SitesBLAST
Comparing 6936061 FitnessBrowser__SB2B:6936061 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)
Q51742 Ornithine carbamoyltransferase, anabolic; OTCase; EC 2.1.3.3 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 3 papers)
47% identity, 100% coverage: 2:301/301 of query aligns to 8:311/315 of Q51742
- W22 (≠ L16) mutation to A: Decreased heat stability.
- E26 (≠ T20) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (vs. gap) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ K26) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (= Y219) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ L232) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E268) mutation to G: Becomes active at low temperatures; when associated with C-228 or D-241.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
44% identity, 99% coverage: 2:300/301 of query aligns to 12:309/316 of Q81M99
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
43% identity, 99% coverage: 2:300/301 of query aligns to 8:305/307 of 4nf2A
- active site: R55 (= R51), T56 (= T52), R83 (≠ K79), R104 (= R100), H131 (= H127), Q134 (= Q130), D226 (= D221), C265 (= C260), R293 (= R288)
- binding phosphoric acid mono(formamide)ester: S53 (= S49), T54 (≠ L50), R55 (= R51), T56 (= T52), R104 (= R100), H131 (= H127), Q134 (= Q130), C265 (= C260), L266 (= L261), R293 (= R288)
- binding norvaline: L126 (= L122), N162 (= N158), D226 (= D221), S230 (= S225), M231 (= M226)
8qeuA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with ornithine (see paper)
42% identity, 100% coverage: 1:301/301 of query aligns to 1:303/304 of 8qeuA
P9WIT9 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
43% identity, 100% coverage: 1:300/301 of query aligns to 2:304/307 of P9WIT9
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
43% identity, 100% coverage: 1:300/301 of query aligns to 3:305/308 of 7nouA
- active site: R102 (= R100), H129 (= H127), Q132 (= Q130), D225 (= D221), C265 (= C260), R293 (= R288)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (≠ L44), T52 (≠ L50), R53 (= R51), R53 (= R51), F56 (≠ V54), F56 (≠ V54), L79 (= L77), D82 (≠ R80), E83 (= E81), V91 (≠ N89), Y95 (≠ W93), L266 (= L261), R293 (= R288)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
43% identity, 100% coverage: 1:300/301 of query aligns to 3:305/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
43% identity, 100% coverage: 1:300/301 of query aligns to 3:305/308 of 7norA
7nnyA Crystal structure of mycobacterium tuberculosis argf in complex with naphthalen-1-ol.
43% identity, 100% coverage: 1:300/301 of query aligns to 3:305/308 of 7nnyA
- active site: R102 (= R100), H129 (= H127), Q132 (= Q130), D225 (= D221), C265 (= C260), R293 (= R288)
- binding 1-naphthol: T52 (≠ L50), R53 (= R51), F56 (≠ V54), E83 (= E81), V91 (≠ N89), Y95 (≠ W93)
7nnwA Crystal structure of mycobacterium tuberculosis argf in complex with methyl 4-hydroxy-3-iodobenzoate.
43% identity, 100% coverage: 1:300/301 of query aligns to 3:305/308 of 7nnwA
- active site: R102 (= R100), H129 (= H127), Q132 (= Q130), D225 (= D221), C265 (= C260), R293 (= R288)
- binding methyl 3-iodanyl-4-oxidanyl-benzoate: I46 (≠ L44), T52 (≠ L50), R53 (= R51), F56 (≠ V54), L79 (= L77), L92 (= L90), Y95 (≠ W93)
7nnvA Crystal structure of mycobacterium tuberculosis argf in complex with carbamoyl phosphate.
43% identity, 100% coverage: 1:300/301 of query aligns to 3:305/308 of 7nnvA
- active site: R102 (= R100), H129 (= H127), Q132 (= Q130), D225 (= D221), C265 (= C260), R293 (= R288)
- binding phosphoric acid mono(formamide)ester: S51 (= S49), T52 (≠ L50), R53 (= R51), T54 (= T52), R102 (= R100), H129 (= H127), C265 (= C260), L266 (= L261), R293 (= R288)
2i6uA Crystal structure of ornithine carbamoyltransferase complexed with carbamoyl phosphate and l-norvaline from mycobacterium tuberculosis (rv1656) at 2.2 a (see paper)
43% identity, 100% coverage: 1:300/301 of query aligns to 2:304/307 of 2i6uA
- active site: R52 (= R51), T53 (= T52), R80 (≠ K79), R101 (= R100), H128 (= H127), Q131 (= Q130), D224 (= D221), C264 (= C260), R292 (= R288)
- binding phosphoric acid mono(formamide)ester: S50 (= S49), T51 (≠ L50), R52 (= R51), T53 (= T52), R101 (= R100), C264 (= C260), L265 (= L261), R292 (= R288)
- binding norvaline: L123 (= L122), N160 (= N158), D224 (= D221), S228 (= S225), M229 (= M226)
8qevA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with carbamoyl phosphate (see paper)
42% identity, 100% coverage: 1:301/301 of query aligns to 1:296/297 of 8qevA
7np0A Crystal structure of mycobacterium tuberculosis argf in complex with (4-nitrophenyl)boronic acid.
43% identity, 100% coverage: 1:300/301 of query aligns to 3:302/305 of 7np0A
7novA Crystal structure of mycobacterium tuberculosis argf in complex with (4-methyl-3-nitrophenyl)boronic acid.
42% identity, 100% coverage: 1:300/301 of query aligns to 3:299/302 of 7novA
- active site: R96 (= R100), H123 (= H127), Q126 (= Q130), D219 (= D221), C259 (= C260), R287 (= R288)
- binding (4-methyl-3-nitro-phenyl)-oxidanyl-oxidanylidene-boron: R53 (= R51), F56 (≠ V54), E77 (= E81), V85 (≠ N89), Y89 (≠ W93), L260 (= L261), A284 (= A285), R287 (= R288)
7nnzB Crystal structure of mycobacterium tuberculosis argf in complex with 5-methyl-4-phenylthiazol-2-amine.
42% identity, 100% coverage: 1:300/301 of query aligns to 2:294/297 of 7nnzB
P00480 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Homo sapiens (Human) (see 31 papers)
40% identity, 99% coverage: 2:300/301 of query aligns to 40:342/354 of P00480
- R40 (≠ K2) to H: in OTCD; late onset; dbSNP:rs72554308
- L43 (≠ I5) to F: in dbSNP:rs72554309
- K46 (= K8) to R: in dbSNP:rs1800321
- Y55 (≠ D17) to D: in OTCD; late onset; dbSNP:rs72554319
- L63 (≠ I25) to P: in OTCD; late onset; dbSNP:rs72554324
- K88 (= K47) modified: N6-acetyllysine; alternate; to N: in OTCD; late onset; dbSNP:rs72554339
- STRT 90:93 (≠ SLRT 49:52) binding
- G100 (= G59) to D: in OTCD; late onset; dbSNP:rs72554349
- F101 (≠ I60) to L: in dbSNP:rs1133135
- L111 (= L70) to P: in dbSNP:rs1800324
- T125 (≠ K84) to M: in OTCD; neonatal; dbSNP:rs72554356
- D126 (= D85) to G: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; 0.9% of wild-type activity; dbSNP:rs72554358
- R129 (≠ S88) to H: in OTCD; early onset; decreased ornithine carbamoyltransferase activity; 2.1% of wild-type activity; dbSNP:rs66656800
- A140 (= A99) to P: in OTCD; late onset; dbSNP:rs72556260
- R141 (= R100) binding ; to Q: in OTCD; most common variant; loss of ornithine carbamoyltransferase activity; activity is 100-fold lower; dbSNP:rs68026851
- H168 (= H127) binding
- Q171 (= Q130) binding
- I172 (≠ G131) to M: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; dbSNP:rs72556280
- Y176 (≠ F135) to C: in OTCD; late onset; dbSNP:rs72556283
- TL 178:179 (≠ SL 137:138) natural variant: Missing (in OTCD; neonatal)
- Y183 (≠ F142) to D: in OTCD; late onset; dbSNP:rs72556292
- G188 (≠ K147) to R: in OTCD; neonatal; dbSNP:rs72556294
- G195 (= G154) to R: in OTCD; loss of ornithine carbamoyltransferase activity; dbSNP:rs67294955
- D196 (= D155) to V: in OTCD; neonatal; decreased ornithine carbamoyltransferase activity; 3.7% activity; dbSNP:rs72556300
- L201 (≠ S160) to P: in OTCD; neonatal; dbSNP:rs72558407
- S207 (≠ G166) to R: in OTCD; neonatal; dbSNP:rs72558415
- A209 (= A168) to V: in OTCD; neonatal; dbSNP:rs72558417
- M213 (≠ A172) to K: in OTCD; late onset
- H214 (≠ T173) to Y: in OTCD; neonatal; dbSNP:rs72558420
- P220 (= P179) to A: in OTCD; late onset; dbSNP:rs72558425
- P225 (= P184) to T: in OTCD; late onset; dbSNP:rs72558428
- L244 (= L203) to Q: in OTCD; late onset; dbSNP:rs72558436
- T262 (= T220) to K: in OTCD; mild; dbSNP:rs67333670
- T264 (= T222) to A: in OTCD; late onset; decreased ornithine carbamoyltransferase activity; 8.9% activity; dbSNP:rs72558444; to I: in OTCD; late onset; dbSNP:rs67156896
- W265 (= W223) to L: in OTCD; mild; dbSNP:rs72558446
- G269 (= G227) to E: in OTCD; neonatal; dbSNP:rs72558450
- Q270 (≠ D228) to R: in dbSNP:rs1800328
- E272 (≠ T230) natural variant: Missing (in OTCD; late onset; dbSNP:rs72558452)
- R277 (≠ I235) to Q: in OTCD; late onset; dbSNP:rs66724222; to W: in OTCD; late onset; dbSNP:rs72558454
- H302 (= H259) to L: in OTCD; female; late onset; dbSNP:rs67993095; to Y: in OTCD; neonatal; dbSNP:rs72558463
- C303 (= C260) to R: in OTCD; neonatal; dbSNP:rs67468335
- CL 303:304 (= CL 260:261) binding
- E309 (≠ L267) natural variant: Missing (in OTCD; late onset)
- R330 (= R288) binding
- T333 (≠ A291) natural variant: T -> A
- S340 (≠ T298) to P: in OTCD; late onset; dbSNP:rs72558489
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 15 R→G: Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-23 and G-26.
- 23 R→G: Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-15 and G-26.
- 26 R→G: Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-15 and G-23.
- 39 G → C: in OTCD; late onset; dbSNP:rs72554306
- 343 T → K: in OTCD; late onset; dbSNP:rs72558491
1othA Crystal structure of human ornithine transcarbamoylase complexed with n-phosphonacetyl-l-ornithine (see paper)
40% identity, 99% coverage: 2:300/301 of query aligns to 7:309/321 of 1othA
- active site: R59 (= R51), T60 (= T52), V87 (≠ K79), R108 (= R100), H135 (= H127), Q138 (= Q130), D230 (= D221), C270 (= C260), R297 (= R288)
- binding n-(phosphonoacetyl)-l-ornithine: S57 (= S49), T58 (≠ L50), R59 (= R51), T60 (= T52), R108 (= R100), L130 (= L122), H135 (= H127), N166 (= N158), D230 (= D221), S234 (= S225), M235 (= M226), C270 (= C260), L271 (= L261), R297 (= R288)
1c9yA Human ornithine transcarbamylase: crystallographic insights into substrate recognition and catalytic mechanism (see paper)
40% identity, 99% coverage: 2:300/301 of query aligns to 7:309/321 of 1c9yA
- active site: R59 (= R51), T60 (= T52), V87 (≠ K79), R108 (= R100), H135 (= H127), Q138 (= Q130), D230 (= D221), C270 (= C260), R297 (= R288)
- binding phosphoric acid mono(formamide)ester: S57 (= S49), T58 (≠ L50), R59 (= R51), T60 (= T52), R108 (= R100), C270 (= C260), L271 (= L261), R297 (= R288)
- binding norvaline: L130 (= L122), N166 (= N158), D230 (= D221), S234 (= S225), M235 (= M226)
2otcA Ornithine transcarbamoylase complexed with n-(phosphonacetyl)-l- ornithine (see paper)
37% identity, 99% coverage: 2:300/301 of query aligns to 6:331/333 of 2otcA
- active site: R57 (= R51), T58 (= T52), H85 (≠ K79), R106 (= R100), H133 (= H127), Q136 (= Q130), D231 (= D221), C273 (= C260), R319 (= R288)
- binding n-(phosphonoacetyl)-l-ornithine: S55 (= S49), T56 (≠ L50), R57 (= R51), T58 (= T52), R106 (= R100), H133 (= H127), N167 (= N158), D231 (= D221), S235 (= S225), M236 (= M226), L274 (= L261), R319 (= R288)
Query Sequence
>6936061 FitnessBrowser__SB2B:6936061
MKHLISIKELTQKQMLDLLTLAKEIKADPAKYSRALAGKSVVMLFEKPSLRTRVSFDIGI
NKLGGHCLYLDQQNGALGKRESVKDFASNLSCWADAIVARTFAHETVEGLAKYGRVPVIN
ALSDLYHPCQGLADFLSLAEKFDDLSKVRLAYVGDGNNVSHSLMYGAALLGATMTVICPP
GHFPDGFEVQQAQQIAAAHGGKLVLTSDINAIEGHDAVYTDTWISMGDNTALTDIKAKFA
PYQVNKALMNKAGASYFMHCLPAHRGLEVTDEVMDGEGSLILDQAENRMHAQNAVLVTLL
G
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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