SitesBLAST
Comparing GFF3565 FitnessBrowser__Marino:GFF3565 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)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
39% identity, 94% coverage: 9:314/327 of query aligns to 1:293/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 92% coverage: 9:310/327 of query aligns to 1:289/291 of 3r7fA
- active site: R49 (= R62), T50 (= T63), K77 (= K90), R99 (= R112), H127 (= H142), Q130 (= Q145), L210 (= L229), P249 (= P270), G277 (= G298)
- binding phosphoric acid mono(formamide)ester: S47 (= S60), T48 (= T61), R49 (= R62), T50 (= T63), R99 (= R112), H127 (= H142), Q130 (= Q145), P249 (= P270), A250 (≠ G271)
- binding phosphate ion: S11 (≠ D19), T12 (≠ R20), Q23 (≠ D31), K26 (≠ R39), E140 (≠ Q155), R171 (≠ E186), K241 (≠ H262), H243 (≠ E264), K272 (≠ N293), K272 (≠ N293), K275 (≠ T296)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 92% coverage: 9:310/327 of query aligns to 1:289/291 of 3r7dA
- active site: R49 (= R62), T50 (= T63), K77 (= K90), R99 (= R112), H127 (= H142), Q130 (= Q145), L210 (= L229), P249 (= P270), G277 (= G298)
- binding phosphate ion: S11 (≠ D19), T12 (≠ R20), T73 (≠ S86), S74 (≠ A87), K77 (= K90), R171 (≠ E186)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
39% identity, 92% coverage: 9:310/327 of query aligns to 1:289/290 of 3r7lA
- active site: R49 (= R62), T50 (= T63), K77 (= K90), R99 (= R112), H127 (= H142), Q130 (= Q145), L210 (= L229), P249 (= P270), G277 (= G298)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S60), T48 (= T61), R49 (= R62), T50 (= T63), S74 (≠ A87), K77 (= K90), R99 (= R112), H127 (= H142), R160 (= R175), R211 (= R230), Q213 (= Q232), A250 (≠ G271)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
38% identity, 91% coverage: 9:306/327 of query aligns to 1:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S60), T49 (= T61), R50 (= R62), T51 (= T63), S75 (≠ A87), K78 (= K90), R100 (= R112), H127 (= H142), R160 (= R175), R210 (= R230), Q212 (= Q232), A253 (≠ G271)
4bjhB Crystal structure of the aquifex reactor complex formed by dihydroorotase (h180a, h232a) with dihydroorotate and aspartate transcarbamoylase with n-(phosphonacetyl)-l-aspartate (pala) (see paper)
39% identity, 89% coverage: 18:308/327 of query aligns to 10:288/291 of 4bjhB
- active site: R47 (= R62), T48 (= T63), K75 (= K90), R97 (= R112), H126 (= H142), Q129 (= Q145)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S60), T46 (= T61), R47 (= R62), T48 (= T63), R97 (= R112), H126 (= H142), R159 (= R175), V160 (= V176), R213 (= R230), Q215 (= Q232), G251 (= G271)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
39% identity, 89% coverage: 18:308/327 of query aligns to 10:288/291 of 3d6nB
- active site: R47 (= R62), T48 (= T63), K75 (= K90), R97 (= R112), H126 (= H142), Q129 (= Q145)
- binding citrate anion: T48 (= T63), R97 (= R112), H126 (= H142), R159 (= R175), V160 (= V176), R213 (= R230), G251 (= G271)
1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
34% identity, 94% coverage: 6:311/327 of query aligns to 1:305/307 of 1ml4A
- active site: R56 (= R62), T57 (= T63), K85 (= K90), R106 (= R112), H134 (= H142), Q137 (= Q145), T227 (≠ L229), P266 (= P270), G292 (= G298)
- binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S60), T55 (= T61), R56 (= R62), T57 (= T63), R106 (= R112), H134 (= H142), R167 (= R175), T168 (≠ V176), R228 (= R230), L267 (≠ G271)
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
34% identity, 91% coverage: 9:307/327 of query aligns to 1:297/304 of 4eknB
5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 6:305/307 of 5g1nE
- active site: R57 (= R62), T58 (= T63), K85 (= K90), R106 (= R112), H134 (= H142), Q137 (= Q145), T227 (≠ L229), P266 (= P270), G292 (= G298)
- binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S60), T56 (= T61), R57 (= R62), T58 (= T63), S82 (≠ A87), K85 (= K90), R106 (= R112), H134 (= H142), R167 (= R175), R228 (= R230), Q230 (= Q232), M267 (≠ G271)
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 2ipoA
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S60), T53 (= T61), R54 (= R62), T55 (= T63), R105 (= R112), H134 (= H142), R167 (= R175), T168 (≠ V176), R229 (= R230), L267 (≠ G271)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 2h3eA
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S60), T53 (= T61), R54 (= R62), T55 (= T63), R105 (= R112), H134 (= H142), R167 (= R175), R229 (= R230), L267 (≠ G271)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 2fzkA
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T63), H134 (= H142), Q137 (= Q145), T168 (≠ V176), R229 (= R230), P266 (= P270), L267 (≠ G271), R296 (= R302)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 2fzgA
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S60), R54 (= R62), T55 (= T63), R105 (= R112), H134 (= H142), R167 (= R175), T168 (≠ V176), R229 (= R230), P266 (= P270), L267 (≠ G271)
2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 2fzcA
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S60), R54 (= R62), T55 (= T63), R105 (= R112), R167 (= R175), T168 (≠ V176), P266 (= P270), L267 (≠ G271)
2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 2airA
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding 3-[hydroxy(nitroso)amino]-l-alanine: S52 (= S60), T53 (= T61), R54 (= R62), R105 (= R112)
- binding phosphoric acid mono(formamide)ester: R54 (= R62), T55 (= T63), R105 (= R112), H134 (= H142)
1za2A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 1za2A
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding phosphoric acid mono(formamide)ester: T53 (= T61), R54 (= R62), T55 (= T63), R105 (= R112), R167 (= R175), T168 (≠ V176), L267 (≠ G271)
1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 1r0cA
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding n-carbamoyl-l-aspartate: S52 (= S60), R54 (= R62), R105 (= R112)
- binding phosphate ion: R105 (= R112), H134 (= H142), Q137 (= Q145)
1r0bA Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate (see paper)
32% identity, 92% coverage: 10:311/327 of query aligns to 7:305/310 of 1r0bA
- active site: R54 (= R62), T55 (= T63), K84 (= K90), R105 (= R112), H134 (= H142), Q137 (= Q145), T228 (≠ L229), P266 (= P270), G292 (= G298)
- binding citrate anion: H134 (= H142), R167 (= R175), R229 (= R230), Q231 (= Q232), P266 (= P270), P268 (= P272)
- binding phosphate ion: S80 (= S86), K84 (= K90)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 92% coverage: 10:311/327 of query aligns to 8:306/311 of P0A786
- R55 (= R62) binding
- T56 (= T63) binding
- R106 (= R112) binding
- H135 (= H142) binding
- Q138 (= Q145) binding
- L268 (≠ G271) binding
- P269 (= P272) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>GFF3565 FitnessBrowser__Marino:GFF3565
MQLTRDGQLRHFLTLDGLDRALLTDILDTADSFIEVGERTIKKVPLLRGRTVVNLFFESS
TRTRSTFELAAKRLSADVLNLDISTSATSKGESLSDTLLNLEAMASDMFVVRHSQSGAPH
FIAESVTPGVAIINAGDGRHAHPTQAMLDMLTIRQHKGRFEGLKVAIVGDVLHSRVARSQ
IRALNELGAEEVRVIAPGTLLPKDVESLGCTVEYDMTRGMKDLDVVIMLRLQKERMEGAL
LPSEREFYRLYGLNQQKLALAHPECIVMHPGPINRGVEIESAVADGPQSVILNQVTNGIA
IRMAVMSMAMGGQVSERQQKLSERGQA
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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