SitesBLAST
Comparing 350099 FitnessBrowser__Btheta:350099 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
2y27B Crystal structure of paak1 in complex with atp from burkholderia cenocepacia (see paper)
51% identity, 99% coverage: 5:430/432 of query aligns to 5:427/427 of 2y27B
- binding adenosine-5'-triphosphate: K65 (= K65), S90 (= S90), S91 (= S91), G92 (= G92), T93 (= T93), T94 (= T94), F138 (= F138), A211 (= A211), E212 (= E212), P213 (= P213), D232 (= D232), I233 (= I233), Y234 (= Y234), G235 (= G235), L236 (= L236), S237 (= S237), D302 (= D301), I320 (= I322), R323 (= R325), K419 (= K422)
- binding magnesium ion: V200 (≠ E200), S202 (≠ F202), L204 (= L204), M226 (≠ L226), G227 (= G227), Q347 (≠ M349), L350 (≠ F352)
2y4nA Paak1 in complex with phenylacetyl adenylate (see paper)
50% identity, 99% coverage: 5:431/432 of query aligns to 5:426/426 of 2y4nA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: Y131 (= Y133), F136 (= F138), G138 (= G140), G208 (= G210), A209 (= A211), E210 (= E212), P211 (= P213), I231 (= I233), Y232 (= Y234), G233 (= G235), L234 (= L236), S235 (= S237), P240 (= P242), D300 (= D301), R321 (= R325), K417 (= K422)
- binding magnesium ion: V198 (≠ E200), S200 (≠ F202), Q345 (≠ M349), L348 (≠ F352)
2y4oA Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
47% identity, 99% coverage: 5:431/432 of query aligns to 7:433/433 of 2y4oA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ Y133), F140 (= F138), A213 (= A211), E214 (= E212), P215 (= P213), I235 (= I233), G237 (= G235), L238 (= L236), S239 (= S237), P244 (= P242), D304 (= D301), R325 (= R325), I331 (= I331), N336 (= N336)
2y4oB Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
48% identity, 99% coverage: 5:430/432 of query aligns to 7:432/432 of 2y4oB
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ Y133), F140 (= F138), G212 (= G210), A213 (= A211), E214 (= E212), P215 (= P213), I235 (= I233), G237 (= G235), L238 (= L236), S239 (= S237), P244 (= P242), D304 (= D301), R325 (= R325), I331 (= I331), N336 (= N336)
- binding magnesium ion: S204 (≠ F202), V228 (≠ L226)
4r1mA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.48 a resolution
46% identity, 99% coverage: 3:430/432 of query aligns to 7:433/435 of 4r1mA
- binding adenosine monophosphate: A215 (= A211), E216 (= E212), P217 (= P213), N236 (≠ D232), S237 (≠ I233), F238 (≠ Y234), G239 (= G235), M240 (≠ L236), T241 (≠ S237), D305 (= D301), R329 (= R325), I335 (= I331), N340 (= N336)
- binding zinc ion: C252 (= C248), H259 (= H255), C314 (= C310), C316 (= C312)
4r1lA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.42 a resolution
46% identity, 99% coverage: 3:430/432 of query aligns to 7:431/433 of 4r1lA
- binding adenosine-5'-diphosphate: A215 (= A211), E216 (= E212), P217 (= P213), S237 (≠ I233), F238 (≠ Y234), G239 (= G235), M240 (≠ L236), T241 (≠ S237), D305 (= D301), R329 (= R325), N340 (= N336)
- binding adenosine monophosphate: A215 (= A211), E216 (= E212), P217 (= P213), S237 (≠ I233), F238 (≠ Y234), G239 (= G235), M240 (≠ L236), T241 (≠ S237), D305 (= D301), R329 (= R325), N340 (= N336)
- binding coenzyme a: S136 (= S132), A164 (≠ S160), G165 (= G161), N166 (= N162), S167 (≠ T163), I185 (≠ T181), Y188 (= Y184), K337 (≠ R333), T408 (≠ G405)
- binding zinc ion: C252 (= C248), H259 (= H255), C314 (= C310), C316 (= C312)
6he0A Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in complex with 2-hib-amp and coa in the thioesterfication state (see paper)
31% identity, 100% coverage: 3:432/432 of query aligns to 25:466/477 of 6he0A
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] 2-methyl-2-oxidanyl-propanoate: S241 (≠ G210), G242 (≠ A211), E243 (= E212), P244 (= P213), G267 (≠ Y234), S268 (≠ G235), M269 (≠ L236), A270 (≠ S237), D335 (= D301), I357 (= I322), N371 (= N336)
- binding adenosine monophosphate: G242 (≠ A211), E243 (= E212), P244 (= P213), C266 (≠ I233), G267 (≠ Y234), S268 (≠ G235), A270 (≠ S237), E271 (= E238), D335 (= D301), N371 (= N336)
- binding coenzyme a: Y166 (≠ F138), A188 (≠ S160), G189 (= G161), P191 (vs. gap), S194 (≠ T163), Y210 (≠ C179), G211 (≠ C180), T212 (= T181), Y215 (= Y184), H218 (≠ Y187), R368 (= R333), G369 (= G334), M401 (≠ T366), V439 (≠ L404), R440 (≠ G405)
6hdyA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with s3-hb-amp (see paper)
30% identity, 100% coverage: 3:432/432 of query aligns to 25:463/474 of 6hdyA
- binding (3s)-3-hydroxybutanoic acid: Y162 (≠ F138), S237 (≠ G210), G263 (≠ Y234), S264 (≠ G235), M265 (≠ L236), A266 (≠ S237), F271 (vs. gap)
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (3~{S})-3-oxidanylbutanoate: Y162 (≠ F138), G164 (= G140), S237 (≠ G210), G238 (≠ A211), E239 (= E212), P240 (= P213), C262 (≠ I233), G263 (≠ Y234), S264 (≠ G235), A266 (≠ S237), F271 (vs. gap), D331 (= D301), I353 (= I322), R356 (= R325), K453 (= K422)
6hdxA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with r3-hib-amp (see paper)
30% identity, 100% coverage: 3:432/432 of query aligns to 25:463/474 of 6hdxA
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (2~{R})-2-methyl-3-oxidanyl-propanoate: Y162 (≠ F138), G164 (= G140), S237 (≠ G210), G238 (≠ A211), E239 (= E212), P240 (= P213), C262 (≠ I233), G263 (≠ Y234), S264 (≠ G235), A266 (≠ S237), F271 (vs. gap), D331 (= D301), I353 (= I322), R356 (= R325), K453 (= K422)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: Y162 (≠ F138), G164 (= G140), S237 (≠ G210), G263 (≠ Y234), S264 (≠ G235), A266 (≠ S237), F271 (vs. gap)
6siyA Paak family amp-ligase with amp and substrate (see paper)
31% identity, 93% coverage: 15:416/432 of query aligns to 14:401/433 of 6siyA
- binding 3-hydroxyanthranilic acid: T125 (≠ Y133), P126 (≠ G134), T132 (≠ G140), L135 (≠ G143), R153 (≠ G161), N177 (≠ T181), A209 (= A211), E232 (≠ I233), G234 (= G235), S235 (≠ L236)
- binding adenosine monophosphate: S85 (= S91), A209 (= A211), E210 (= E212), P211 (= P213), E232 (≠ I233), Y233 (= Y234), G234 (= G235), S235 (≠ L236), T236 (≠ S237), D296 (= D301), V316 (≠ I322)
- binding magnesium ion: R75 (≠ M81), E76 (≠ S82), L78 (≠ I84), P117 (≠ R125), G144 (= G152), A145 (= A153), T146 (≠ S154)
6sixB Paak family amp-ligase with anp (see paper)
31% identity, 93% coverage: 15:416/432 of query aligns to 18:405/437 of 6sixB
- binding phosphoaminophosphonic acid-adenylate ester: S88 (= S90), S89 (= S91), A213 (= A211), E214 (= E212), P215 (= P213), E236 (≠ I233), Y237 (= Y234), G238 (= G235), S239 (≠ L236), T240 (≠ S237), E241 (= E238), D300 (= D301), V320 (≠ I322), R323 (= R325)
- binding magnesium ion: R79 (≠ M81), E80 (≠ S82), P121 (≠ R125), T150 (≠ S154)
- binding zinc ion: C249 (= C250), H255 (= H255), C309 (= C310), C311 (= C312)
6siwA Paak family amp-ligase with amp (see paper)
31% identity, 93% coverage: 15:416/432 of query aligns to 13:400/432 of 6siwA
- binding adenosine monophosphate: S84 (= S91), A208 (= A211), E209 (= E212), P210 (= P213), E231 (≠ I233), Y232 (= Y234), G233 (= G235), S234 (≠ L236), T235 (≠ S237), D295 (= D301), V315 (≠ I322)
- binding magnesium ion: E75 (≠ S82), L77 (≠ I84), S83 (= S90), P116 (≠ R125), G143 (= G152), T145 (≠ S154), E236 (= E238)
- binding zinc ion: C244 (= C250), H250 (= H255), C304 (= C310), C306 (= C312)
3pbkA Structural and functional studies of fatty acyl-adenylate ligases from e. Coli and l. Pneumophila (see paper)
35% identity, 24% coverage: 322:426/432 of query aligns to 443:542/555 of 3pbkA
Sites not aligning to the query:
- active site: 171, 191, 216, 327, 328
- binding 5'-O-[(S)-(dodecanoyloxy)(hydroxy)phosphoryl]adenosine: 217, 222, 295, 296, 297, 323, 324, 325, 326, 327, 331, 432
P9WQ59 Long-chain-fatty-acid--AMP ligase FadD28; Acyl-AMP synthetase; FAAL28; Long-chain fatty acid adenylyltransferase FadD28; EC 6.2.1.49 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
33% identity, 24% coverage: 322:425/432 of query aligns to 457:563/580 of P9WQ59
Sites not aligning to the query:
- 227 I→W: Shows substantial decrease (69%) in the activity with lauric acid (C12 fatty acid) as substrate but shows a 4-fold higher activity with the long chain fatty acyl capric acid (C10 fatty acid) as substrate.
- 330 G→W: No activity with lauric acid (C12 fatty acid) as substrate. Instead, it catalyzes activation of acetic acid (C2 fatty acid) as acetyl-AMP.
P40806 Polyketide synthase PksJ; PKS from Bacillus subtilis (strain 168) (see paper)
24% identity, 78% coverage: 90:426/432 of query aligns to 195:552/5043 of P40806
Sites not aligning to the query:
- 1689 modified: O-(pantetheine 4'-phosphoryl)serine
Query Sequence
>350099 FitnessBrowser__Btheta:350099
MIWNETIECMDRESLRKIQSIRLKKIVDYVYHNTPFYRKKMQEMGITPDDINTIDDIVKL
PFTTKHDLRDNYPFGLCAVPMSQIVRIHASSGTTGKPTVVGYTRKDLSSWAECISRAFTA
YGAGRSDIFQVSYGYGLFTGGLGAHAGAENIGASVIPMSSGNTEKQITLMHDFGSTVLCC
TPSYALYLADAIKDSGYPREEFQLKVGALGAEPWTENMRHEIEEKLGIKAYDIYGLSEIA
GPGVGYECECQHGTHLNEDHYFPEIIDPNTLQPVEPGQTGELVFTHLTKEGMPLLRYRTR
DLTALHYDKCSCGRTLVRMDRILGRSDDMLIIRGVNVFPTQIESVILEMEEFEPHYLLIV
GRENNTDTMELQVEVRPDFYSDEINRMLALKKKLASRLQSVLGLGVNVKLVEPRSIERSV
GKAKRVIDNRKI
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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