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Conserved domains on  [gi|1016711777|ref|XP_016076096|]
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PREDICTED: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 isoform X4 [Miniopterus natalensis]

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 1.76e-138

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: 397.09  E-value: 1.76e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  30 RRGSTIPQFTNSPTMVIMVGLPARGKTYISSKLTRYLNWIGTPTKVFNLGQYRREAV-SYKNYEFFLPDNTEAQLIRKRF 108
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVkAYSNYEFFRPDNPEAMKIREQC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 109 ALAALKDVHDYLSHGEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPDYIDCDREK 188
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016711777 189 VLEDFLKRIECYELNYQPLDDELDSHLSYIKIFDVGTRYMVNRVQDHIQSRTVYYLMNIHVTP 251
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
254-440 2.47e-55

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: 182.79  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQ---ENVLVICHQAVMRCLLAYF 404
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 405 LDKSSDELPYLKCPLHTVLKLTPVAYGCKVESIYLN 440
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, ...
30-251 1.76e-138

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: 397.09  E-value: 1.76e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  30 RRGSTIPQFTNSPTMVIMVGLPARGKTYISSKLTRYLNWIGTPTKVFNLGQYRREAV-SYKNYEFFLPDNTEAQLIRKRF 108
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVkAYSNYEFFRPDNPEAMKIREQC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 109 ALAALKDVHDYLSHGEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPDYIDCDREK 188
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016711777 189 VLEDFLKRIECYELNYQPLDDELDSHLSYIKIFDVGTRYMVNRVQDHIQSRTVYYLMNIHVTP 251
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
254-440 2.47e-55

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: 182.79  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQ---ENVLVICHQAVMRCLLAYF 404
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 405 LDKSSDELPYLKCPLHTVLKLTPVAYGCKVESIYLN 440
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
33-454 7.65e-48

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 174.70  E-value: 7.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  33 STIPQFTNSPTMVIMVGLPARGKTYISSKLTRYLNWIGTPTKVFNLGQYRRE------AVSyknyefflpDNTEAQLIRK 106
Cdd:PTZ00322  206 SAVPQPMMGSLIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRlerrggAVS---------SPTGAAEVEF 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 107 RFALAALKDVHDYLSHGEGhVAVFDATNTTRERRSLILQFAKEHGY----KVFFIESICNDPGIIAENIRQVKLGSPDyi 182
Cdd:PTZ00322  277 RIAKAIAHDMTTFICKTDG-VAVLDGTNTTHARRMALLRAIRETGLirmtRVVFVEVVNNNSETIRRNVLRAKEMFPG-- 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 183 dcDREKVLEDFLKRIECYELNYQPLDDELDSHLSYIKIFDvGTRYMVNRVQDHIQSRTVYYLMNIHVTPRSIYLCRHGES 262
Cdd:PTZ00322  354 --APEDFVDRYYEVIEQLEAVYKSLNPVTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEY 430
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 263 ELNLRGRIGGDSGLSARGKQYAYALANFIQSQ-GISSLKVWTSHMKRTIQTAE---------------------ALGVPY 320
Cdd:PTZ00322  431 VDLLSGRIGGNSRLTERGRAYSRALFEYFQKEiSTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRV 510
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 321 EQWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQ-RLEPVIMELE-RQENVLVICHQAVMR 398
Cdd:PTZ00322  511 LYFPTLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGECIHQVFNaRLEPHIHDIQaSTTPVLVVSHLHLLQ 590
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016711777 399 CLLAYFLDKSSDELP-----YLKCPLHTVLKLTPVAYGCKVESIYLNVEAVNTHREKPENV 454
Cdd:PTZ00322  591 GLYSYFVTDGDNIVApqnayKIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQSRTGLV 651
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
254-418 3.45e-46

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 158.95  E-value: 3.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISslKVWTSHMKRTIQTAEAL----GVPYEQWKALN 327
Cdd:COG0406     4 LYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALaealGLPVEVDPRLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQ---ENVLVICHQAVMRCLLAYF 404
Cdd:COG0406    82 EIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARhpgGTVLVVTHGGVIRALLAHL 161
                         170
                  ....*....|....
gi 1016711777 405 LDKSSDELPYLKCP 418
Cdd:COG0406   162 LGLPLEAFWRLRID 175
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
254-400 1.04e-38

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: 137.98  E-value: 1.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQG-ISSLKVWTSHMKRTIQTAEALGVPYEQWkALNEID 330
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALGLP-GLRERD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016711777  331 AGVCEEMTYEEIQEHYPEEFALRDQDKYRYRY---PKGESYEDLVQRLEPVIMELERQ-----ENVLVICHQAVMRCL 400
Cdd:smart00855  81 FGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPpapPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
254-439 1.28e-35

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: 129.36  E-value: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEAL-----GVPYEQWKAL 326
Cdd:cd07067     2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIIleelpGLPVEVDPRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 327 NEidagvceemtyeeiqehypeefalrdqdkyryrypkgesyedlvQRLEPVIMELERQ---ENVLVICHQAVMRCLLAY 403
Cdd:cd07067    82 RE--------------------------------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLAY 117
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 404 FLDKSSDELPYLKCPLHTVLKLTPVAYGCKVESIYL 439
Cdd:cd07067   118 LLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
254-432 2.08e-30

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 116.18  E-value: 2.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIG-GDSGLSARGKQYAYALANfiQSQGISSLKVWTSHMKRTIQTAEALG----VPYEQWKALNE 328
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALRE--KLADVPFDAVYSSPLSRCRELAEILAerrgLPIIKDDRLRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 329 IDAGVCEEMTYEEIQEHYPeEFALRDQDKYRYRYPKGESYEDLVQRLEPV---IMELERQENVLVICHQAVMRCLLAYFL 405
Cdd:TIGR03162  79 MDFGDWEGRSWDEIPEAYP-ELDAWAADWQHARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRALLAHLL 157
                         170       180
                  ....*....|....*....|....*..
gi 1016711777 406 DKSSDELPYLkcplhtvlkltPVAYGC 432
Cdd:TIGR03162 158 GLPLEQWWSF-----------AVEYGS 173
PRK13463 PRK13463
phosphoserine phosphatase 1;
253-404 4.45e-16

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 76.63  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 253 SIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSlkVWTSHMKRTIQTAEAL----GVPYEQWKAL 326
Cdd:PRK13463    4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLGERMKDLSIHA--IYSSPSERTLHTAELIkgerDIPIIADEHF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 327 NEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQR-LEPVIMELERQ--ENVLVICHQAVMRCLLAY 403
Cdd:PRK13463   82 YEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHkgESILIVSHAAAAKLLVGH 161

                  .
gi 1016711777 404 F 404
Cdd:PRK13463  162 F 162
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
44-215 1.17e-07

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 51.45  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  44 MVIMVGLPARGKTYISSKLTRYLNWIgtptkvfnlgQYRREAVSYKNYEFFLPDNTEAQLIRKR-----FALAAlkdvhD 118
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLGAV----------RLRSDVVRKRLFGAGLAPLERSPEATARtyarlLALAR-----E 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 119 YLSHgeGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICnDPGIIAENI--RQVKLGSPDYidcdREKVLEDFLKR 196
Cdd:COG0645    66 LLAA--GRSVILDATFLRRAQREAFRALAEEAGAPFVLIWLDA-PEEVLRERLeaRNAEGGDSDA----TWEVLERQLAF 138
                         170
                  ....*....|....*....
gi 1016711777 197 iecyelnYQPLDDELDSHL 215
Cdd:COG0645   139 -------EEPLTEDEGFLL 150
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
38-105 9.85e-03

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 37.06  E-value: 9.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016711777  38 FTNSPTMVIMVGLPARGKTYISSKLTRYLNWIGTPTKVFNLgqyrrEAVSYKNYEFFLPDNTEAQLIR 105
Cdd:cd04149     5 FGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNV-----ETVTYKNVKFNVWDVGGQDKIR 67
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
30-251 1.76e-138

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: 397.09  E-value: 1.76e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  30 RRGSTIPQFTNSPTMVIMVGLPARGKTYISSKLTRYLNWIGTPTKVFNLGQYRREAV-SYKNYEFFLPDNTEAQLIRKRF 108
Cdd:pfam01591   1 PRGSTGPNFTNSKTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSAVkAYSNYEFFRPDNPEAMKIREQC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 109 ALAALKDVHDYLSHGEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPDYIDCDREK 188
Cdd:pfam01591  81 ALAALKDVLAYLNEESGQVAIFDATNTTRERRKNILDFAEENGLKVFFLESICNDPEIIARNIKLVKFSSPDYKGKPPEE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016711777 189 VLEDFLKRIECYELNYQPLDDELDSHLSYIKIFDVGTRYMVNRVQDHIQSRTVYYLMNIHVTP 251
Cdd:pfam01591 161 AIDDFMKRLECYEKQYEPLDDEHDEDLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHVTP 223
His_Phos_1 pfam00300
Histidine phosphatase superfamily (branch 1); The histidine phosphatase superfamily is so ...
254-440 2.47e-55

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: 182.79  E-value: 2.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:pfam00300   1 LYLVRHGETEWNLEGRFQGrtDSPLTELGREQAEALAERLAGEPFD--AIYSSPLKRARQTAEiiaeALGLPVEIDPRLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQ---ENVLVICHQAVMRCLLAYF 404
Cdd:pfam00300  79 EIDFGDWEGLTFEEIAERYPEEYDAWLADPADYRPPGGESLADVRARVRAALEELAARhpgKTVLVVSHGGVIRALLAHL 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 405 LDKSSDELPYLKCPLHTVLKLTPVAYGCKVESIYLN 440
Cdd:pfam00300 159 LGLPLEALRRFPLDNASLSILEFDGGGWVLVLLNDT 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
33-454 7.65e-48

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 174.70  E-value: 7.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  33 STIPQFTNSPTMVIMVGLPARGKTYISSKLTRYLNWIGTPTKVFNLGQYRRE------AVSyknyefflpDNTEAQLIRK 106
Cdd:PTZ00322  206 SAVPQPMMGSLIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIFIHQAYRRRlerrggAVS---------SPTGAAEVEF 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 107 RFALAALKDVHDYLSHGEGhVAVFDATNTTRERRSLILQFAKEHGY----KVFFIESICNDPGIIAENIRQVKLGSPDyi 182
Cdd:PTZ00322  277 RIAKAIAHDMTTFICKTDG-VAVLDGTNTTHARRMALLRAIRETGLirmtRVVFVEVVNNNSETIRRNVLRAKEMFPG-- 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 183 dcDREKVLEDFLKRIECYELNYQPLDDELDSHLSYIKIFDvGTRYMVNRVQDHIQSRTVYYLMNIHVTPRSIYLCRHGES 262
Cdd:PTZ00322  354 --APEDFVDRYYEVIEQLEAVYKSLNPVTDCDLTYIRIED-TQTFSLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEY 430
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 263 ELNLRGRIGGDSGLSARGKQYAYALANFIQSQ-GISSLKVWTSHMKRTIQTAE---------------------ALGVPY 320
Cdd:PTZ00322  431 VDLLSGRIGGNSRLTERGRAYSRALFEYFQKEiSTTSFTVMSSCAKRCTETVHyfaeesilqqstasaassqspSLNCRV 510
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 321 EQWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQ-RLEPVIMELE-RQENVLVICHQAVMR 398
Cdd:PTZ00322  511 LYFPTLDDINHGDCEGQLLSDVRRTMPNTLQSMKADPYYTAWPNGECIHQVFNaRLEPHIHDIQaSTTPVLVVSHLHLLQ 590
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016711777 399 CLLAYFLDKSSDELP-----YLKCPLHTVLKLTPVAYGCKVESIYLNVEAVNTHREKPENV 454
Cdd:PTZ00322  591 GLYSYFVTDGDNIVApqnayKIDIPFEHVIKIRMVGFNRVAELIDLSKEVDRIQQSRTGLV 651
PhoE COG0406
Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];
254-418 3.45e-46

Broad specificity phosphatase PhoE [Carbohydrate transport and metabolism];


Pssm-ID: 440175 [Multi-domain]  Cd Length: 195  Bit Score: 158.95  E-value: 3.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISslKVWTSHMKRTIQTAEAL----GVPYEQWKALN 327
Cdd:COG0406     4 LYLVRHGETEWNAEGRLQGrlDVPLTELGRAQARALAERLADIPFD--AVYSSPLQRARQTAEALaealGLPVEVDPRLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQ---ENVLVICHQAVMRCLLAYF 404
Cdd:COG0406    82 EIDFGDWEGLTFAELEARYPEALAAWLADPAEFRPPGGESLADVQARVRAALEELLARhpgGTVLVVTHGGVIRALLAHL 161
                         170
                  ....*....|....
gi 1016711777 405 LDKSSDELPYLKCP 418
Cdd:COG0406   162 LGLPLEAFWRLRID 175
PGAM smart00855
Phosphoglycerate mutase family; Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase ...
254-400 1.04e-38

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: 137.98  E-value: 1.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQG-ISSLKVWTSHMKRTIQTAEALGVPYEQWkALNEID 330
Cdd:smart00855   2 LYLIRHGETEWNREGRLYGdtDVPLTELGRAQAEALGRLLASLLlPRFDVVYSSPLKRARQTAEALAIALGLP-GLRERD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016711777  331 AGVCEEMTYEEIQEHYPEEFALRDQDKYRYRY---PKGESYEDLVQRLEPVIMELERQ-----ENVLVICHQAVMRCL 400
Cdd:smart00855  81 FGAWEGLTWDEIAAKYPEEYLAAWRDPYDPAPpapPGGESLADLVERVEPALDELIATadasgQNVLIVSHGGVIRAL 158
HP_PGM_like cd07067
Histidine phosphatase domain found in phosphoglycerate mutases and related proteins, mostly ...
254-439 1.28e-35

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: 129.36  E-value: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEAL-----GVPYEQWKAL 326
Cdd:cd07067     2 LYLVRHGESEWNAEGRFQGwtDVPLTEKGREQARALGKRLKELGIKFDRIYSSPLKRAIQTAEIIleelpGLPVEVDPRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 327 NEidagvceemtyeeiqehypeefalrdqdkyryrypkgesyedlvQRLEPVIMELERQ---ENVLVICHQAVMRCLLAY 403
Cdd:cd07067    82 RE--------------------------------------------ARVLPALEELIAPhdgKNVLIVSHGGVLRALLAY 117
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 404 FLDKSSDELPYLKCPLHTVLKLTPVAYGCKVESIYL 439
Cdd:cd07067   118 LLGLSDEDILRLNLPNGSISVLELDENGGGVLLLRL 153
ribazole_cobC TIGR03162
alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of ...
254-432 2.08e-30

alpha-ribazole phosphatase; Members of this protein family include the known CobC protein of Salmonella and Eschichia coli species, and homologous proteins found in cobalamin biosynthesis regions in other bacteria. This protein is alpha-ribazole phosphatase (EC 3.1.3.73) and, like many phosphatases, can be closely related in sequence to other phosphatases with different functions. Close homologs excluded from this model include proteins with duplications, so this model is built in -g mode to suppress hits to those proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274461 [Multi-domain]  Cd Length: 177  Bit Score: 116.18  E-value: 2.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIG-GDSGLSARGKQYAYALANfiQSQGISSLKVWTSHMKRTIQTAEALG----VPYEQWKALNE 328
Cdd:TIGR03162   1 LYLIRHGETDVNAGLCYGqTDVPLAESGEEQAAALRE--KLADVPFDAVYSSPLSRCRELAEILAerrgLPIIKDDRLRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 329 IDAGVCEEMTYEEIQEHYPeEFALRDQDKYRYRYPKGESYEDLVQRLEPV---IMELERQENVLVICHQAVMRCLLAYFL 405
Cdd:TIGR03162  79 MDFGDWEGRSWDEIPEAYP-ELDAWAADWQHARPPGGESFADFYQRVSEFleeLLKAHEGDNVLIVTHGGVIRALLAHLL 157
                         170       180
                  ....*....|....*....|....*..
gi 1016711777 406 DKSSDELPYLkcplhtvlkltPVAYGC 432
Cdd:TIGR03162 158 GLPLEQWWSF-----------AVEYGS 173
HP cd07040
Histidine phosphatase domain found in a functionally diverse set of proteins, mostly ...
254-438 1.81e-25

Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction; Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.


Pssm-ID: 132716 [Multi-domain]  Cd Length: 153  Bit Score: 101.72  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEIDA 331
Cdd:cd07040     2 LYLVRHGEREPNAEGRFTGwgDGPLTEKGRQQARELGKALRERYIKFDRIYSSPLKRAIQTAEIILEGLFEGLPVEVDPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 332 GVCEEMTYEEIQEHYPEefalrdqdkyryrypkgesyedlvqrlepvimelerQENVLVICHQAVMRCLLAYFLDKSSDE 411
Cdd:cd07040    82 ARVLNALLELLARHLLD------------------------------------GKNVLIVSHGGTIRALLAALLGLSDEE 125
                         170       180
                  ....*....|....*....|....*..
gi 1016711777 412 LPYLKCPLHTVLKLTPVAYGCKVESIY 438
Cdd:cd07040   126 ILSLNLPNGSILVLELDECGGKYVRLL 152
PRK13463 PRK13463
phosphoserine phosphatase 1;
253-404 4.45e-16

phosphoserine phosphatase 1;


Pssm-ID: 172065 [Multi-domain]  Cd Length: 203  Bit Score: 76.63  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 253 SIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSlkVWTSHMKRTIQTAEAL----GVPYEQWKAL 326
Cdd:PRK13463    4 TVYVTRHGETEWNVAKRMQGrkNSALTENGILQAKQLGERMKDLSIHA--IYSSPSERTLHTAELIkgerDIPIIADEHF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 327 NEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQR-LEPVIMELERQ--ENVLVICHQAVMRCLLAY 403
Cdd:PRK13463   82 YEINMGIWEGQTIDDIERQYPDDIQLFWNEPHLFQSTSGENFEAVHKRvIEGMQLLLEKHkgESILIVSHAAAAKLLVGH 161

                  .
gi 1016711777 404 F 404
Cdd:PRK13463  162 F 162
PRK15004 PRK15004
adenosylcobalamin/alpha-ribazole phosphatase;
254-406 7.28e-16

adenosylcobalamin/alpha-ribazole phosphatase;


Pssm-ID: 184966 [Multi-domain]  Cd Length: 199  Bit Score: 75.86  E-value: 7.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQsqGISSLKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:PRK15004    3 LWLVRHGETQANVDGLYSGhaPTPLTARGIEQAQNLHTLLR--DVPFDLVLCSELERAQHTARlvlsDRQLPVHIIPELN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 328 EIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMEL---ERQENVLVICHQAVMRCLLAYF 404
Cdd:PRK15004   81 EMFFGDWEMRHHRDLMQEDAENYAAWCNDWQHAIPTNGEGFQAFSQRVERFIARLsafQHYQNLLIVSHQGVLSLLIARL 160

                  ..
gi 1016711777 405 LD 406
Cdd:PRK15004  161 LG 162
PRK07238 PRK07238
bifunctional RNase H/acid phosphatase; Provisional
250-393 8.08e-15

bifunctional RNase H/acid phosphatase; Provisional


Pssm-ID: 180903 [Multi-domain]  Cd Length: 372  Bit Score: 75.79  E-value: 8.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 250 TPRSIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQG-ISSlkVWTSHMKRTIQTA----EALGVPYEQ 322
Cdd:PRK07238  170 TPTRLLLLRHGQTELSVQRRYSGrgNPELTEVGRRQAAAAARYLAARGgIDA--VVSSPLQRARDTAaaaaKALGLDVTV 247
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016711777 323 WKALNEIDAGVCEEMTYEEIQEHYPEEFA--LRDQDkyrYRYPKGESYEDLVQRLEPVIMELERQ---ENVLVICH 393
Cdd:PRK07238  248 DDDLIETDFGAWEGLTFAEAAERDPELHRawLADTS---VAPPGGESFDAVARRVRRARDRLIAEypgATVLVVSH 320
PRK03482 PRK03482
phosphoglycerate mutase GpmB;
254-405 9.24e-15

phosphoglycerate mutase GpmB;


Pssm-ID: 179583 [Multi-domain]  Cd Length: 215  Bit Score: 73.22  E-value: 9.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISslKVWTSHMKRTIQTAE----ALGVPYEQWKALN 327
Cdd:PRK03482    4 VYLVRHGETQWNAERRIQGqsDSPLTAKGEQQAMQVAERAKELGIT--HIISSDLGRTRRTAEiiaqACGCDIIFDPRLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 328 EIDAGVCEEmtyEEIQEHYPEEFALRDQ---DKYRYRYPKGESYEDLVQRLEPVI---MELERQENVLVICHQAVMRCLL 401
Cdd:PRK03482   82 ELNMGVLEK---RHIDSLTEEEEGWRRQlvnGTVDGRIPEGESMQELSDRMHAALescLELPQGSRPLLVSHGIALGCLV 158

                  ....
gi 1016711777 402 AYFL 405
Cdd:PRK03482  159 STIL 162
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
44-198 9.13e-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: 59.63  E-value: 9.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  44 MVIMVGLPARGKTYISSKLTRYLNWIgtptkVFNLGQYRREAVSYKNyefflPDNTEAQLIRKRFALAALKDVHDYLSHG 123
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAV-----RLSSDDERKRLFGEGR-----PSISYYTDATDRTYERLHELARIALRAG 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016711777 124 EGhvAVFDATNTTRERRSLILQFAKEHGYKVFFIEsICNDPGIIAENIRQVKLGSPDYIDCDREkVLEDFLKRIE 198
Cdd:pfam13671  71 RP--VILDATNLRRDERARLLALAREYGVPVRIVV-FEAPEEVLRERLAARARAGGDPSDVPEE-VLDRQKARFE 141
SixA COG2062
Phosphohistidine phosphatase SixA [Signal transduction mechanisms];
254-394 1.60e-10

Phosphohistidine phosphatase SixA [Signal transduction mechanisms];


Pssm-ID: 441665 [Multi-domain]  Cd Length: 153  Bit Score: 59.12  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 254 IYLCRHGESELNLRGRIGGDSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEALGvpyeqwKALneidaGV 333
Cdd:COG2062     1 LILVRHAKAEWRAPGGDDFDRPLTERGRRQARAMARWLAALGLKPDRILSSPALRARQTAEILA------EAL-----GL 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016711777 334 CEEMTYEEiqehypeefALrdqdkyryrypkgesYEDLVQRLEPVIMELERQENVLVICHQ 394
Cdd:COG2062    70 PPKVEVED---------EL---------------YDADPEDLLDLLRELDDGETVLLVGHN 106
GpmA COG0588
Phosphoglycerate mutase (BPG-dependent) [Carbohydrate transport and metabolism]; ...
256-411 3.19e-09

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: 57.01  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTA----EALG---VP-YEQWKa 325
Cdd:COG0588     5 LLRHGESEWNLENRFTGwtDVDLSEKGRAEAKRAGRLLKEAGFLFDVAYTSVLKRAIRTLwivlDEMDrlwIPvEKSWR- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 326 LNEIDAGVCEEMTYEEIQEHYPEEF-------------ALRDQDKY------RYR------YPKGESYEDLVQRLEP--- 377
Cdd:COG0588    84 LNERHYGALQGLNKAETAAKYGEEQvhiwrrsydvpppPLDPDDPRhpgndpRYAdlppaeLPLTESLKDTVARVLPywe 163
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 378 -VIM-ELERQENVLVICHQAVMRCLLAYfLDKSSDE 411
Cdd:COG0588   164 eEIApALKAGKRVLIAAHGNSLRALVKH-LDGISDE 198
PTZ00123 PTZ00123
phosphoglycerate mutase like-protein; Provisional
264-411 4.12e-09

phosphoglycerate mutase like-protein; Provisional


Pssm-ID: 240280  Cd Length: 236  Bit Score: 56.97  E-value: 4.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 264 LNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTA----EALGVPY----EQWKaLNEIDAGV 333
Cdd:PTZ00123    1 WNKENRFTGwtDVPLSEKGVQEAREAGKLLKEKGFRFDVVYTSVLKRAIKTAwivlEELGQLHvpviKSWR-LNERHYGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 334 CEEMTYEEIQEHYPEEF-------------ALRDQDKY------RYRY------PKGESYEDLVQRLEP-----VIMELE 383
Cdd:PTZ00123   80 LQGLNKSETAEKHGEEQvkiwrrsydipppPLEKSDERypgndpVYKDipkdalPNTECLKDTVERVLPywedhIAPDIL 159
                         170       180
                  ....*....|....*....|....*...
gi 1016711777 384 RQENVLVICHQAVMRCLLAYfLDKSSDE 411
Cdd:PTZ00123  160 AGKKVLVAAHGNSLRALVKY-LDKMSEE 186
gpmA PRK14120
phosphoglyceromutase; Provisional
250-411 4.79e-08

phosphoglyceromutase; Provisional


Pssm-ID: 184519  Cd Length: 249  Bit Score: 53.89  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 250 TPRSIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAE-ALG------VPY 320
Cdd:PRK14120    3 MTYTLVLLRHGESEWNAKNLFTGwvDVDLTEKGEAEAKRGGELLAEAGVLPDVVYTSLLRRAIRTANlALDaadrlwIPV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 321 EQ-WKaLNEIDAGVCEEMTYEEIQEHY-PEEF------------ALRDQDKYRY----RY------PKGESYEDLVQRLE 376
Cdd:PRK14120   83 RRsWR-LNERHYGALQGKDKAETKAEYgEEQFmlwrrsydtpppPIEDGSEYSQdndpRYadlgvgPRTECLKDVVARFL 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1016711777 377 P-----VIMELERQENVLVICHQAVMRCLLAYfLDKSSDE 411
Cdd:PRK14120  162 PyweddIVPDLKAGKTVLIAAHGNSLRALVKH-LDGISDE 200
PRK01295 PRK01295
phosphoglyceromutase; Provisional
251-411 7.16e-08

phosphoglyceromutase; Provisional


Pssm-ID: 167205 [Multi-domain]  Cd Length: 206  Bit Score: 52.77  E-value: 7.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 251 PRSIYLCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTA----EALG---VPYE 321
Cdd:PRK01295    2 SRTLVLVRHGQSEWNLKNLFTGwrDPDLTEQGVAEAKAAGRKLKAAGLKFDIAFTSALSRAQHTCqlilEELGqpgLETI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 322 QWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIME-----LERQENVLVICHQAV 396
Cdd:PRK01295   82 RDQALNERDYGDLSGLNKDDARAKWGEEQVHIWRRSYDVPPPGGESLKDTGARVLPYYLQeilprVLRGERVLVAAHGNS 161
                         170
                  ....*....|....*
gi 1016711777 397 MRCLLAyFLDKSSDE 411
Cdd:PRK01295  162 LRALVM-VLDGLTPE 175
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
44-215 1.17e-07

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 51.45  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  44 MVIMVGLPARGKTYISSKLTRYLNWIgtptkvfnlgQYRREAVSYKNYEFFLPDNTEAQLIRKR-----FALAAlkdvhD 118
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLGAV----------RLRSDVVRKRLFGAGLAPLERSPEATARtyarlLALAR-----E 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 119 YLSHgeGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICnDPGIIAENI--RQVKLGSPDYidcdREKVLEDFLKR 196
Cdd:COG0645    66 LLAA--GRSVILDATFLRRAQREAFRALAEEAGAPFVLIWLDA-PEEVLRERLeaRNAEGGDSDA----TWEVLERQLAF 138
                         170
                  ....*....|....*....
gi 1016711777 197 iecyelnYQPLDDELDSHL 215
Cdd:COG0645   139 -------EEPLTEDEGFLL 150
COG4639 COG4639
Predicted kinase [General function prediction only];
42-154 5.12e-07

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 49.06  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  42 PTMVIMVGLPARGKTYISSKLTRylnwigtPTKVFNLGQYRREAvsyknyeFFLPDNTEAQlirkRFALAALKD-VHDYL 120
Cdd:COG4639     2 LSLVVLIGLPGSGKSTFARRLFA-------PTEVVSSDDIRALL-------GGDENDQSAW----GDVFQLAHEiARARL 63
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1016711777 121 ShgEGHVAVFDATNTTRERRSLILQFAKEHGYKV 154
Cdd:COG4639    64 R--AGRLTVVDATNLQREARRRLLALARAYGALV 95
gpmA PRK14117
phosphoglyceromutase; Provisional
258-418 1.63e-06

phosphoglyceromutase; Provisional


Pssm-ID: 184517  Cd Length: 230  Bit Score: 49.25  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 258 RHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQT-------AEALGVPYEQWKALNE 328
Cdd:PRK14117    8 RHGESEWNKANLFTGwaDVDLSEKGTQQAIDAGKLIKEAGIEFDLAFTSVLKRAIKTtnlaleaSDQLWVPVEKSWRLNE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 329 IDAGVCEEMTYEEIQEHYPEEF-------------ALRDQDKYR----YRY--------PKGESYEDLVQRLEP-----V 378
Cdd:PRK14117   88 RHYGGLTGKNKAEAAEQFGDEQvhiwrrsydvlppAMAKDDEYSahtdRRYaslddsviPDAENLKVTLERALPfwedkI 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1016711777 379 IMELERQENVLVICHQAVMRCLLAYFLDKSSDELPYLKCP 418
Cdd:PRK14117  168 APALKDGKNVFVGAHGNSIRALVKHIKGLSDDEIMDVEIP 207
gpmA PRK14116
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
256-411 4.67e-06

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 172606  Cd Length: 228  Bit Score: 47.60  E-value: 4.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQT-------AEALGVP-YEQWKa 325
Cdd:PRK14116    6 LIRHGQSEWNLSNQFTGwvDVDLSEKGVEEAKKAGRLIKEAGLEFDQAYTSVLTRAIKTlhyaleeSDQLWIPeTKTWR- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 326 LNEIDAGVCEEMTYEEIQEHYPEEF-------------ALRDQDKYRY----RY--------PKGESYEDLVQRLEP--- 377
Cdd:PRK14116   85 LNERHYGALQGLNKKETAEKYGDEQvhiwrrsydvlppLLDADDEGSAakdrRYanldpriiPGGENLKVTLERVIPfwe 164
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 378 --VIMELERQENVLVICHQAVMRCLLAYfLDKSSDE 411
Cdd:PRK14116  165 dhIAPDLLDGKNVIIAAHGNSLRALTKY-IENISDE 199
gpmA PRK14119
phosphoglyceromutase; Provisional
256-411 4.75e-06

phosphoglyceromutase; Provisional


Pssm-ID: 184518  Cd Length: 228  Bit Score: 47.58  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQT-------AEALGVP-YEQWKa 325
Cdd:PRK14119    6 LCRHGQSEWNAKNLFTGweDVNLSEQGINEATRAGEKVRENNIAIDVAFTSLLTRALDTthyilteSKQQWIPvYKSWR- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 326 LNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKY-------------------RYRY------PKGESYEDLVQRLEP--- 377
Cdd:PRK14119   85 LNERHYGGLQGLNKDDARKEFGEEQVHIWRRSYdvkppaeteeqreayladrRYNHldkrmmPYSESLKDTLVRVIPfwt 164
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 378 --VIMELERQENVLVICHQAVMRCLLAYfLDKSSDE 411
Cdd:PRK14119  165 dhISQYLLDGQTVLVSAHGNSIRALIKY-LEDVSDE 199
gpmA PRK14115
2,3-diphosphoglycerate-dependent phosphoglycerate mutase;
256-411 5.36e-05

2,3-diphosphoglycerate-dependent phosphoglycerate mutase;


Pssm-ID: 184516  Cd Length: 247  Bit Score: 44.47  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQT----AEALG---VPYEQ-WKa 325
Cdd:PRK14115    5 LIRHGESQWNKENRFTGwtDVDLSEKGVSEAKAAGKLLKEEGYTFDVAYTSVLKRAIRTlwivLDELDqmwLPVEKsWR- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 326 LNEIDAGVCEEMTYEEIQEHYPEE--------FALR----DQDKYRY-----RY--------PKGESYEDLVQRLEP--- 377
Cdd:PRK14115   84 LNERHYGALQGLNKAETAAKYGDEqvkiwrrsYDVPppalEKDDERYpghdpRYaklpeeelPLTESLKDTIARVLPywn 163
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1016711777 378 -VIM-ELERQENVLVICHQAVMRCLLAYfLDKSSDE 411
Cdd:PRK14115  164 eTIApQLKSGKRVLIAAHGNSLRALVKY-LDNISDE 198
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
41-157 8.00e-05

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


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 43.18  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  41 SPTMVIMVGLPARGKTYISSKLTRYLNWIGTPTKVFNLGQYRREAVSyknyEFFlPDNTEAQLIRK-RFALAALkdvhdY 119
Cdd:COG4088     3 SPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVN----ESF-PKETYEEVVEDvRTTTADN-----A 72
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1016711777 120 LSHgeGHVAVFDATNTTRERRSLILQFAKeHGYKVFFI 157
Cdd:COG4088    73 LDN--GYSVIVDGTFYYRSWQRDFRNLAK-HKAPIHII 107
sixA TIGR00249
phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]
254-317 2.91e-04

phosphohistidine phosphatase SixA; [Regulatory functions, Protein interactions]


Pssm-ID: 129351  Cd Length: 152  Bit Score: 41.36  E-value: 2.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016711777 254 IYLCRHGESElnLRGRIGGDSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEALG 317
Cdd:TIGR00249   3 LFIMRHGDAA--LDAASDSVRPLTTNGCDESRLVAQWLKGQGVEIERILVSPFVRAEQTAEIVG 64
PRK13462 PRK13462
acid phosphatase; Provisional
256-406 3.45e-04

acid phosphatase; Provisional


Pssm-ID: 139587 [Multi-domain]  Cd Length: 203  Bit Score: 41.74  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777 256 LCRHGESELNLRGRIGG--DSGLSARGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEALGVPY-EQWKALNEIDAG 332
Cdd:PRK13462   10 LLRHGETEWSKSGRHTGrtELELTETGRTQAELAGQALGELELDDPLVISSPRRRALDTAKLAGLTVdEVSGLLAEWDYG 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016711777 333 VCEEMTYEEIQEHYPEEFAlrdqdkYRYRYPKGESYEDLVQRLEPVI---MELERQENVLVICHQAVMRCLLAYFLD 406
Cdd:PRK13462   90 SYEGLTTPQIRESEPDWLV------WTHGCPGGESVAQVNERADRAValaLEHMESRDVVFVSHGHFSRAVITRWVE 160
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
45-139 8.30e-03

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 37.52  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016711777  45 VIMVGLPARGKTYISSKLTryLNWIGT--PTKVFNLgqyrrEAVSYKNYEFFLPDNTEAQLIRKRFalaalkdvHDYLSH 122
Cdd:PTZ00133   20 ILMVGLDAAGKTTILYKLK--LGEVVTtiPTIGFNV-----ETVEYKNLKFTMWDVGGQDKLRPLW--------RHYYQN 84
                          90
                  ....*....|....*..
gi 1016711777 123 GEGHVAVFDATNttRER 139
Cdd:PTZ00133   85 TNGLIFVVDSND--RER 99
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
38-105 9.85e-03

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 37.06  E-value: 9.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016711777  38 FTNSPTMVIMVGLPARGKTYISSKLTRYLNWIGTPTKVFNLgqyrrEAVSYKNYEFFLPDNTEAQLIR 105
Cdd:cd04149     5 FGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNV-----ETVTYKNVKFNVWDVGGQDKIR 67
 
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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