SitesBLAST
Comparing Pf1N1B4_225 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_225 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
44% identity, 100% coverage: 4:653/653 of query aligns to 2:653/654 of P9WPQ3
- K322 (≠ P322) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7ybuA Human propionyl-coenzyme a carboxylase
42% identity, 100% coverage: 3:653/653 of query aligns to 4:670/670 of 7ybuA
P05165 Propionyl-CoA carboxylase alpha chain, mitochondrial; PCCase subunit alpha; Propanoyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.3 from Homo sapiens (Human) (see 6 papers)
42% identity, 100% coverage: 3:653/653 of query aligns to 62:728/728 of P05165
- A75 (= A16) to P: in PA-1; dbSNP:rs794727479
- R77 (= R18) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A79) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I105) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G138) to E: in PA-1
- M229 (= M170) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q238) to R: in PA-1
- D368 (= D309) to G: in PA-1
- M373 (≠ Q314) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G320) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V339) to R: in PA-1
- R399 (= R340) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P362) to L: in PA-1; dbSNP:rs1443858896
- L532 (= L469) natural variant: Missing (in PA-1)
- V551 (vs. gap) to F: in dbSNP:rs61749895
- W559 (= W485) to L: in PA-1; dbSNP:rs118169528
- G631 (= G564) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G593) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K619) modified: N6-biotinyllysine; by HLCS
- C712 (≠ V637) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
Q5LUF3 Propionyl-CoA carboxylase alpha chain; EC 6.4.1.3 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
42% identity, 100% coverage: 4:653/653 of query aligns to 2:681/681 of Q5LUF3
- F348 (= F350) binding
- W515 (≠ Y495) mutation to L: No effect on holoenzyme formation.
- L599 (≠ R571) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (≠ A574) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (≠ L575) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K619) modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
41% identity, 100% coverage: 4:653/653 of query aligns to 1:646/646 of 3n6rG
- active site: K115 (= K118), K157 (= K160), D180 (= D197), H193 (= H210), R219 (= R236), T258 (= T275), E260 (= E277), E273 (= E290), N275 (= N292), R277 (= R294), E281 (= E298), R323 (= R340), G519 (vs. gap)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M618), K612 (= K619)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
39% identity, 99% coverage: 7:653/653 of query aligns to 1:657/657 of 8sgxX
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
50% identity, 67% coverage: 4:443/653 of query aligns to 2:437/442 of 4mv4A
- active site: K116 (= K118), K159 (= K160), D193 (= D197), H206 (= H210), R232 (= R236), T271 (= T275), E273 (= E277), E285 (= E290), N287 (= N292), R289 (= R294), E293 (= E298), R335 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K160), G164 (= G165), M166 (= M170), E198 (= E202), Y200 (≠ A204), L201 (= L205), H233 (= H237), L275 (= L279), E285 (= E290)
- binding magnesium ion: E273 (= E277), E285 (= E290)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
51% identity, 67% coverage: 4:443/653 of query aligns to 2:438/444 of 2vr1A
- active site: K116 (= K118), K159 (= K160), D194 (= D197), H207 (= H210), R233 (= R236), T272 (= T275), E274 (= E277), E286 (= E290), N288 (= N292), R290 (= R294), E294 (= E298), R336 (= R340)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K160), R165 (= R168), M167 (= M170), Y201 (≠ A204), L202 (= L205), E274 (= E277), L276 (= L279), E286 (= E290), N288 (= N292), I435 (≠ T440)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
49% identity, 67% coverage: 4:443/653 of query aligns to 2:434/439 of 4mv3A
- active site: K116 (= K118), K159 (= K160), D190 (= D197), H203 (= H210), R229 (= R236), T268 (= T275), E270 (= E277), E282 (= E290), N284 (= N292), R286 (= R294), E290 (= E298), R332 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K160), M163 (= M170), E195 (= E202), Y197 (≠ A204), L198 (= L205), E270 (= E277), L272 (= L279), E282 (= E290)
- binding bicarbonate ion: R286 (= R294), Q288 (= Q296), V289 (= V297)
6oi8A Crystal structure of haemophilus influenzae biotin carboxylase complexed with 7-((1r,5s,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl)- 6-(2-chloro-6-(pyridin-3-yl)phenyl)pyrido[2,3-d]pyrimidin-2-amine (see paper)
49% identity, 67% coverage: 4:443/653 of query aligns to 2:435/440 of 6oi8A
- active site: K116 (= K118), K159 (= K160), D191 (= D197), H204 (= H210), R230 (= R236), T269 (= T275), E271 (= E277), E283 (= E290), N285 (= N292), R287 (= R294), E291 (= E298), R333 (= R340)
- binding 7-[(1R,5S,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl]-6-[2-chloro-6-(pyridin-3-yl)phenyl]pyrido[2,3-d]pyrimidin-2-amine: I157 (≠ M158), K159 (= K160), M164 (= M170), E196 (= E202), Y198 (≠ A204), L199 (= L205), H204 (= H210), Q228 (= Q234), E271 (= E277), L273 (= L279), E283 (= E290), I432 (≠ T440)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
48% identity, 67% coverage: 5:443/653 of query aligns to 1:440/448 of 2vpqB
- active site: V116 (≠ L120), K156 (= K160), H206 (= H210), R232 (= R236), T271 (= T275), E273 (= E277), E287 (= E290), N289 (= N292), R291 (= R294), E295 (= E298), R337 (= R340)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K118), I154 (≠ M158), K156 (= K160), G161 (= G165), G163 (= G167), I166 (≠ M170), F200 (≠ A204), I201 (≠ L205), E273 (= E277), I275 (≠ L279), M286 (≠ L289), E287 (= E290)
- binding magnesium ion: E273 (= E277), E287 (= E290)
6ojhA Crystal structure of haemophilus influenzae biotin carboxylase complexed with (r)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl) pyrido[2,3-d]pyrimidin-2-amine
51% identity, 67% coverage: 4:443/653 of query aligns to 2:440/445 of 6ojhA
- active site: K116 (= K118), K159 (= K160), D196 (= D197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding calcium ion: E276 (= E277), E288 (= E290), N290 (= N292)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K160), M169 (= M170), E201 (= E202), Y203 (≠ A204), L204 (= L205), H236 (= H237), L278 (= L279), E288 (= E290), I437 (≠ T440)
P43873 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
51% identity, 67% coverage: 4:443/653 of query aligns to 2:440/448 of P43873
- K116 (= K118) binding
- K159 (= K160) binding
- EKYL 201:204 (≠ EQAL 202:205) binding
- E276 (= E277) binding ; binding
- E288 (= E290) binding ; binding
- N290 (= N292) binding
6oi9A Crystal structure of e. Coli biotin carboxylase complexed with 7-[3- (aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3- d]pyrimidin-2-amine (see paper)
52% identity, 66% coverage: 4:436/653 of query aligns to 2:433/446 of 6oi9A
- active site: E276 (= E277), E288 (= E290), N290 (= N292), E296 (= E298), R338 (= R340)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K160), M169 (= M170), E201 (= E202), Y203 (≠ A204), L204 (= L205), H209 (= H210), Q233 (= Q234), H236 (= H237), E276 (= E277), L278 (= L279), E288 (= E290)
Sites not aligning to the query:
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
52% identity, 66% coverage: 4:436/653 of query aligns to 2:433/446 of 2w71A
- active site: K116 (= K118), K159 (= K160), D196 (= D197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K160), Y203 (≠ A204), L204 (= L205), H209 (= H210), Q233 (= Q234), H236 (= H237), L278 (= L279)
Sites not aligning to the query:
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
52% identity, 66% coverage: 4:436/653 of query aligns to 2:433/446 of 2w70A
- active site: K116 (= K118), K159 (= K160), D196 (= D197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ M158), K159 (= K160), G166 (= G167), M169 (= M170), E201 (= E202), Y203 (≠ A204), L204 (= L205), L278 (= L279)
2w6zA Crystal structure of biotin carboxylase from e. Coli in complex with the 3-(3-methyl-but-2-enyl)-3h-purin-6-ylamine fragment (see paper)
52% identity, 66% coverage: 4:436/653 of query aligns to 2:433/446 of 2w6zA
- active site: K116 (= K118), K159 (= K160), D196 (= D197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 3-(3-methylbut-2-en-1-yl)-3H-purin-6-amine: K159 (= K160), Y203 (≠ A204), L204 (= L205), L278 (= L279)
2w6qA Crystal structure of biotin carboxylase from e. Coli in complex with the triazine-2,4-diamine fragment (see paper)
52% identity, 66% coverage: 4:436/653 of query aligns to 2:433/446 of 2w6qA
- active site: K116 (= K118), K159 (= K160), D196 (= D197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine: I157 (≠ M158), K159 (= K160), E201 (= E202), K202 (≠ Q203), Y203 (≠ A204), L204 (= L205), H236 (= H237), L278 (= L279)
2w6pA Crystal structure of biotin carboxylase from e. Coli in complex with 5-methyl-6-phenyl-quinazoline-2,4-diamine (see paper)
52% identity, 66% coverage: 4:436/653 of query aligns to 2:433/446 of 2w6pA
- active site: K116 (= K118), K159 (= K160), D196 (= D197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding 5-methyl-6-phenylquinazoline-2,4-diamine: K159 (= K160), Y203 (≠ A204), L204 (= L205), Q233 (= Q234), H236 (= H237), L278 (= L279)
Sites not aligning to the query:
2w6mA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
52% identity, 66% coverage: 4:436/653 of query aligns to 2:433/446 of 2w6mA
- active site: K116 (= K118), K159 (= K160), D196 (= D197), H209 (= H210), R235 (= R236), T274 (= T275), E276 (= E277), E288 (= E290), N290 (= N292), R292 (= R294), E296 (= E298), R338 (= R340)
- binding (2-amino-1,3-oxazol-5-yl)-(3-bromophenyl)methanone: I157 (≠ M158), K159 (= K160), M169 (= M170), E201 (= E202), K202 (≠ Q203), Y203 (≠ A204), H236 (= H237), L278 (= L279)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_225 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_225
MPAFSKILIANRGEIACRIQRTAQALGYRTVAVFSDADADALHVQMADEAVNIGPAPVQQ
SYLNIQAIIDAARRTGADAIHPGYGFLSENAEFARACQQAGIIFIGPSPEAIELMGSKRL
SKLAMIKAGVPCIKGYQGSEQDDATLSREAERIGYPLMIKASAGGGGRGMRLVHSAGELL
EQLRTARSEAQHGFGSDELILEQALIDPRHVEVQVFGDQHGNLIYLGERDCSIQRRHQKI
IEEAPCPVMTADLRQAMGEAALKAGRAVNYVGAGTVEFLLDARGQFYFLEMNTRLQVEHP
VTELITGLDLVAWQFHVAEGLPLPLQQEQVQLNGHAMEVRLYAEDPAQGFLPQTGRIAAW
EPALPGGVRIDHGLIEGQSVSPFYDPMLGKLIAHGATREEARRKLLRAVQDSVLLGVQSN
QRLLACLLEHPQFISGKFSTGFIPTHFADHPCLHPHVPSAEELAIAAALFYQASAQAHRT
PLAGWRNNASVPLHYRIGLEDQDWPVELNAEPGKPYRAQIGARTLELKVIQCDGRWATLE
IDGIRQRHAYRLKAGQLWLFTRPGSLRLVDRTQALVSGQASVSSGTLKAPMDGAIVDVLV
SEGSPVSKGQLLVVLEAMKMEHPLKSGIDGVLKRLQVRVGDQVKNRQILLEVE
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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