvkiwrrsYdipppPLEKSDERYpgndPVYkdipkdalPNTECLKDTVERVLPywedhIAPDIL 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 295293217 379 RQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCP 413
Cdd:PTZ00123 160 AGKKVLVAAHGNSLRALVKYLDKMSEEDILELNIP 194
gpmA PRK14119
phosphoglyceromutase; Provisional
246-407 4.61e-08

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 53.74  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 246 PRTIyLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQT-------AEALRLP-Y 315
Cdd:PRK14119   2 PKLI-LCRHGQSEWNAKNLFTGweDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTthyilteSKQQWIPvY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 316 EQWKaLNEIDAGVCEELTYEEIRDTYPEE--------YALR------EQDKYY-----YRY------PTGESYQDLVQRL 370
Cdd:PRK14119  81 KSWR-LNERHYGGLQGLNKDDARKEFGEEqvhiwrrsYDVKppaeteEQREAYladrrYNHldkrmmPYSESLKDTLVRV 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 295293217 371 EP-----VIMELERQENVLVICHQAVLRCLLAYFLDKSAEEM 407
Cdd:PRK14119 160 IPfwtdhISQYLLDGQTVLVSAHGNSIRALIKYLEDVSDEDI 201
gpmA PRK14120
phosphoglyceromutase; Provisional
246-413 3.26e-07

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 51.58  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 246 PRTIYLCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTA-----EALRL--PYE 316
Cdd:PRK14120   4 TYTLVLLRHGESEWNAKNLFTGwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTAnlaldAADRLwiPVR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 317 Q-WKaLNEIDAGVCEELTYEEIRDTYPEE--------YA-----LREQDKYYY----RY------PTGESYQDLVQRLEP 372
Cdd:PRK14120  84 RsWR-LNERHYGALQGKDKAETKAEYGEEqfmlwrrsYDtppppIEDGSEYSQdndpRYadlgvgPRTECLKDVVARFLP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 295293217 373 -----VIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCP 413
Cdd:PRK14120 163 yweddIVPDLKAGKTVLIAAHGNSLRALVKHLDGISDEDIAGLNIP 208
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
247-336 2.82e-06

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 224973  Cd Length: 163  Bit Score: 47.29  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 247 RTIYLCRHGENEYNLQGKIGGDSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRlpyeqwKALNEIDA 326
Cdd:COG2062    2 MRLYLMRHGKAEWAAPGIADFDRPLTERGRKEAELVAAWLAGQGVEPDLVLVSPAVRARQTAEIVA------EHLGEKKV 75
                         90
                 ....*....|
gi 295293217 327 GVCEELTYEE 336
Cdd:COG2062   76 EVFEELLPNG 85
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
251-407 4.50e-05

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 44.90  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 251 LCRHGENEYNLQGKIGG--DSGLSSRGKKFANALSKFVEEQNLKDLRVWTSQLKSTIQT-------AEALRLP-YEQWKa 320
Cdd:PRK14116   6 LIRHGQSEWNLSNQFTGwvDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTlhyaleeSDQLWIPeTKTWR- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217 321 LNEIDAGVCEELTYEEIRDTYPEEY-------------ALREQDKYYY----RY--------PTGESYQDLVQRLEP--- 372
Cdd:PRK14116  85 LNERHYGALQGLNKKETAEKYGDEQvhiwrrsydvlppLLDADDEGSAakdrRYanldpriiPGGENLKVTLERVIPfwe 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 295293217 373 --VIMELERQENVLVICHQAVLRCLLAYFLDKSAEEM 407
Cdd:PRK14116 165 dhIAPDLLDGKNVIIAAHGNSLRALTKYIENISDEDI 201
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteristic of the ...
37-147 1.41e-04

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


Pssm-ID: 433395 [Multi-domain]  Cd Length: 143  Bit Score: 41.91  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217   37 VIVMVGLPARGKTYISKKLTRYLNWIGVptkvfNVGEYRR----EAVKQYSSYNFFRPDNEEAMRVRKQCALAALRDVks 112
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAVRL-----SSDAERKrlfgEGRPSISYYTDATDLTYQRLHELARIALRAGRPV-- 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 295293217  113 yltkeggqiaVFDATNTTRERRHMILNFAKENDFK 147
Cdd:pfam13671  74 ----------ILDATNLRRAERARLLALAREYGVP 98
COG4639 COG4639
Predicted kinase [General function prediction only];
36-152 6.16e-03

Predicted kinase [General function prediction only];


Pssm-ID: 226986 [Multi-domain]  Cd Length: 168  Bit Score: 37.83  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295293217  36 TVIVMVGLPARGK-TYISKKLtrylnwigVPTKVFNVGEYRREAVKQYSSYNFFRPDneeamrvrkqcaLAALRDVKSYL 114
Cdd:COG4639    3 ILVVLRGASGSGKsTFAKENF--------LQNYVLSLDDLRLLLGVSASKENSQKND------------ELVWDILYKQL 62
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 295293217 115 TK--EGGQIAVFDATNTTRERRHMILNFAKENDFKAFFIE 152
Cdd:COG4639   63 EQrlRRGKFTIIDATNLRREDRRKLIDLAKAYGYKIYAIV 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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