SitesBLAST
Comparing BPHYT_RS17360 FitnessBrowser__BFirm:BPHYT_RS17360 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
2y27B Crystal structure of paak1 in complex with atp from burkholderia cenocepacia (see paper)
92% identity, 98% coverage: 5:430/434 of query aligns to 2:427/427 of 2y27B
- binding adenosine-5'-triphosphate: K65 (= K68), S90 (= S93), S91 (= S94), G92 (= G95), T93 (= T96), T94 (= T97), F138 (= F141), A211 (= A214), E212 (= E215), P213 (= P216), D232 (= D235), I233 (= I236), Y234 (= Y237), G235 (= G238), L236 (= L239), S237 (= S240), D302 (= D305), I320 (= I323), R323 (= R326), K419 (= K422)
- binding magnesium ion: V200 (≠ A203), S202 (≠ C205), L204 (= L207), M226 (= M229), G227 (= G230), Q347 (= Q350), L350 (= L353)
2y4nA Paak1 in complex with phenylacetyl adenylate (see paper)
91% identity, 98% coverage: 5:431/434 of query aligns to 2:426/426 of 2y4nA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: Y131 (= Y136), F136 (= F141), G138 (= G143), G208 (= G213), A209 (= A214), E210 (= E215), P211 (= P216), I231 (= I236), Y232 (= Y237), G233 (= G238), L234 (= L239), S235 (= S240), P240 (= P245), D300 (= D305), R321 (= R326), K417 (= K422)
- binding magnesium ion: V198 (≠ A203), S200 (≠ C205), Q345 (= Q350), L348 (= L353)
2y4oA Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
69% identity, 99% coverage: 4:431/434 of query aligns to 3:433/433 of 2y4oA
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ Y136), F140 (= F141), A213 (= A214), E214 (= E215), P215 (= P216), I235 (= I236), G237 (= G238), L238 (= L239), S239 (= S240), P244 (= P245), D304 (= D305), R325 (= R326), I331 (= I332), N336 (= N337)
2y4oB Crystal structure of paak2 in complex with phenylacetyl adenylate (see paper)
69% identity, 98% coverage: 4:430/434 of query aligns to 3:432/432 of 2y4oB
- binding 5'-o-[hydroxy(phenylacetyl)phosphoryl]adenosine: F135 (≠ Y136), F140 (= F141), G212 (= G213), A213 (= A214), E214 (= E215), P215 (= P216), I235 (= I236), G237 (= G238), L238 (= L239), S239 (= S240), P244 (= P245), D304 (= D305), R325 (= R326), I331 (= I332), N336 (= N337)
- binding magnesium ion: S204 (≠ C205), V228 (≠ M229)
4r1mA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.48 a resolution
42% identity, 99% coverage: 1:430/434 of query aligns to 2:433/435 of 4r1mA
- binding adenosine monophosphate: A215 (= A214), E216 (= E215), P217 (= P216), N236 (≠ D235), S237 (≠ I236), F238 (≠ Y237), G239 (= G238), M240 (≠ L239), T241 (≠ S240), D305 (= D305), R329 (= R326), I335 (= I332), N340 (= N337)
- binding zinc ion: C252 (= C251), H259 (≠ T259), C314 (≠ A314), C316 (vs. gap)
4r1lA Crystal structure of a putative acyl-coa ligase (bt_0428) from bacteroides thetaiotaomicron vpi-5482 at 2.42 a resolution
42% identity, 99% coverage: 1:430/434 of query aligns to 2:431/433 of 4r1lA
- binding adenosine-5'-diphosphate: A215 (= A214), E216 (= E215), P217 (= P216), S237 (≠ I236), F238 (≠ Y237), G239 (= G238), M240 (≠ L239), T241 (≠ S240), D305 (= D305), R329 (= R326), N340 (= N337)
- binding adenosine monophosphate: A215 (= A214), E216 (= E215), P217 (= P216), S237 (≠ I236), F238 (≠ Y237), G239 (= G238), M240 (≠ L239), T241 (≠ S240), D305 (= D305), R329 (= R326), N340 (= N337)
- binding coenzyme a: S136 (= S135), A164 (≠ G163), G165 (= G164), N166 (≠ Q165), S167 (≠ T166), I185 (≠ T184), Y188 (= Y187), K337 (≠ R334), T408 (≠ S405)
- binding zinc ion: C252 (= C251), H259 (≠ T259), C314 (≠ A314), C316 (vs. gap)
6he0A Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in complex with 2-hib-amp and coa in the thioesterfication state (see paper)
34% identity, 94% coverage: 23:432/434 of query aligns to 42:466/477 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 (≠ G213), G242 (≠ A214), E243 (= E215), P244 (= P216), G267 (≠ Y237), S268 (≠ G238), M269 (≠ L239), A270 (≠ S240), D335 (= D305), I357 (= I323), N371 (= N337)
- binding adenosine monophosphate: G242 (≠ A214), E243 (= E215), P244 (= P216), C266 (≠ I236), G267 (≠ Y237), S268 (≠ G238), A270 (≠ S240), E271 (= E241), D335 (= D305), N371 (= N337)
- binding coenzyme a: Y166 (≠ F141), A188 (≠ G163), G189 (vs. gap), P191 (vs. gap), S194 (≠ T166), Y210 (≠ M182), G211 (≠ V183), T212 (= T184), Y215 (= Y187), H218 (≠ S190), R368 (= R334), G369 (= G335), M401 (≠ L367), V439 (= V404), R440 (≠ S405)
6hdyA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with s3-hb-amp (see paper)
33% identity, 94% coverage: 23:432/434 of query aligns to 42:463/474 of 6hdyA
- binding (3s)-3-hydroxybutanoic acid: Y162 (≠ F141), S237 (≠ G213), G263 (≠ Y237), S264 (≠ G238), M265 (≠ L239), A266 (≠ S240), F271 (≠ P245)
- 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 (≠ F141), G164 (= G143), S237 (≠ G213), G238 (≠ A214), E239 (= E215), P240 (= P216), C262 (≠ I236), G263 (≠ Y237), S264 (≠ G238), A266 (≠ S240), F271 (≠ P245), D331 (= D305), I353 (= I323), R356 (= R326), K453 (= K422)
6hdxA Crystal structure of 2-hydroxyisobutyryl-coa ligase (hcl) in the postadenylation state in complex with r3-hib-amp (see paper)
33% identity, 94% coverage: 23:432/434 of query aligns to 42:463/474 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 (≠ F141), G164 (= G143), S237 (≠ G213), G238 (≠ A214), E239 (= E215), P240 (= P216), C262 (≠ I236), G263 (≠ Y237), S264 (≠ G238), A266 (≠ S240), F271 (≠ P245), D331 (= D305), I353 (= I323), R356 (= R326), K453 (= K422)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: Y162 (≠ F141), G164 (= G143), S237 (≠ G213), G263 (≠ Y237), S264 (≠ G238), A266 (≠ S240), F271 (≠ P245)
6siyA Paak family amp-ligase with amp and substrate (see paper)
30% identity, 84% coverage: 13:375/434 of query aligns to 9:366/433 of 6siyA
- binding 3-hydroxyanthranilic acid: T125 (≠ Y136), P126 (≠ G137), T132 (≠ G143), L135 (≠ G146), R153 (≠ Q165), N177 (≠ T184), A209 (= A214), E232 (≠ I236), G234 (= G238), S235 (≠ L239)
- binding adenosine monophosphate: S85 (= S94), A209 (= A214), E210 (= E215), P211 (= P216), E232 (≠ I236), Y233 (= Y237), G234 (= G238), S235 (≠ L239), T236 (≠ S240), D296 (= D305), V316 (≠ I323)
- binding magnesium ion: R75 (≠ Q84), E76 (= E85), L78 (≠ I87), P117 (≠ R128), G144 (= G155), A145 (≠ L156), T146 (= T157)
6sixB Paak family amp-ligase with anp (see paper)
30% identity, 84% coverage: 13:375/434 of query aligns to 13:370/437 of 6sixB
- binding phosphoaminophosphonic acid-adenylate ester: S88 (= S93), S89 (= S94), A213 (= A214), E214 (= E215), P215 (= P216), E236 (≠ I236), Y237 (= Y237), G238 (= G238), S239 (≠ L239), T240 (≠ S240), E241 (= E241), D300 (= D305), V320 (≠ I323), R323 (= R326)
- binding magnesium ion: R79 (≠ Q84), E80 (= E85), P121 (≠ R128), T150 (= T157)
- binding zinc ion: C249 (= C251), H255 (≠ T259), C309 (≠ G312), C311 (≠ A314)
6siwA Paak family amp-ligase with amp (see paper)
30% identity, 84% coverage: 13:375/434 of query aligns to 8:365/432 of 6siwA
- binding adenosine monophosphate: S84 (= S94), A208 (= A214), E209 (= E215), P210 (= P216), E231 (≠ I236), Y232 (= Y237), G233 (= G238), S234 (≠ L239), T235 (≠ S240), D295 (= D305), V315 (≠ I323)
- binding magnesium ion: E75 (= E85), L77 (≠ I87), S83 (= S93), P116 (≠ R128), G143 (= G155), T145 (= T157), E236 (= E241)
- binding zinc ion: C244 (= C251), H250 (≠ T259), C304 (≠ G312), C306 (≠ A314)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
25% identity, 47% coverage: 85:288/434 of query aligns to 188:390/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (≠ Y136), F245 (≠ Y138), T249 (= T142), G314 (≠ A214), A315 (≠ E215), P316 (= P216), G337 (≠ I236), Y338 (= Y237), G339 (= G238), L340 (= L239), T341 (≠ S240), A346 (≠ P245)
Sites not aligning to the query:
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
25% identity, 47% coverage: 85:288/434 of query aligns to 188:390/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (≠ Y136), F245 (≠ Y138), T249 (= T142), G314 (≠ A214), A315 (≠ E215), P316 (= P216), G337 (≠ I236), Y338 (= Y237), G339 (= G238), L340 (= L239), T341 (≠ S240), S345 (≠ G244), A346 (≠ P245)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y138), R335 (vs. gap), G337 (≠ I236), G339 (= G238), L340 (= L239), A346 (≠ P245)
Sites not aligning to the query:
1t5dX 4-chlorobenzoyl-coa ligase/synthetase bound to 4-chlorobenzoate (see paper)
26% identity, 41% coverage: 170:347/434 of query aligns to 235:419/502 of 1t5dX
Sites not aligning to the query:
3cw8X 4-chlorobenzoyl-coa ligase/synthetase, bound to 4cba-adenylate (see paper)
26% identity, 41% coverage: 170:347/434 of query aligns to 237:421/501 of 3cw8X
- binding 5'-O-[(S)-{[(4-chlorophenyl)carbonyl]oxy}(hydroxy)phosphoryl]adenosine: G281 (≠ A214), A282 (≠ E215), T283 (≠ P216), I303 (= I236), Y304 (= Y237), G305 (= G238), T306 (≠ L239), T307 (≠ S240), M310 (= M243), N311 (≠ G244), M324 (≠ W261), D385 (= D305)
Sites not aligning to the query:
3cw9A 4-chlorobenzoyl-coa ligase/synthetase in the thioester-forming conformation, bound to 4-chlorophenacyl-coa (see paper)
26% identity, 41% coverage: 170:347/434 of query aligns to 237:421/503 of 3cw9A
- active site: T307 (≠ S240), E308 (= E241), I406 (= I332), N411 (= N337)
- binding 4-Chlorophenacyl-coenzyme A: A280 (≠ G213), G305 (= G238), T306 (≠ L239), M310 (= M243), N311 (≠ G244), S407 (≠ V333), G408 (≠ R334), G409 (= G335), E410 (≠ V336)
- binding adenosine monophosphate: G281 (≠ A214), A282 (≠ E215), T283 (≠ P216), I303 (= I236), Y304 (= Y237), G305 (= G238), T306 (≠ L239), T307 (≠ S240), D385 (= D305), R400 (= R326), I406 (= I332), N411 (= N337)
Sites not aligning to the query:
- active site: 161, 181, 207, 492
- binding 4-Chlorophenacyl-coenzyme A: 87, 203, 204, 207, 208, 209, 440, 473, 475, 477
- binding adenosine monophosphate: 161
6m2uA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-chloro-1,3-thiazole-5-carboxylate-amp (see paper)
24% identity, 59% coverage: 93:350/434 of query aligns to 176:440/518 of 6m2uA
- active site: S176 (= S93), T196 (≠ W113), T324 (≠ S240), E325 (= E241), K422 (≠ I332), Y427 (≠ N337)
- binding adenosine monophosphate: G298 (≠ A214), E299 (= E215), A300 (≠ P216), D319 (= D235), G320 (≠ I236), I321 (≠ Y237), G322 (= G238), T324 (≠ S240), D401 (≠ P311), R416 (= R326), K422 (≠ I332), Y427 (≠ N337)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ G143), A297 (≠ G213), G322 (= G238), S323 (≠ L239), A328 (≠ G244)
Sites not aligning to the query:
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
24% identity, 59% coverage: 93:350/434 of query aligns to 176:440/518 of 6m2tA
- active site: S176 (= S93), T196 (≠ W113), T324 (≠ S240), E325 (= E241), K422 (≠ I332), Y427 (≠ N337)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ G143), G322 (= G238), S323 (≠ L239), A328 (≠ G244)
- binding adenosine monophosphate: G298 (≠ A214), E299 (= E215), A300 (≠ P216), G320 (≠ I236), I321 (≠ Y237), S323 (≠ L239), T324 (≠ S240), D401 (≠ P311), R416 (= R326), K422 (≠ I332), Y427 (≠ N337)
Sites not aligning to the query:
3vnqA Co-crystal structure of nrps adenylation protein cytc1 with atp from streptomyces
29% identity, 60% coverage: 85:344/434 of query aligns to 143:414/497 of 3vnqA
- binding adenosine-5'-triphosphate: T151 (≠ S93), S152 (= S94), G153 (= G95), T154 (= T96), T155 (= T97), K159 (≠ T101), G269 (≠ A214), E270 (= E215), K271 (≠ P216), Y295 (= Y237), G296 (= G238), I297 (≠ L239), D381 (= D305), Y393 (≠ M317), R396 (= R326)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS17360 FitnessBrowser__BFirm:BPHYT_RS17360
MTTALPLDPIETASRDELAALQLERLKWSLNHAYENSPVYRHKFDEAGVHPSEVKTLADL
ARFPFTTKKDLRDSYPFGMFAVPQEQISRIHASSGTTGKPTVVGYTARDIDTWANLVARS
VRAAGAKRGDKVHISYGYGLFTGGLGAHYGAERAGLTVIPFGGGQTEKQVQLIQDFRPDI
IMVTPSYMLSIADELERQGVDPANCSLRIGIFGAEPWTNDMRQAIEKRMGIDAVDIYGLS
EVMGPGVASECVETKDGPTIWEDHFYPEIIDPETGEVLPDGELGELVFTSLTKEALPIVR
YRTRDLTRLLPGSARTMRRMEKITGRSDDMMIVRGVNVFPTQIEELLLKQRALAPHYQIV
LTKEGPLDVLTLNVEPCPESAPDTAALSTAKQALAYDIKALIGVSAVVNVLAVNGIERSV
GKARRVVDKRKLGL
Or try a new SitesBLAST search
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