SitesBLAST
Comparing WP_015739792.1 NCBI__GCF_000024605.1:WP_015739792.1 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)
58% identity, 96% coverage: 12:312/312 of query aligns to 8:310/315 of Q51742
- W22 (≠ M26) mutation to A: Decreased heat stability.
- E26 (≠ S30) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ E34) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ A38) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (≠ V230) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (= A243) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E280) 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
53% identity, 98% coverage: 8:312/312 of query aligns to 8:309/316 of Q81M99
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
53% identity, 98% coverage: 8:312/312 of query aligns to 4:305/307 of 4nf2A
- active site: R55 (= R63), T56 (= T64), R83 (= R91), R104 (= R112), H131 (= H139), Q134 (= Q142), D226 (= D232), C265 (= C272), R293 (= R300)
- binding phosphoric acid mono(formamide)ester: S53 (= S61), T54 (= T62), R55 (= R63), T56 (= T64), R104 (= R112), H131 (= H139), Q134 (= Q142), C265 (= C272), L266 (= L273), R293 (= R300)
- binding norvaline: L126 (= L134), N162 (= N170), D226 (= D232), S230 (= S236), M231 (= M237)
8qeuA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with ornithine (see paper)
46% identity, 96% coverage: 12:312/312 of query aligns to 2:302/304 of 8qeuA
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
50% identity, 96% coverage: 12:312/312 of query aligns to 4:305/308 of 7nouA
- active site: R102 (= R112), H129 (= H139), Q132 (= Q142), D225 (= D232), C265 (= C272), R293 (= R300)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (= I56), T52 (= T62), R53 (= R63), R53 (= R63), F56 (≠ V66), F56 (≠ V66), L79 (= L89), D82 (≠ G92), E83 (= E93), V91 (= V101), Y95 (= Y105), L266 (= L273), R293 (= R300)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
50% identity, 96% coverage: 12:312/312 of query aligns to 4:305/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
50% identity, 96% coverage: 12:312/312 of query aligns to 4:305/308 of 7norA
7nnyA Crystal structure of mycobacterium tuberculosis argf in complex with naphthalen-1-ol.
50% identity, 96% coverage: 12:312/312 of query aligns to 4:305/308 of 7nnyA
- active site: R102 (= R112), H129 (= H139), Q132 (= Q142), D225 (= D232), C265 (= C272), R293 (= R300)
- binding 1-naphthol: T52 (= T62), R53 (= R63), F56 (≠ V66), E83 (= E93), V91 (= V101), Y95 (= Y105)
7nnwA Crystal structure of mycobacterium tuberculosis argf in complex with methyl 4-hydroxy-3-iodobenzoate.
50% identity, 96% coverage: 12:312/312 of query aligns to 4:305/308 of 7nnwA
- active site: R102 (= R112), H129 (= H139), Q132 (= Q142), D225 (= D232), C265 (= C272), R293 (= R300)
- binding methyl 3-iodanyl-4-oxidanyl-benzoate: I46 (= I56), T52 (= T62), R53 (= R63), F56 (≠ V66), L79 (= L89), L92 (= L102), Y95 (= Y105)
7nnvA Crystal structure of mycobacterium tuberculosis argf in complex with carbamoyl phosphate.
50% identity, 96% coverage: 12:312/312 of query aligns to 4:305/308 of 7nnvA
- active site: R102 (= R112), H129 (= H139), Q132 (= Q142), D225 (= D232), C265 (= C272), R293 (= R300)
- binding phosphoric acid mono(formamide)ester: S51 (= S61), T52 (= T62), R53 (= R63), T54 (= T64), R102 (= R112), H129 (= H139), C265 (= C272), L266 (= L273), R293 (= R300)
P9WIT9 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
50% identity, 96% coverage: 12:312/312 of query aligns to 3:304/307 of P9WIT9
2i6uA Crystal structure of ornithine carbamoyltransferase complexed with carbamoyl phosphate and l-norvaline from mycobacterium tuberculosis (rv1656) at 2.2 a (see paper)
50% identity, 96% coverage: 12:312/312 of query aligns to 3:304/307 of 2i6uA
- active site: R52 (= R63), T53 (= T64), R80 (= R91), R101 (= R112), H128 (= H139), Q131 (= Q142), D224 (= D232), C264 (= C272), R292 (= R300)
- binding phosphoric acid mono(formamide)ester: S50 (= S61), T51 (= T62), R52 (= R63), T53 (= T64), R101 (= R112), C264 (= C272), L265 (= L273), R292 (= R300)
- binding norvaline: L123 (= L134), N160 (= N170), D224 (= D232), S228 (= S236), M229 (= M237)
P00481 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Rattus norvegicus (Rat) (see 2 papers)
44% identity, 98% coverage: 8:312/312 of query aligns to 36:342/354 of P00481
- R92 (= R63) mutation to L: Strong decrease in ornithine carbamoyltransferase activity.
- C303 (= C272) mutation to S: Increases KM for ornithine 5-fold and decreases kcat 20-fold.
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
7np0A Crystal structure of mycobacterium tuberculosis argf in complex with (4-nitrophenyl)boronic acid.
50% identity, 96% coverage: 12:312/312 of query aligns to 4:302/305 of 7np0A
P00480 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Homo sapiens (Human) (see 31 papers)
44% identity, 98% coverage: 8:312/312 of query aligns to 36:342/354 of P00480
- G39 (≠ H11) to C: in OTCD; late onset; dbSNP:rs72554306
- R40 (= R12) to H: in OTCD; late onset; dbSNP:rs72554308
- L43 (= L15) to F: in dbSNP:rs72554309
- K46 (≠ A18) to R: in dbSNP:rs1800321
- Y55 (≠ G27) to D: in OTCD; late onset; dbSNP:rs72554319
- L63 (= L35) to P: in OTCD; late onset; dbSNP:rs72554324
- K88 (= K59) modified: N6-acetyllysine; alternate; to N: in OTCD; late onset; dbSNP:rs72554339
- STRT 90:93 (= STRT 61:64) binding
- G100 (≠ A71) to D: in OTCD; late onset; dbSNP:rs72554349
- F101 (≠ M72) to L: in dbSNP:rs1133135
- L111 (= L82) to P: in dbSNP:rs1800324
- T125 (≠ A96) to M: in OTCD; neonatal; dbSNP:rs72554356
- D126 (= D97) to G: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; 0.9% of wild-type activity; dbSNP:rs72554358
- R129 (= R100) to H: in OTCD; early onset; decreased ornithine carbamoyltransferase activity; 2.1% of wild-type activity; dbSNP:rs66656800
- A140 (≠ I111) to P: in OTCD; late onset; dbSNP:rs72556260
- R141 (= R112) binding ; to Q: in OTCD; most common variant; loss of ornithine carbamoyltransferase activity; activity is 100-fold lower; dbSNP:rs68026851
- H168 (= H139) binding
- Q171 (= Q142) binding
- I172 (= I143) to M: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; dbSNP:rs72556280
- Y176 (≠ F147) to C: in OTCD; late onset; dbSNP:rs72556283
- TL 178:179 (≠ TI 149:150) natural variant: Missing (in OTCD; neonatal)
- Y183 (≠ K154) to D: in OTCD; late onset; dbSNP:rs72556292
- G188 (= G159) to R: in OTCD; neonatal; dbSNP:rs72556294
- G195 (= G166) to R: in OTCD; loss of ornithine carbamoyltransferase activity; dbSNP:rs67294955
- D196 (= D167) to V: in OTCD; neonatal; decreased ornithine carbamoyltransferase activity; 3.7% activity; dbSNP:rs72556300
- L201 (≠ C172) to P: in OTCD; neonatal; dbSNP:rs72558407
- S207 (≠ G178) to R: in OTCD; neonatal; dbSNP:rs72558415
- A209 (≠ P180) to V: in OTCD; neonatal; dbSNP:rs72558417
- M213 (= M184) to K: in OTCD; late onset
- H214 (≠ S185) to Y: in OTCD; neonatal; dbSNP:rs72558420
- P220 (= P191) to A: in OTCD; late onset; dbSNP:rs72558425
- P225 (= P196) to T: in OTCD; late onset; dbSNP:rs72558428
- L244 (≠ V213) to Q: in OTCD; late onset; dbSNP:rs72558436
- T262 (= T231) to K: in OTCD; mild; dbSNP:rs67333670
- T264 (≠ V233) to A: in OTCD; late onset; decreased ornithine carbamoyltransferase activity; 8.9% activity; dbSNP:rs72558444; to I: in OTCD; late onset; dbSNP:rs67156896
- W265 (= W234) to L: in OTCD; mild; dbSNP:rs72558446
- G269 (= G238) to E: in OTCD; neonatal; dbSNP:rs72558450
- Q270 (= Q239) to R: in dbSNP:rs1800328
- E272 (= E241) natural variant: Missing (in OTCD; late onset; dbSNP:rs72558452)
- R277 (≠ K246) to Q: in OTCD; late onset; dbSNP:rs66724222; to W: in OTCD; late onset; dbSNP:rs72558454
- H302 (= H271) to L: in OTCD; female; late onset; dbSNP:rs67993095; to Y: in OTCD; neonatal; dbSNP:rs72558463
- C303 (= C272) to R: in OTCD; neonatal; dbSNP:rs67468335
- CL 303:304 (= CL 272:273) binding
- E309 (= E279) natural variant: Missing (in OTCD; late onset)
- R330 (= R300) binding
- T333 (≠ V303) natural variant: T -> A
- S340 (≠ L310) 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.
- 343 T → K: in OTCD; late onset; dbSNP:rs72558491
1othA Crystal structure of human ornithine transcarbamoylase complexed with n-phosphonacetyl-l-ornithine (see paper)
44% identity, 98% coverage: 8:312/312 of query aligns to 3:309/321 of 1othA
- active site: R59 (= R63), T60 (= T64), V87 (≠ R91), R108 (= R112), H135 (= H139), Q138 (= Q142), D230 (= D232), C270 (= C272), R297 (= R300)
- binding n-(phosphonoacetyl)-l-ornithine: S57 (= S61), T58 (= T62), R59 (= R63), T60 (= T64), R108 (= R112), L130 (= L134), H135 (= H139), N166 (= N170), D230 (= D232), S234 (= S236), M235 (= M237), C270 (= C272), L271 (= L273), R297 (= R300)
1c9yA Human ornithine transcarbamylase: crystallographic insights into substrate recognition and catalytic mechanism (see paper)
44% identity, 98% coverage: 8:312/312 of query aligns to 3:309/321 of 1c9yA
- active site: R59 (= R63), T60 (= T64), V87 (≠ R91), R108 (= R112), H135 (= H139), Q138 (= Q142), D230 (= D232), C270 (= C272), R297 (= R300)
- binding phosphoric acid mono(formamide)ester: S57 (= S61), T58 (= T62), R59 (= R63), T60 (= T64), R108 (= R112), C270 (= C272), L271 (= L273), R297 (= R300)
- binding norvaline: L130 (= L134), N166 (= N170), D230 (= D232), S234 (= S236), M235 (= M237)
7novA Crystal structure of mycobacterium tuberculosis argf in complex with (4-methyl-3-nitrophenyl)boronic acid.
49% identity, 96% coverage: 12:312/312 of query aligns to 4:299/302 of 7novA
- active site: R96 (= R112), H123 (= H139), Q126 (= Q142), D219 (= D232), C259 (= C272), R287 (= R300)
- binding (4-methyl-3-nitro-phenyl)-oxidanyl-oxidanylidene-boron: R53 (= R63), F56 (≠ V66), E77 (= E93), V85 (= V101), Y89 (= Y105), L260 (= L273), A284 (= A297), R287 (= R300)
8qevA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with carbamoyl phosphate (see paper)
44% identity, 96% coverage: 12:312/312 of query aligns to 2:295/297 of 8qevA
7nnzB Crystal structure of mycobacterium tuberculosis argf in complex with 5-methyl-4-phenylthiazol-2-amine.
49% identity, 96% coverage: 12:312/312 of query aligns to 3:294/297 of 7nnzB
Query Sequence
>WP_015739792.1 NCBI__GCF_000024605.1:WP_015739792.1
MYASLRKRFRHRDFLSIADFTSEEIMGLLSFAAELKEAKKRGETHTFCAGKSLAMIFQKP
STRTRVSFEVAMFDLGGYALYLNAQDLQLGRGESIADTGRVLSRYVDGCVIRTFRQEEVE
ELAEAATIPVINGLTSWEHPCQILADFLTILQSKGRLAGLKLAYVGDGNNICHSLLLGCP
RVGMSIYVATPPQYAPHPTVVARAQEAARGTEVVVTEDPVQAVKGADVVVTDVWVSMGQE
EEAETKKKVFLPYQVNEELVSHAKPDFIFLHCLPAHRGEEVTAEIIDGPHSLVWEEAENR
LHVQKALLALLL
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