|
Name |
Accession |
Description |
Interval |
E-value |
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
4-172 |
1.73e-61 |
|
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: 188.37 E-value: 1.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:COG0529 19 VWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVAKLLADAGLIVLVAFISP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 84 FDDVRKELKEKYDAR---TVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:COG0529 99 YRADREEARELIGEGefiEVYVDTPLEVCEARDPKGLYAKARA-----GEIKNFTGIDDPYEAPENPELVLDTDKESVEE 173
|
170
....*....|..
gi 1477141595 161 SAVRLFSFILDN 172
Cdd:COG0529 174 SVEKILAYLEER 185
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
4-165 |
2.24e-48 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 154.79 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:PRK00889 7 VWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVSAISP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 84 FDDVRKELKEKY-DARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLETSA 162
Cdd:PRK00889 87 YRETREEVRANIgNFLEVFVDAPLEVCEQRDVKGLYAKAR-----AGEIKHFTGIDDPYEPPLNPEVECRTDLESLEESV 161
|
...
gi 1477141595 163 VRL 165
Cdd:PRK00889 162 DKV 164
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
4-153 |
4.37e-45 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 145.70 E-value: 4.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:cd02027 2 IWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFISP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1477141595 84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYT 153
Cdd:cd02027 82 YREDReaaRKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARA-----GEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
4-154 |
5.54e-45 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 145.54 E-value: 5.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:pfam01583 5 IWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITAFISP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1477141595 84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTH 154
Cdd:pfam01583 85 YREDReqaRELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKAR-----AGEIKGFTGIDSPYEAPENPELVLDTD 153
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
4-169 |
1.39e-42 |
|
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 129547 Cd Length: 184 Bit Score: 140.30 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:TIGR00455 21 IWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGEVAKLFVRNGIIVITSFISP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:TIGR00455 101 YRADRqmvRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKAR-----NGEIKGFTGIDSPYEAPENPEVVLDTDQNDREE 175
|
....*....
gi 1477141595 161 SAVRLFSFI 169
Cdd:TIGR00455 176 CVGQIIEKL 184
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
4-172 |
1.73e-61 |
|
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: 188.37 E-value: 1.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:COG0529 19 VWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVAKLLADAGLIVLVAFISP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 84 FDDVRKELKEKYDAR---TVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:COG0529 99 YRADREEARELIGEGefiEVYVDTPLEVCEARDPKGLYAKARA-----GEIKNFTGIDDPYEAPENPELVLDTDKESVEE 173
|
170
....*....|..
gi 1477141595 161 SAVRLFSFILDN 172
Cdd:COG0529 174 SVEKILAYLEER 185
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
4-165 |
2.24e-48 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 154.79 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:PRK00889 7 VWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVSAISP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 84 FDDVRKELKEKY-DARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLETSA 162
Cdd:PRK00889 87 YRETREEVRANIgNFLEVFVDAPLEVCEQRDVKGLYAKAR-----AGEIKHFTGIDDPYEPPLNPEVECRTDLESLEESV 161
|
...
gi 1477141595 163 VRL 165
Cdd:PRK00889 162 DKV 164
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
4-153 |
4.37e-45 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 145.70 E-value: 4.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:cd02027 2 IWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFISP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1477141595 84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYT 153
Cdd:cd02027 82 YREDReaaRKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARA-----GEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
4-154 |
5.54e-45 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 145.54 E-value: 5.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:pfam01583 5 IWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITAFISP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1477141595 84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTH 154
Cdd:pfam01583 85 YREDReqaRELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKAR-----AGEIKGFTGIDSPYEAPENPELVLDTD 153
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
4-169 |
1.39e-42 |
|
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 129547 Cd Length: 184 Bit Score: 140.30 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:TIGR00455 21 IWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGEVAKLFVRNGIIVITSFISP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:TIGR00455 101 YRADRqmvRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKAR-----NGEIKGFTGIDSPYEAPENPEVVLDTDQNDREE 175
|
....*....
gi 1477141595 161 SAVRLFSFI 169
Cdd:TIGR00455 176 CVGQIIEKL 184
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
3-165 |
5.30e-38 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 128.91 E-value: 5.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 3 LIQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAIN 82
Cdd:PRK03846 26 VLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKENIRRVGEVAKLMVDAGLVVLTAFIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 83 PF----DDVRKELKEKyDARTVWIHCALDILVERDTKGLYRKAllpgdHPDKIRNLTGLNDIYEIPIGADLVIYTHTEDL 158
Cdd:PRK03846 106 PHraerQMVRERLGEG-EFIEVFVDTPLAICEARDPKGLYKKA-----RAGEIRNFTGIDSVYEAPESPEIHLDTGEQLV 179
|
....*..
gi 1477141595 159 ETSAVRL 165
Cdd:PRK03846 180 TNLVEQL 186
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
6-171 |
5.88e-35 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 128.89 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 6 LTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINPFD 85
Cdd:PRK05506 465 FTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADRVENIRRVAEVARLMADAGLIVLVSFISPFR 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 86 DVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLETSA 162
Cdd:PRK05506 545 EERelaRALHGEGEFVEVFVDTPLEVCEARDPKGLYAKAR-----AGEIKNFTGIDSPYEAPENPELRLDTTGRSPEELA 619
|
....*....
gi 1477141595 163 VRLFSFILD 171
Cdd:PRK05506 620 EQVLELLRR 628
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
6-162 |
1.99e-30 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 115.92 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 6 LTGLSGAGKTSIAFRVQQMLLQ-REIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINPF 84
Cdd:PRK05537 397 FTGLSGAGKSTIAKALMVKLMEmRGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICAPIAPY 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 85 DDVRKELKEKYDA--RTVWIHCALDILV--ERDTKGLYRKAllpgdHPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:PRK05537 477 RATRREVREMIEAygGFIEVHVATPLEVceQRDRKGLYAKA-----REGKIKGFTGISDPYEPPANPELVIDTTNVTPDE 551
|
..
gi 1477141595 161 SA 162
Cdd:PRK05537 552 CA 553
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
2-151 |
1.58e-17 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 75.48 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 2 LLIQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKsICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAI 81
Cdd:PRK05541 8 YVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELRE-ILGHYGYDKQSRIEMALKRAKLAKFLADQGMIVIVTTI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1477141595 82 NPFDDV----RKELKEKYDartVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPiGADLVI 151
Cdd:PRK05541 87 SMFDEIyaynRKHLPNYFE---VYLKCDMEELIRRDQKGLYTKALK-----GEIKNVVGVDIPFDEP-KADLVI 151
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
1-112 |
9.23e-09 |
|
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: 52.04 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 1 MLLIqLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPAdRRENIRRLGAIAQALVLKNTIAIIA- 79
Cdd:COG4088 5 MLLI-LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNESFPKET-YEEVVEDVRTTTADNALDNGYSVIVd 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 1477141595 80 AINPFDDVRKEL----KEKYDARTVWIHCALDILVER 112
Cdd:COG4088 83 GTFYYRSWQRDFrnlaKHKAPIHIIYLKAPLETALRR 119
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
3-123 |
7.99e-05 |
|
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: 40.70 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 3 LIQLTGLSGAGKTSIAfrvqqMLLQREIAAEIIDGDMYRK--SICKDLGFSP---ADRRENIRRL-GAIAQALVLKNTIA 76
Cdd:cd02021 1 IIVVMGVSGSGKSTVG-----KALAERLGAPFIDGDDLHPpaNIAKMAAGIPlndEDRWPWLQALtDALLAKLASAGEGV 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1477141595 77 IIAAINPFDDVRKEL-KEKYDARTVWIHCAL--DILVERDT--KGLYRKALL 123
Cdd:cd02021 76 VVACSALKRIYRDILrGGAANPRVRFVHLDGprEVLAERLAarKGHFMPADL 127
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
3-112 |
2.77e-04 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 39.51 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 3 LIQLTGLSGAGKTSIAfrvqqMLLQREIAAEIIDGDMYRKSICKDlGFSPADRRENIR-----RLGAIAQALVLKNTIAI 77
Cdd:COG0645 1 LILVCGLPGSGKSTLA-----RALAERLGAVRLRSDVVRKRLFGA-GLAPLERSPEATartyaRLLALARELLAAGRSVI 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1477141595 78 IAAINPFDDVRKELKE-----KYDARTVWIHCALDILVER 112
Cdd:COG0645 75 LDATFLRRAQREAFRAlaeeaGAPFVLIWLDAPEEVLRER 114
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
4-134 |
7.90e-04 |
|
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: 37.92 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 4 IQLTGLSGAGKTSIAFRVQQMLlqreiAAEIIDGDMYrksICKDLGFSPAD-----RRENIRRLGAIAQALVLKNTIAII 78
Cdd:cd00464 2 IVLIGMMGAGKTTVGRLLAKAL-----GLPFVDLDEL---IEQRAGMSIPEifaeeGEEGFRELEREVLLLLLTKENAVI 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1477141595 79 AA-----INPfdDVRKELKEKydARTVWIHCALDILVERDTKGLYRkALLPGDHPDKIRNL 134
Cdd:cd00464 74 ATgggavLRE--ENRRLLLEN--GIVVWLDASPEELLERLARDKTR-PLLQDEDPERLREL 129
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
3-113 |
8.42e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 37.89 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 3 LIQLTGLSGAGKTSIAFRVQQmllqreiAAEIIDGDMYRksicKDLGFSPADRREN---IRRLGAIAQALVLKNTIAIIA 79
Cdd:COG4639 4 LVVLIGLPGSGKSTFARRLFA-------PTEVVSSDDIR----ALLGGDENDQSAWgdvFQLAHEIARARLRAGRLTVVD 72
|
90 100 110
....*....|....*....|....*....|....*....
gi 1477141595 80 AINPFDDVRKELKE---KYDART--VWIHCALDILVERD 113
Cdd:COG4639 73 ATNLQREARRRLLAlarAYGALVvaVVLDVPLEVCLARN 111
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
3-112 |
1.07e-03 |
|
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: 37.67 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 3 LIQLTGLSGAGKTSIAFRvqqmlLQREIAAEIIDGDMYRKSICKDLGFSPADRRENI----RRLGAIAQALVLKNTIAII 78
Cdd:pfam13671 1 LILLVGLPGSGKSTLARR-----LLEELGAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVIL 75
|
90 100 110
....*....|....*....|....*....|....*....
gi 1477141595 79 AAINPFDDVRK---ELKEKYDART--VWIHCALDILVER 112
Cdd:pfam13671 76 DATNLRRDERArllALAREYGVPVriVVFEAPEEVLRER 114
|
|
| KTI12 |
pfam08433 |
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ... |
3-123 |
2.72e-03 |
|
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which interact with the Elongator complex, a component of the elongating form of RNA polymerase II. The Elongator complex has histone acetyltransferase activity.
Pssm-ID: 400643 Cd Length: 269 Bit Score: 37.28 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595 3 LIQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSiCKDLGFSPADR--RENIRRlgAIAQALVlKNTIAIIAA 80
Cdd:pfam08433 1 LVLLTGLPSSGKSTRAKQLAKYLEESNYDVIVISDESLGIE-KDDYKDSAKEKflRGSLRS--AVKRDLS-KNTIVIVDS 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1477141595 81 INPFDDVRKEL----KEkYDARTVWIHCA--LDILV----ERDTKGLYRKALL 123
Cdd:pfam08433 77 LNYIKGFRYELyciaKA-ARTTYCVIHCKapLDLCRkwneERGQKSRYPDELL 128
|
|
|