|
Name |
Accession |
Description |
Interval |
E-value |
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
3-165 |
1.66e-96 |
|
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442496 [Multi-domain] Cd Length: 164 Bit Score: 276.24 E-value: 1.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 3 GSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVC 82
Cdd:COG3265 1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 83 SALKKSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVSIDTTIEDVVANAA 162
Cdd:COG3265 81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQIL 160
|
...
gi 515989842 163 ELI 165
Cdd:COG3265 161 AAL 163
|
|
| therm_gnt_kin |
TIGR01313 |
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ... |
7-167 |
4.69e-77 |
|
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.
Pssm-ID: 273551 Cd Length: 163 Bit Score: 226.90 E-value: 4.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 7 IVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVCSALK 86
Cdd:TIGR01313 2 VLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 87 KSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDG-EPRTLLVSIDTTIEDVVANAAELI 165
Cdd:TIGR01313 82 RHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLAdETDVLRVDIDQPLEGVEEDCIAVV 161
|
..
gi 515989842 166 LE 167
Cdd:TIGR01313 162 LK 163
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
6-152 |
1.94e-73 |
|
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
Pssm-ID: 238979 [Multi-domain] Cd Length: 150 Bit Score: 217.12 E-value: 1.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYS-LESKNEHGIIVCSA 84
Cdd:cd02021 2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAkLASAGEGVVVACSA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 85 LKKSYRDQIRDG--NNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVsIDT 152
Cdd:cd02021 82 LKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIV-IDV 150
|
|
| gntK |
PRK11545 |
gluconokinase; |
9-165 |
1.27e-70 |
|
gluconokinase;
Pssm-ID: 236926 Cd Length: 163 Bit Score: 210.73 E-value: 1.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 9 MGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVCSALKKS 88
Cdd:PRK11545 1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515989842 89 YRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERP-DGEPRTLLVSIDTTIEDVVANAAELI 165
Cdd:PRK11545 81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPgADETDVLVVDIDQPLEGVVASTIEVI 158
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
9-120 |
4.49e-10 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 55.28 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 9 MGvcaSGKTTIGELLAEKLGRKFIDGDDLHPRANiqKMASGQPLNDD----DRKPWLERIRDAAysleskNEHGIIVC-- 82
Cdd:pfam01202 1 MG---AGKSTIGRLLAKALGLPFIDTDEEIEKRT--GMSIAEIFEEEgeegFRRLESEVLKELL------AEHGLVIAtg 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 515989842 83 --SALKKSYRDQIRDGNnnvTFLFLDGDKSLILERMRQRQ 120
Cdd:pfam01202 70 ggAVLSEENRDLLKERG---IVIYLDAPLEVLLERLKRDK 106
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
3-165 |
1.66e-96 |
|
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442496 [Multi-domain] Cd Length: 164 Bit Score: 276.24 E-value: 1.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 3 GSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVC 82
Cdd:COG3265 1 PMVIVVMGVSGSGKSTVGQALAERLGWPFIDGDDFHPPANIAKMAAGIPLTDEDRAPWLEALADAIAAHLAAGEGAVLAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 83 SALKKSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVSIDTTIEDVVANAA 162
Cdd:COG3265 81 SALKRSYRDRLREGNPDVRFVYLDGSRELIAERLAARKGHFMPASLLDSQFATLEPPGPDEDAIVVDIDQPPEEIVAQIL 160
|
...
gi 515989842 163 ELI 165
Cdd:COG3265 161 AAL 163
|
|
| therm_gnt_kin |
TIGR01313 |
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ... |
7-167 |
4.69e-77 |
|
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.
Pssm-ID: 273551 Cd Length: 163 Bit Score: 226.90 E-value: 4.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 7 IVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVCSALK 86
Cdd:TIGR01313 2 VLMGVAGSGKSTIASALAHRLGAKFIEGDDLHPAANIEKMSAGIPLNDDDRWPWLQNLNDASTAAAAKNKVGIITCSALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 87 KSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDG-EPRTLLVSIDTTIEDVVANAAELI 165
Cdd:TIGR01313 82 RHYRDILREAEPNLHFIYLSGDKDVILERMKARKGHFMKADMLESQFAALEEPLAdETDVLRVDIDQPLEGVEEDCIAVV 161
|
..
gi 515989842 166 LE 167
Cdd:TIGR01313 162 LK 163
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
6-152 |
1.94e-73 |
|
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
Pssm-ID: 238979 [Multi-domain] Cd Length: 150 Bit Score: 217.12 E-value: 1.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYS-LESKNEHGIIVCSA 84
Cdd:cd02021 2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDDLHPPANIAKMAAGIPLNDEDRWPWLQALTDALLAkLASAGEGVVVACSA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 85 LKKSYRDQIRDG--NNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLLVsIDT 152
Cdd:cd02021 82 LKRIYRDILRGGaaNPRVRFVHLDGPREVLAERLAARKGHFMPADLLDSQFETLEPPGEDEEDVIV-IDV 150
|
|
| gntK |
PRK11545 |
gluconokinase; |
9-165 |
1.27e-70 |
|
gluconokinase;
Pssm-ID: 236926 Cd Length: 163 Bit Score: 210.73 E-value: 1.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 9 MGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGIIVCSALKKS 88
Cdd:PRK11545 1 MGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515989842 89 YRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERP-DGEPRTLLVSIDTTIEDVVANAAELI 165
Cdd:PRK11545 81 YRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPgADETDVLVVDIDQPLEGVVASTIEVI 158
|
|
| idnK |
PRK09825 |
gluconokinase; |
1-157 |
1.19e-64 |
|
gluconokinase;
Pssm-ID: 182097 Cd Length: 176 Bit Score: 196.02 E-value: 1.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 1 MAGSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNEHGII 80
Cdd:PRK09825 1 MAGESYILMGVSGSGKSLIGSKIAALFSAKFIDGDDLHPAKNIDKMSQGIPLTDEDRLPWLERLNDASYSLYKKNETGFI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515989842 81 VCSALKKSYRDQIRDGNNNVTFLFLDGDKSLILERMRQRQGHFMKENMVNSQFETLERPDGEPRTLL-VSIDTTIEDV 157
Cdd:PRK09825 81 VCSSLKKQYRDILRKSSPNVHFLWLDGDYETILARMQRRAGHFMPPDLLQSQFDALERPCADEHDIArIDVNHDIENV 158
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
9-120 |
4.49e-10 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 55.28 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 9 MGvcaSGKTTIGELLAEKLGRKFIDGDDLHPRANiqKMASGQPLNDD----DRKPWLERIRDAAysleskNEHGIIVC-- 82
Cdd:pfam01202 1 MG---AGKSTIGRLLAKALGLPFIDTDEEIEKRT--GMSIAEIFEEEgeegFRRLESEVLKELL------AEHGLVIAtg 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 515989842 83 --SALKKSYRDQIRDGNnnvTFLFLDGDKSLILERMRQRQ 120
Cdd:pfam01202 70 ggAVLSEENRDLLKERG---IVIYLDAPLEVLLERLKRDK 106
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
6-162 |
2.27e-08 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 50.68 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDlhpranIQKMASGQPLNDDDRKPWL-ERIRDAAYSLESKN-EHG---II 80
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRLRSDV------VRKRLFGAGLAPLERSPEAtARTYARLLALARELlAAGrsvIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 81 VCSALKKSYRDQIRD--GNNNVTF--LFLDGDKSLILERMRQRQGHFMK----ENMVNSQFETLERPDGEPRTLLVsIDT 152
Cdd:COG0645 76 DATFLRRAQREAFRAlaEEAGAPFvlIWLDAPEEVLRERLEARNAEGGDsdatWEVLERQLAFEEPLTEDEGFLLV-VDT 154
|
170
....*....|
gi 515989842 153 TIEDVVANAA 162
Cdd:COG0645 155 SGLEEALAAL 164
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
1-54 |
3.29e-07 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 47.88 E-value: 3.29e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 515989842 1 MAGSSVIV----MGvcaSGKTTIGELLAEKLGRKFIDGDDLhpranIQKMAsGQPLND 54
Cdd:PRK00131 1 MLKGPNIVligfMG---AGKSTIGRLLAKRLGYDFIDTDHL-----IEARA-GKSIPE 49
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
5-37 |
8.71e-07 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 46.39 E-value: 8.71e-07
10 20 30
....*....|....*....|....*....|...
gi 515989842 5 SVIVMGVCASGKTTIGELLAEKLGRKFIDGDDL 37
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDEL 33
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
9-37 |
1.67e-06 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 45.50 E-value: 1.67e-06
10 20
....*....|....*....|....*....
gi 515989842 9 MGvcaSGKTTIGELLAEKLGRKFIDGDDL 37
Cdd:COG0703 7 MG---AGKSTVGRLLAKRLGLPFVDTDAE 32
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
1-164 |
2.10e-05 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 42.70 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 1 MAGSSVIVMGVCASGKTTIGELLAEKL---GRKF--IDGDDLhpRANIQKmasGQPLNDDDRKpwlERIRDAAYSLESKN 75
Cdd:PRK00889 2 QRGVTVWFTGLSGAGKTTIARALAEKLreaGYPVevLDGDAV--RTNLSK---GLGFSKEDRD---TNIRRIGFVANLLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 76 EHGIIVCSALKKSYRD---QIRDGNNNVTFLFLDGDKSLILER------MRQRQG---HFMKenmVNSQFETLERPDGEP 143
Cdd:PRK00889 74 RHGVIVLVSAISPYREtreEVRANIGNFLEVFVDAPLEVCEQRdvkglyAKARAGeikHFTG---IDDPYEPPLNPEVEC 150
|
170 180
....*....|....*....|.
gi 515989842 144 RTLLVSIDTTIEDVVANAAEL 164
Cdd:PRK00889 151 RTDLESLEESVDKVLQKLEEL 171
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
6-119 |
4.81e-05 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 40.87 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPR----ANIQKMASGQPLNDDDRKPWLERIRDAAYSLESKNehgIIV 81
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENglvlGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGN---LII 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 515989842 82 CSALKKSYRDQIRDGNnnvtFLFLDGDKSLILERMRQR 119
Cdd:pfam13238 78 DGHLAELEPERAKDLV----GIVLRASPEELLERLEKR 111
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
13-35 |
4.83e-05 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 41.47 E-value: 4.83e-05
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
14-165 |
7.99e-05 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 41.23 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 14 SGKTTIGELLAEKL---GRK--FIDGDDLhpRANiqkmasgqpLN------DDDRKPWLERIRDAAYSLeskNEHGIIVC 82
Cdd:COG0529 27 SGKSTLANALERRLferGRHvyLLDGDNV--RHG---------LNkdlgfsKEDRDENIRRIGEVAKLL---ADAGLIVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 83 SAL---KKSYRDQIRDgnnnvtfLFLDG-------DKSL-ILERmRQRQGHFMK------ENM--VNSQFETLERPDgep 143
Cdd:COG0529 93 VAFispYRADREEARE-------LIGEGefievyvDTPLeVCEA-RDPKGLYAKarageiKNFtgIDDPYEAPENPE--- 161
|
170 180
....*....|....*....|..
gi 515989842 144 rtllVSIDTTIEDVVANAAELI 165
Cdd:COG0529 162 ----LVLDTDKESVEESVEKIL 179
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
6-139 |
1.50e-04 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 39.99 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515989842 6 VIVM-GVCASGKTTIGELLAEKLGRKFIDGDDLhpRANIQKMASGQPLNDDDRKPWL-ERIRDAAYSLESKNEHGIIVCS 83
Cdd:pfam13671 1 LILLvGLPGSGKSTLARRLLEELGAVRLSSDDE--RKRLFGEGRPSISYYTDATDRTyERLHELARIALRAGRPVILDAT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515989842 84 ALKKSYRDQIRD--GNNNVTF--LFLDGDKSLILERMRQRQGH-----FMKENMVNSQFETLERP 139
Cdd:pfam13671 79 NLRRDERARLLAlaREYGVPVriVVFEAPEEVLRERLAARARAggdpsDVPEEVLDRQKARFEPP 143
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
1-41 |
5.26e-04 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 5.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 515989842 1 MAGSSVIVMGVCASGKTTIGELLAEKLGRKFIDGDDLHPRA 41
Cdd:PLN02199 100 LNGRSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQA 140
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
14-38 |
6.55e-04 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 38.65 E-value: 6.55e-04
10 20
....*....|....*....|....*
gi 515989842 14 SGKTTIGELLAEKLGRKFIDGDDLH 38
Cdd:COG1102 11 SGGTTIAKRLAEKLGLPLYDGEILR 35
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
6-47 |
6.76e-04 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 38.53 E-value: 6.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 515989842 6 VIVMGVCASGKTTIGELLAEKLGRKFIDGDDLhpranIQKMA 47
Cdd:PRK13947 4 IVLIGFMGTGKTTVGKRVATTLSFGFIDTDKE-----IEKMT 40
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| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
10-81 |
4.81e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 35.54 E-value: 4.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515989842 10 GVCASGKTTIGELLAEKLGRKFIDGDDLHpRANIQKMASGQPLNDDDRKPWLERIRDAAysleskNEHGIIV 81
Cdd:cd02020 6 GPAGSGKSTVAKLLAKKLGLPYLDTGGIR-TEEVGKLASEVAAIPEVRKALDERQRELA------KKPGIVL 70
|
|
| Fap7 |
COG1936 |
Broad-specificity NMP kinase [Nucleotide transport and metabolism]; |
6-33 |
5.50e-03 |
|
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
Pssm-ID: 441539 [Multi-domain] Cd Length: 173 Bit Score: 35.95 E-value: 5.50e-03
10 20
....*....|....*....|....*...
gi 515989842 6 VIVMGVCASGKTTIGELLAEKLGRKFID 33
Cdd:COG1936 3 IAITGTPGTGKTTVAKLLAERLGLEVIH 30
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
6-35 |
6.76e-03 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 35.48 E-value: 6.76e-03
10 20 30
....*....|....*....|....*....|
gi 515989842 6 VIVMGVCASGKTTIGELLAEKLGRKFIDGD 35
Cdd:PRK13949 4 IFLVGYMGAGKTTLGKALARELGLSFIDLD 33
|
|
|