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Conserved domains on  [gi|569011805|ref|XP_006528819|]
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 isoform X4 [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, ...
 30-251 4.80e-141

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: 399.40  E-value: 4.80e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805   30 RRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAV-SYRNYEFFRPDNMEAQLIRKQC 108
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVkAYSNYEFFRPDNPEAMKIREQC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  109 ALAALKDVHKYLSREEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPDIIAENIKQVKLGSPDYIDCDQEK 188
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569011805  189 VLEDFLKRIECYEINYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHVQSRTAYYLMNIHVTP 251
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 254-366 2.37e-35

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: 127.71  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 569011805  328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGE 366
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGE 117
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 30-251 4.80e-141

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: 399.40  E-value: 4.80e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805   30 RRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAV-SYRNYEFFRPDNMEAQLIRKQC 108
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVkAYSNYEFFRPDNPEAMKIREQC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  109 ALAALKDVHKYLSREEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPDIIAENIKQVKLGSPDYIDCDQEK 188
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569011805  189 VLEDFLKRIECYEINYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHVQSRTAYYLMNIHVTP 251
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 33-366 7.31e-44

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 160.83  E-value: 7.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  33 SSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREaVSYRNYEFFRPDNMEAQLIRKQCALAa 112
Cdd:PTZ00322 206 SAVPQPMMGSLIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRR-LERRGGAVSSPTGAAEVEFRIAKAIA- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 113 lKDVHKYLSREEGhVAVFDATNTTRERRSLILQFAKEHGY----KVFFIESICNDPDIIAENI---KQVKLGSPdyidcd 185
Cdd:PTZ00322 284 -HDMTTFICKTDG-VAVLDGTNTTHARRMALLRAIRETGLirmtRVVFVEVVNNNSETIRRNVlraKEMFPGAP------ 355

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 186 qEKVLEDFLKRIECYEINYQPLDEELDSHLSYIKIFDvGTRYMVNRVQDHVQSRTAYYLMNIHVTPRSIYLCRHGESELN 265
Cdd:PTZ00322 356 -EDFVDRYYEVIEQLEAVYKSLNPVTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDL 433

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 266 LRGRIGGDSGLSARGKQYAYALANFIRSQ-SISSLKVWTSHMKRTIQTAE---------------------ALGVPYEQW 323
Cdd:PTZ00322 434 LSGRIGGNSRLTERGRAYSRALFEYFQKEiSTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYF 513

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 569011805 324 KALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGE 366
Cdd:PTZ00322 514 PTLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGE 556
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 254-366 2.37e-35

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: 127.71  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 569011805  328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGE 366
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGE 117
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
254-366 2.02e-30

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 115.04  E-value: 2.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAEAL----GVPYEQWKALN 327
Cdd:COG0406    4 LYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALaealGLPVEVDPRLR 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 569011805 328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGE 366
Cdd:COG0406   82 EIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGE 120
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 254-363 1.71e-25

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: 100.61  E-value: 1.71e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805   254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQS-ISSLKVWTSHMKRTIQTAEALGVPYEQWkALNEID 330
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALGLP-GLRERD 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 569011805   331 AGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYP 363
Cdd:smart00855  81 FGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPP 113
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 254-328 1.28e-22

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: 92.77  E-value: 1.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAEAL-----GVPYEQWKAL 326
Cdd:cd07067    2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIIleelpGLPVEVDPRL 81


                 ..
gi 569011805 327 NE 328
Cdd:cd07067   82 RE 83
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 254-366 1.84e-16

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: 76.51  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  254 IYLCRHGESELNLRGRIG-GDSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAEALG----VPYEQWKALNE 328
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILAerrgLPIIKDDRLRE 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569011805  329 IDAGVCEEMTYEEIQEHYPeEFALRDQDKYRYRYPKGE 366
Cdd:TIGR03162  79 MDFGDWEGRSWDEIPEAYP-ELDAWAADWQHARPPGGE 115
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
254-366 8.04e-11

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 61.28  E-value: 8.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:PRK03482   4 VYLVRHGETQWNAERRIQGqsDSPLTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAEiiaqACGCDIIFDPRLR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 569011805 328 EIDAGVCEEmtyEEIQEHYPEEFALRDQ---DKYRYRYPKGE 366
Cdd:PRK03482  82 ELNMGVLEK---RHIDSLTEEEEGWRRQlvnGTVDGRIPEGE 120
COG4639 COG4639
Predicted kinase [General function prediction only];
42-154 1.66e-08

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 52.91  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  42 PTMVIMVGLPARGKtyiSTKLTRYLnwigTPTKVFNLGQYRREAvsyrnyeFFRPDNMEAQLIrkqcALAALKD-VHKYL 120
Cdd:COG4639    2 LSLVVLIGLPGSGK---STFARRLF----APTEVVSSDDIRALL-------GGDENDQSAWGD----VFQLAHEiARARL 63

                         90       100       110
                 ....*....|....*....|....*....|....
gi 569011805 121 srEEGHVAVFDATNTTRERRSLILQFAKEHGYKV 154
Cdd:COG4639   64 --RAGRLTVVDATNLQREARRRLLALARAYGALV 95
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 114-180 9.31e-03

monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 37.25  E-value: 9.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569011805 114 KDVHKYLSREEGHVAVFDAT---NTTRERRSLILQFAKEHGYKVFFIESIC-NDPDIIAENIKQVKLGSPD 180
Cdd:cd19965  115 KRIAEKFKPGGGHVLLGISTpgqSALEQRLDGIKQALKEYGRGITYDVIDTgTDLAEALSRIEAYYTAHPD 185
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 30-251 4.80e-141

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: 399.40  E-value: 4.80e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805   30 RRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAV-SYRNYEFFRPDNMEAQLIRKQC 108
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVkAYSNYEFFRPDNPEAMKIREQC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  109 ALAALKDVHKYLSREEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPDIIAENIKQVKLGSPDYIDCDQEK 188
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569011805  189 VLEDFLKRIECYEINYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHVQSRTAYYLMNIHVTP 251
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 33-366 7.31e-44

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 160.83  E-value: 7.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  33 SSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREaVSYRNYEFFRPDNMEAQLIRKQCALAa 112
Cdd:PTZ00322 206 SAVPQPMMGSLIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRR-LERRGGAVSSPTGAAEVEFRIAKAIA- 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 113 lKDVHKYLSREEGhVAVFDATNTTRERRSLILQFAKEHGY----KVFFIESICNDPDIIAENI---KQVKLGSPdyidcd 185
Cdd:PTZ00322 284 -HDMTTFICKTDG-VAVLDGTNTTHARRMALLRAIRETGLirmtRVVFVEVVNNNSETIRRNVlraKEMFPGAP------ 355

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 186 qEKVLEDFLKRIECYEINYQPLDEELDSHLSYIKIFDvGTRYMVNRVQDHVQSRTAYYLMNIHVTPRSIYLCRHGESELN 265
Cdd:PTZ00322 356 -EDFVDRYYEVIEQLEAVYKSLNPVTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDL 433

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 266 LRGRIGGDSGLSARGKQYAYALANFIRSQ-SISSLKVWTSHMKRTIQTAE---------------------ALGVPYEQW 323
Cdd:PTZ00322 434 LSGRIGGNSRLTERGRAYSRALFEYFQKEiSTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRVLYF 513

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 569011805 324 KALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGE 366
Cdd:PTZ00322 514 PTLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGE 556
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
 254-366 2.37e-35

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: 127.71  E-value: 2.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 569011805  328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGE 366
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGE 117
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
254-366 2.02e-30

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 115.04  E-value: 2.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAEAL----GVPYEQWKALN 327
Cdd:COG0406    4 LYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALaealGLPVEVDPRLR 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 569011805 328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGE 366
Cdd:COG0406   82 EIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGE 120
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
 254-363 1.71e-25

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: 100.61  E-value: 1.71e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805   254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQS-ISSLKVWTSHMKRTIQTAEALGVPYEQWkALNEID 330
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALGLP-GLRERD 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 569011805   331 AGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYP 363
Cdd:smart00855  81 FGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPP 113
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
 254-328 1.28e-22

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: 92.77  E-value: 1.28e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAEAL-----GVPYEQWKAL 326
Cdd:cd07067    2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIIleelpGLPVEVDPRL 81


                 ..
gi 569011805 327 NE 328
Cdd:cd07067   82 RE 83
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
 254-349 1.45e-18

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: 81.69  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEIDA 331
Cdd:cd07040    2 LYLVRHGEREPNAEGRFTGwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEVDPR 81

                         90
                 ....*....|....*...
gi 569011805 332 GVCEEMTYEEIQEHYPEE 349
Cdd:cd07040   82 ARVLNALLELLARHLLDG 99
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
 254-366 1.84e-16

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: 76.51  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  254 IYLCRHGESELNLRGRIG-GDSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAEALG----VPYEQWKALNE 328
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALREKLADVPFD--AVYSSPLSRCRELAEILAerrgLPIIKDDRLRE 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569011805  329 IDAGVCEEMTYEEIQEHYPeEFALRDQDKYRYRYPKGE 366
Cdd:TIGR03162  79 MDFGDWEGRSWDEIPEAYP-ELDAWAADWQHARPPGGE 115
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 44-198 3.50e-11

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: 60.40  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805   44 MVIMVGLPARGKTYISTKLTRYLNW--IGTPTKVFNLGQYRREAVSYRNYEFFRPDNMEAQLIRKqcALAALKDVhkyls 121
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAvrLSSDDERKRLFGEGRPSISYYTDATDRTYERLHELARI--ALRAGRPV----- 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569011805  122 reeghvaVFDATNTTRERRSLILQFAKEHGYKVFFIEsICNDPDIIAENIKQVKLGSPDYIDCDqEKVLEDFLKRIE 198
Cdd:pfam13671  74 -------ILDATNLRRDERARLLALAREYGVPVRIVV-FEAPEEVLRERLAARARAGGDPSDVP-EEVLDRQKARFE 141
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
254-366 8.04e-11

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 61.28  E-value: 8.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:PRK03482   4 VYLVRHGETQWNAERRIQGqsDSPLTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAEiiaqACGCDIIFDPRLR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 569011805 328 EIDAGVCEEmtyEEIQEHYPEEFALRDQ---DKYRYRYPKGE 366
Cdd:PRK03482  82 ELNMGVLEK---RHIDSLTEEEEGWRRQlvnGTVDGRIPEGE 120
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
 250-354 1.17e-10

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 62.30  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 250 TPRSIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQS-ISSlkVWTSHMKRTIQTA----EALGVPYEQ 322
Cdd:PRK07238 170 TPTRLLLLRHGQTELSVQRRYSGrgNPELTEVGRRQAAAAARYLAARGgIDA--VVSSPLQRARDTAaaaaKALGLDVTV 247

                         90       100       110
                 ....*....|....*....|....*....|....
gi 569011805 323 WKALNEIDAGVCEEMTYEEIQEHYPEEFA--LRD 354
Cdd:PRK07238 248 DDDLIETDFGAWEGLTFAEAAERDPELHRawLAD 281
PRK13463 PRK13463
phosphoserine phosphatase 1;
253-366 2.29e-10

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 59.68  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 253 SIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSlkVWTSHMKRTIQTAEAL----GVPYEQWKAL 326
Cdd:PRK13463   4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLGERMKDLSIHA--IYSSPSERTLHTAELIkgerDIPIIADEHF 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 569011805 327 NEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGE 366
Cdd:PRK13463  82 YEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGE 121
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
254-332 6.01e-09

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 54.50  E-value: 6.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAEALG------VPYEQWKALN 327
Cdd:COG2062    1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILAealglpPKVEVEDELY 80


                 ....*
gi 569011805 328 EIDAG 332
Cdd:COG2062   81 DADPE 85
COG4639 COG4639
Predicted kinase [General function prediction only];
42-154 1.66e-08

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 52.91  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  42 PTMVIMVGLPARGKtyiSTKLTRYLnwigTPTKVFNLGQYRREAvsyrnyeFFRPDNMEAQLIrkqcALAALKD-VHKYL 120
Cdd:COG4639    2 LSLVVLIGLPGSGK---STFARRLF----APTEVVSSDDIRALL-------GGDENDQSAWGD----VFQLAHEiARARL 63

                         90       100       110
                 ....*....|....*....|....*....|....
gi 569011805 121 srEEGHVAVFDATNTTRERRSLILQFAKEHGYKV 154
Cdd:COG4639   64 --RAGRLTVVDATNLQREARRRLLALARAYGALV 95
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
254-351 3.08e-07

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 50.43  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:PRK15004   3 LWLVRHGETQANVDGLYSGhaPTPLTARGIEQAQNLHTLLRDVPFD--LVLCSELERAQHTARlvlsDRQLPVHIIPELN 80

                         90       100
                 ....*....|....*....|....
gi 569011805 328 EIDAGVCEEMTYEEIQEHYPEEFA 351
Cdd:PRK15004  81 EMFFGDWEMRHHRDLMQEDAENYA 104
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
 256-328 4.18e-05

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


Pssm-ID: 440353  Cd Length: 229  Bit Score: 44.30  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTA----EALG---VP-YEQWKa 325
Cdd:COG0588    5 LLRHGESEWNLENRFTGwtDVDLSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLwivlDEMDrlwIPvEKSWR- 83


                 ...
gi 569011805 326 LNE 328
Cdd:COG0588   84 LNE 86
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
256-349 1.55e-04

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 42.59  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQT-------AEALGVP-YEQWKa 325
Cdd:PRK14116   6 LIRHGQSEWNLSNQFTGwvDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTlhyaleeSDQLWIPeTKTWR- 84

                         90       100
                 ....*....|....*....|....
gi 569011805 326 LNEIDAGVCEEMTYEEIQEHYPEE 349
Cdd:PRK14116  85 LNERHYGALQGLNKKETAEKYGDE 108
gpmA PRK14117
phosphoglyceromutase; Provisional
 258-349 1.55e-04

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 42.70  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 258 RHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQT-------AEALGVPYEQWKALNE 328
Cdd:PRK14117   8 RHGESEWNKANLFTGwaDVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTtnlaleaSDQLWVPVEKSWRLNE 87

                         90       100
                 ....*....|....*....|.
gi 569011805 329 IDAGVCEEMTYEEIQEHYPEE 349
Cdd:PRK14117  88 RHYGGLTGKNKAEAAEQFGDE 108
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 41-157 5.37e-04

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


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 40.48  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805  41 SPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAVSyrnyEFFrPDNMEAQLIRkqcalaalkDVHKYL 120
Cdd:COG4088    3 SPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVN----ESF-PKETYEEVVE---------DVRTTT 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 569011805 121 SREE---GHVAVFDATNTTRERRSLILQFAKeHGYKVFFI 157
Cdd:COG4088   69 ADNAldnGYSVIVDGTFYYRSWQRDFRNLAK-HKAPIHII 107
PRK13462 PRK13462
acid phosphatase; Provisional
 256-348 1.33e-03

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 39.43  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAEALGVPY-EQWKALNEIDAG 332
Cdd:PRK13462  10 LLRHGETEWSKSGRHTGrtELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKLAGLTVdEVSGLLAEWDYG 89

                         90
                 ....*....|....*.
gi 569011805 333 VCEEMTYEEIQEHYPE 348
Cdd:PRK13462  90 SYEGLTTPQIRESEPD 105
gpmA PRK14119
phosphoglyceromutase; Provisional
 256-367 2.18e-03

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 39.10  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQT-------AEALGVP-YEQWKa 325
Cdd:PRK14119   6 LCRHGQSEWNAKNLFTGweDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTthyilteSKQQWIPvYKSWR- 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 569011805 326 LNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGEE 367
Cdd:PRK14119  85 LNERHYGGLQGLNKDDARKEFGEEQVHIWRRSYDVKPPAETE 126
PRK01295 PRK01295
phosphoglyceromutase; Provisional
 251-332 2.79e-03

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 38.52  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 251 PRSIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTA----EALG---VPYE 321
Cdd:PRK01295   2 SRTLVLVRHGQSEWNLKNLFTGwrDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCqlilEELGqpgLETI 81

                         90
                 ....*....|.
gi 569011805 322 QWKALNEIDAG 332
Cdd:PRK01295  82 RDQALNERDYG 92
gpmA PRK14120
phosphoglyceromutase; Provisional
 250-349 2.86e-03

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 38.87  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805 250 TPRSIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAE-ALG------VPY 320
Cdd:PRK14120   3 MTYTLVLLRHGESEWNAKNLFTGwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTANlALDaadrlwIPV 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 569011805 321 EQ-WKaLNEIDAGVCEEMTYEEIQEHYPEE 349
Cdd:PRK14120  83 RRsWR-LNERHYGALQGKDKAETKAEYGEE 111
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
 254-317 3.82e-03

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 37.51  E-value: 3.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569011805  254 IYLCRHGESElnLRGRIGGDSGLSARGKQYAYALANFIRSQSISSLKVWTSHMKRTIQTAEALG 317
Cdd:TIGR00249   3 LFIMRHGDAA--LDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVG 64
Zeta_toxin pfam06414
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...
 41-154 8.83e-03

Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.


Pssm-ID: 428926  Cd Length: 192  Bit Score: 36.96  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011805   41 SPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTkVFNLGQYR---------REAVSYRNYEFFRPDNmeAQLIRKQCALA 111
Cdd:pfam06414  10 RPKAILLGGQPGAGKTELARALLDELGRQGNVV-RIDPDDFRelhphyrelQAADPKTASEYTQPDA--SRWVEKLLQHA 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 569011805  112 alkdvhkylsREEGHVAVFDATNTTRERRSLILQFAKEHGYKV 154
Cdd:pfam06414  87 ----------IENGYNIILEGTLRSPDVAKKIARALKAAGYRV 119
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 114-180 9.31e-03

monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 37.25  E-value: 9.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569011805 114 KDVHKYLSREEGHVAVFDAT---NTTRERRSLILQFAKEHGYKVFFIESIC-NDPDIIAENIKQVKLGSPD 180
Cdd:cd19965  115 KRIAEKFKPGGGHVLLGISTpgqSALEQRLDGIKQALKEYGRGITYDVIDTgTDLAEALSRIEAYYTAHPD 185
 
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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