SitesBLAST
Comparing WP_014026302.1 NCBI__GCF_000223395.1:WP_014026302.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
3vpbB Argx from sulfolobus tokodaii complexed with lysw/glu/adp/mg/zn/sulfate (see paper)
49% identity, 98% coverage: 3:277/282 of query aligns to 2:277/282 of 3vpbB
- binding adenosine-5'-diphosphate: K87 (= K87), I125 (≠ V125), K127 (= K127), S132 (= S132), G134 (= G134), V137 (= V137), Q167 (= Q167), Y169 (= Y169), I170 (≠ V170), D176 (= D176), R200 (= R200), A201 (≠ S201), N202 (= N202), N249 (= N249), E250 (= E250)
- binding glutamic acid: Y190 (≠ I190), R192 (= R192), N202 (= N202), V203 (= V203), A204 (= A204), E256 (= E256), G259 (= G259)
- binding magnesium ion: D237 (= D237), E250 (= E250)
- binding zinc ion: E250 (= E250), N252 (= N252)
Q970U6 Glutamate--LysW ligase ArgX; EC 6.3.2.- from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see paper)
49% identity, 98% coverage: 3:277/282 of query aligns to 2:277/282 of Q970U6
- D237 (= D237) binding Mg(2+)
- E250 (= E250) binding Mg(2+); binding Mg(2+)
- N252 (= N252) binding Mg(2+)
5k2mI Bifunctional lysx/argx from thermococcus kodakarensis with lysw-gamma- aaa (see paper)
41% identity, 99% coverage: 3:281/282 of query aligns to 2:272/273 of 5k2mI
- binding adenosine-5'-diphosphate: K83 (= K87), V120 (= V125), K122 (= K127), S127 (= S132), L132 (≠ V137), Q162 (= Q167), V165 (= V170), K167 (≠ T172), D171 (= D176), W192 (= W199), I193 (≠ R200), T194 (≠ S201), N195 (= N202), F231 (= F239), N240 (= N249), E241 (= E250)
- binding 2-aminohexanedioic acid: R173 (= R178), N195 (= N202), T196 (≠ V203), A197 (= A204), E247 (= E256), F248 (= F257), N250 (≠ G259)
- binding : V51 (≠ T55), S52 (= S56), H53 (≠ M57), F54 (= F58), F125 (≠ I130), W128 (= W133), R130 (= R135), N153 (= N158), Y156 (≠ M161), N245 (≠ I254)
5k2mG Bifunctional lysx/argx from thermococcus kodakarensis with lysw-gamma- aaa (see paper)
41% identity, 99% coverage: 3:281/282 of query aligns to 2:272/273 of 5k2mG
- binding adenosine-5'-diphosphate: K83 (= K87), V120 (= V125), K122 (= K127), S127 (= S132), G129 (= G134), Q162 (= Q167), V165 (= V170), K167 (≠ T172), D171 (= D176), W192 (= W199), T194 (≠ S201), N195 (= N202), F231 (= F239), N240 (= N249), E241 (= E250)
- binding magnesium ion: D229 (= D237), E241 (= E250)
- binding : V51 (≠ T55), S52 (= S56), H53 (≠ M57), F54 (= F58), F125 (≠ I130), S127 (= S132), W128 (= W133), R130 (= R135), Y156 (≠ M161), R173 (= R178), R187 (= R192), T196 (≠ V203), A197 (= A204), N243 (= N252), P244 (≠ G253), N245 (≠ I254), E247 (= E256), F248 (= F257), N250 (≠ G259), A251 (≠ F260)
Q4JAP9 Alpha-aminoadipate--LysW ligase LysX; AAA--LysW ligase LysX; EC 6.3.2.43 from Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) (see paper)
35% identity, 95% coverage: 11:278/282 of query aligns to 1:276/276 of Q4JAP9
- NT 253:254 (≠ GF 259:260) mutation to GF: Alters substrate specificity, so that glutamate is preferred over alpha-aminoadipate.
3vpdA Lysx from thermus thermophilus complexed with amp-pnp (see paper)
34% identity, 99% coverage: 4:281/282 of query aligns to 2:280/281 of 3vpdA
- binding phosphoaminophosphonic acid-adenylate ester: V127 (= V125), K129 (= K127), W135 (= W133), G136 (= G134), L139 (≠ V137), Q169 (= Q167), V172 (= V170), K174 (≠ T172), D178 (= D176), R194 (= R192), W199 (= W199), T201 (≠ S201), F239 (= F239), E249 (= E250)
- binding butanoic acid: F256 (= F257), K257 (= K258), N258 (≠ G259), S259 (≠ F260)
1uc9A Crystal structure of a lysine biosynthesis enzyme, lysx, from thermus thermophilus hb8 (see paper)
30% identity, 98% coverage: 4:279/282 of query aligns to 2:254/256 of 1uc9A
4iwxA Rimk structure at 2.85a (see paper)
32% identity, 83% coverage: 45:277/282 of query aligns to 58:289/294 of 4iwxA
- binding adenosine-5'-diphosphate: V141 (= V125), K143 (= K127), E180 (= E168), Y181 (= Y169), I182 (≠ V170), K183 (vs. gap), D189 (= D176), R213 (= R200), S214 (= S201), N215 (= N202), M261 (≠ N249), E262 (= E250)
- binding glutamic acid: R98 (≠ Y83), R104 (≠ L89), Q107 (≠ S92), L108 (= L93), R111 (= R96)
5zctH The crystal structure of the poly-alpha-l-glutamate peptides synthetase rimk at 2.05 angstrom resolution. (see paper)
32% identity, 83% coverage: 45:277/282 of query aligns to 56:287/292 of 5zctH
- binding phosphoaminophosphonic acid-adenylate ester: V139 (= V125), K141 (= K127), Q177 (= Q167), Y179 (= Y169), I180 (≠ V170), D187 (= D176), F210 (≠ W199), R211 (= R200), S212 (= S201), N213 (= N202), R216 (≠ L205), L250 (≠ F239), M259 (≠ N249), E260 (= E250)
- binding magnesium ion: D248 (= D237), E260 (= E250)
5zctA The crystal structure of the poly-alpha-l-glutamate peptides synthetase rimk at 2.05 angstrom resolution. (see paper)
32% identity, 83% coverage: 45:277/282 of query aligns to 56:287/292 of 5zctA
- binding phosphoaminophosphonic acid-adenylate ester: K100 (= K87), K141 (= K127), T146 (≠ S132), Q147 (≠ W133), G148 (= G134), Q177 (= Q167), Y179 (= Y169), I180 (≠ V170), R211 (= R200), S212 (= S201), N213 (= N202), L250 (≠ F239), M259 (≠ N249)
7qyrD Crystal structure of rimk from pseudomonas aeruginosa pao1 (see paper)
31% identity, 94% coverage: 12:277/282 of query aligns to 25:287/293 of 7qyrD
- binding adenosine-5'-diphosphate: V139 (= V125), Y179 (= Y169), I180 (≠ V170), D187 (= D176), R211 (= R200), S212 (= S201), L250 (≠ F239), M259 (≠ N249)
- binding : R64 (= R53), R189 (= R178), N262 (= N252), S264 (≠ I254), G266 (≠ E256)
Sites not aligning to the query:
Query Sequence
>WP_014026302.1 NCBI__GCF_000223395.1:WP_014026302.1
MTRVALAYDYLRQEEKLVIEALREVGLEVKMLPVTEKPFHIGGEPDIDLVVVRTTSMFNG
LYTAAAYESMGIRSINQSRTILYSGDKALTYSLLARAKIPTPDTYIALGSRAVFEAAKLL
GYPLVDKPPIGSWGRLVSLIYDDFNLVTVVEHREALCNRQMRIHVMQEYVETGNKDIRCL
VLGGELLGCIYRIAREGEWRSNVALGGHTEVVDVTPDLENLVLRAAAVVEGDFVSIDVFE
HPEKGYVVNEVNGIPEFKGFMRATGVNVARKLAEYVKSLVKA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory