SitesBLAST
Comparing HSERO_RS22345 FitnessBrowser__HerbieS:HSERO_RS22345 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)
3va7A Crystal structure of the kluyveromyces lactis urea carboxylase (see paper)
41% identity, 84% coverage: 181:1199/1207 of query aligns to 110:1129/1130 of 3va7A
- active site: H138 (= H207), E205 (= E274), E219 (= E288), N221 (= N290), V226 (= V295), E227 (= E296), R269 (= R340), A550 (≠ T621), I648 (≠ L717), L730 (= L794), D760 (= D821), N762 (≠ V823), F895 (≠ Y957)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y633 (= Y702), T641 (= T710), P653 (= P722), G656 (= G725), F658 (= F727), P943 (= P1004), G944 (= G1005), K1096 (= K1166)
- binding urea: D893 (= D955), Y937 (= Y999), G944 (= G1005), G945 (= G1006), Y946 (= Y1007)
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)
47% identity, 37% coverage: 1:442/1207 of query aligns to 1:458/681 of Q5LUF3
Sites not aligning to the query:
- 515 W→L: No effect on holoenzyme formation.
- 599 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 602 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 603 M→A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- 647 modified: N6-biotinyllysine
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
47% identity, 37% coverage: 2:442/1207 of query aligns to 1:423/646 of 3n6rG
- active site: K115 (= K116), K157 (= K157), D180 (≠ A194), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E288), N275 (= N290), R277 (= R292), E281 (= E296), R323 (= R340)
Sites not aligning to the query:
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
46% identity, 37% coverage: 1:447/1207 of query aligns to 1:445/654 of P9WPQ3
- K322 (≠ L320) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
43% identity, 37% coverage: 5:447/1207 of query aligns to 3:442/448 of 2vpqB
- active site: V116 (≠ T118), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E288), N289 (= N290), R291 (= R292), E295 (= E296), R337 (= R340)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (≠ M167), F200 (≠ Y201), I201 (= I202), E273 (= E274), I275 (≠ V276), M286 (≠ L287), E287 (= E288)
- binding magnesium ion: E273 (= E274), E287 (= E288)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:440/444 of 2vr1A
- active site: K116 (= K116), K159 (= K157), D194 (≠ A194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R340)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (≠ I165), M167 (= M167), Y201 (= Y201), L202 (≠ I202), E274 (= E274), L276 (≠ V276), E286 (= E288), N288 (= N290), I435 (≠ T442)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
41% identity, 37% coverage: 1:447/1207 of query aligns to 1:439/442 of 4mv4A
- active site: K116 (= K116), K159 (= K157), D193 (≠ A194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E288), N287 (= N290), R289 (= R292), E293 (= E296), R335 (= R340)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G162), M166 (= M167), E198 (= E199), Y200 (= Y201), L201 (≠ I202), H233 (≠ N234), L275 (≠ V276), E285 (= E288)
- binding magnesium ion: E273 (= E274), E285 (= E288)
7ybuA Human propionyl-coenzyme a carboxylase
41% identity, 37% coverage: 2:448/1207 of query aligns to 5:449/670 of 7ybuA
Sites not aligning to the query:
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)
41% identity, 37% coverage: 2:448/1207 of query aligns to 63:507/728 of P05165
- A75 (= A14) to P: in PA-1; dbSNP:rs794727479
- R77 (= R16) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A77) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ V103) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (vs. gap) to E: in PA-1
- M229 (= M167) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q235) to R: in PA-1
- D368 (= D307) to G: in PA-1
- M373 (= M312) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G318) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A339) to R: in PA-1
- R399 (= R340) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P364) to L: in PA-1; dbSNP:rs1443858896
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 532 natural variant: Missing (in PA-1)
- 551 V → F: in dbSNP:rs61749895
- 559 W → L: in PA-1; dbSNP:rs118169528
- 631 G → R: in PA-1; loss of function; dbSNP:rs796052018
- 668 G → R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- 694 modified: N6-biotinyllysine; by HLCS
- 712 natural variant: Missing (in PA-1; loss of biotinylation)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/449 of P24182
- R19 (= R19) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ T23) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K116) binding
- K159 (= K157) binding
- GG 165:166 (= GG 163:164) binding
- EKYL 201:204 (≠ EKYI 199:202) binding
- H209 (= H207) binding
- H236 (≠ N234) binding
- K238 (= K236) binding
- E276 (= E274) binding ; binding
- E288 (= E288) binding ; binding
- R292 (= R292) active site; binding
- V295 (= V295) binding
- E296 (= E296) mutation to A: Severe reduction in catalytic activity.
- R338 (= R340) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ Q368) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (= R371) mutation to E: Loss of homodimerization. No effect on ATP binding.
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 3:444/447 of 3jzfB
- active site: K118 (= K116), K161 (= K157), D198 (≠ A194), H211 (= H207), R237 (= R233), T276 (= T272), E278 (= E274), E290 (= E288), N292 (= N290), R294 (= R292), E298 (= E296), R340 (= R340)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K116), K161 (= K157), A162 (≠ S158), G166 (= G162), G168 (= G164), R169 (≠ I165), G170 (= G166), M171 (= M167), Y201 (≠ F197), E203 (= E199), K204 (= K200), Y205 (= Y201), H211 (= H207), H238 (≠ N234), L280 (≠ V276), I289 (≠ L287), E290 (= E288)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/445 of 3jziA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K116), K159 (= K157), A160 (≠ S158), G164 (= G162), G165 (= G163), M169 (= M167), Y199 (≠ F197), E201 (= E199), K202 (= K200), Y203 (= Y201), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), I287 (≠ L287), E288 (= E288)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/445 of 2w6oA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K157), K202 (= K200), Y203 (= Y201), L204 (≠ I202), L278 (≠ V276), I437 (≠ T442)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/445 of 2w6nA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ M155), K159 (= K157), M169 (= M167), E201 (= E199), K202 (= K200), Y203 (= Y201), L278 (≠ V276)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/445 of 2v59A
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K157), Y203 (= Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), I437 (≠ T442)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/444 of 3rupA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding adenosine-5'-diphosphate: Y82 (= Y82), G83 (= G83), K116 (= K116), K159 (= K157), G164 (= G162), G164 (= G162), G165 (= G163), G166 (= G164), R167 (≠ I165), M169 (= M167), F193 (= F191), E201 (= E199), K202 (= K200), Y203 (= Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), K238 (= K236), L278 (≠ V276), E288 (= E288), R292 (= R292), V295 (= V295), E296 (= E296), R338 (= R340), D382 (= D387), I437 (≠ T442)
- binding calcium ion: E87 (= E87), E276 (= E274), E288 (= E288), E288 (= E288), N290 (= N290)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/444 of 3g8cA
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding adenosine-5'-diphosphate: I157 (≠ M155), K159 (= K157), G164 (= G162), M169 (= M167), E201 (= E199), K202 (= K200), Y203 (= Y201), L204 (≠ I202), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), E288 (= E288), I437 (≠ T442)
- binding bicarbonate ion: K238 (= K236), R292 (= R292), Q294 (= Q294), V295 (= V295), E296 (= E296)
- binding biotin: Y82 (= Y82), F84 (= F84), R292 (= R292), V295 (= V295), R338 (= R340), D382 (= D387)
- binding magnesium ion: E276 (= E274), E288 (= E288)
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)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/446 of 6oi9A
- active site: E276 (= E274), E288 (= E288), N290 (= N290), E296 (= E296), R338 (= R340)
- binding 7-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-6-(2,6-dichlorophenyl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K157), M169 (= M167), E201 (= E199), Y203 (= Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), E276 (= E274), L278 (≠ V276), E288 (= E288), I437 (≠ T442)
2w71A Crystal structure of biotin carboxylase from e. Coli in complex with the imidazole-pyrimidine inhibitor (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/446 of 2w71A
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine: K159 (= K157), Y203 (= Y201), L204 (≠ I202), H209 (= H207), Q233 (= Q231), H236 (≠ N234), L278 (≠ V276), I437 (≠ T442)
2w70A Crystal structure of biotin carboxylase from e. Coli in complex with the amino-thiazole-pyrimidine fragment (see paper)
43% identity, 37% coverage: 1:447/1207 of query aligns to 1:442/446 of 2w70A
- active site: K116 (= K116), K159 (= K157), D196 (≠ A194), H209 (= H207), R235 (= R233), T274 (= T272), E276 (= E274), E288 (= E288), N290 (= N290), R292 (= R292), E296 (= E296), R338 (= R340)
- binding 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine: I157 (≠ M155), K159 (= K157), G166 (= G164), M169 (= M167), E201 (= E199), Y203 (= Y201), L204 (≠ I202), L278 (≠ V276)
Query Sequence
>HSERO_RS22345 FitnessBrowser__HerbieS:HSERO_RS22345
MFDHLLIANRGAIACRILRTLRTLDVTGVCVYSEADLGSLHVLQADRAISLGEGPAAQTY
LAVDKILAAARDSGAQAIHPGYGFLSENAAFAEACEAAGIAFVGPTPAQLRIFGLKHTAR
ALAREQGVPMLEGTDLLESIDDALAAASRVGYPVMLKSTAGGGGIGMRVCRSDAELADAF
DSVRRLGQNNFSDAGVFIEKYIERARHLEVQVFGDGRGEVIALGVRDCSVQRRNQKVLEE
TPAPNLPDGMAEALCAAAIKLAKAVNYRSAGTVEFVYDSLAGQFYFLEVNTRLQVEHGVT
EQVWGVDLVRWMIELAAGDLPPLAQLAAGLQPRGHAIQARLYAEDPGRQFQPCPGLLTAV
DFPPVDGQALRIDTWVEAGCEIAPYFDPMIAKLISWQPTREAARLALDAALRATLLYGVE
TNQHYLRQILADVPFASGQPWTRCLEQLVYRADTVEVLAPGTQTTVQDHPGRIGYWAVGV
PPSGPMDERALRLGNRLLGNAEEAAGLEVTMSGPILRFNTAAMVVVTGAVIPVLLDGVAQ
PMATVLHIAAGSTLKLGAISGAGARSYLAVRGGVQVPTYLGSRSTFTLGQFGGHAGRALA
SGDILHLAPLAADAMTQAGQTLPAALYPALEAVRQVRVIYGPHGAPEYFTPAYMETFFAT
DWEVHFNSSRTGVRLIGPKPEWVRDSGGEAGLHPSNIHDNPYAVGAVDFTGDMPVILGPD
GPSLGGFVCPVTVIEADLWQIGQLKAGDKVRFVPVEVNTARRIALAAQAGVASLQPQPVD
WSPAPLASPIVLDLGQDERRLVARLSGDANLLLEVGSPQLDLVLRFRVHALITALEEQAL
PGVIDLTPGIRSLQVHYQPEALPLPTLLQTIAGLWDAVCASENLTVSSRIVHLPLSWDDP
ACQLAIEKYMTTVRKDAPWCPSNLEFIRRINDLKDIGAVRETVFDASYLVMGLGDVYLGA
PVATPLDPRHRLVTTKYNPARTWTAENSVGIGGAYLCIYGMEGPGGYQFVGRTLQMWNRY
REVAAFRGKPWLLRFFDQIRFYPVTAEELQTIRRDFPLGRFEVGIEETQLNLADYQDFLQ
READGIAAFRQHQQAAFDAERQRWIASGQANYESEESSAIAQEAAPLQDGQMAVDAPIAG
NLWQVKVSPGQRVAQGELLMILESMKMEIHIAAPAAGVVAEVRVQPGSPVRAGQCVLVME
DTEEEVA
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