SitesBLAST
Comparing Ga0059261_3206 FitnessBrowser__Korea:Ga0059261_3206 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)
49% identity, 99% coverage: 4:306/307 of query aligns to 8:313/315 of Q51742
- W22 (≠ A18) mutation to A: Decreased heat stability.
- E26 (≠ A22) mutation to Q: Increased dissociation of dodecamers into trimers.
- M30 (≠ I25) mutation to A: Increased dissociation of dodecamers into trimers.
- W34 (≠ R29) mutation to A: Increased dissociation of dodecamers into trimers.
- Y228 (≠ V222) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (= A234) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E271) 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
42% identity, 100% coverage: 1:306/307 of query aligns to 9:312/316 of Q81M99
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
43% identity, 99% coverage: 1:303/307 of query aligns to 5:305/307 of 4nf2A
- active site: R55 (= R60), T56 (= T61), R83 (= R88), R104 (= R109), H131 (= H136), Q134 (= Q139), D226 (= D224), C265 (= C263), R293 (= R291)
- binding phosphoric acid mono(formamide)ester: S53 (= S58), T54 (= T59), R55 (= R60), T56 (= T61), R104 (= R109), H131 (= H136), Q134 (= Q139), C265 (= C263), L266 (= L264), R293 (= R291)
- binding norvaline: L126 (= L131), N162 (= N167), D226 (= D224), S230 (= S228), M231 (= M229)
8qeuA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with ornithine (see paper)
42% identity, 98% coverage: 4:304/307 of query aligns to 2:303/304 of 8qeuA
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
51% identity, 85% coverage: 44:303/307 of query aligns to 36:305/308 of 7nouA
- active site: R102 (= R109), H129 (= H136), Q132 (= Q139), D225 (= D224), C265 (= C263), R293 (= R291)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (≠ V53), T52 (= T59), R53 (= R60), R53 (= R60), F56 (≠ V63), F56 (≠ V63), L79 (= L86), D82 (≠ G89), E83 (= E90), V91 (= V98), Y95 (= Y102), L266 (= L264), R293 (= R291)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
51% identity, 85% coverage: 44:303/307 of query aligns to 36:305/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
51% identity, 85% coverage: 44:303/307 of query aligns to 36:305/308 of 7norA
7nnyA Crystal structure of mycobacterium tuberculosis argf in complex with naphthalen-1-ol.
51% identity, 85% coverage: 44:303/307 of query aligns to 36:305/308 of 7nnyA
- active site: R102 (= R109), H129 (= H136), Q132 (= Q139), D225 (= D224), C265 (= C263), R293 (= R291)
- binding 1-naphthol: T52 (= T59), R53 (= R60), F56 (≠ V63), E83 (= E90), V91 (= V98), Y95 (= Y102)
7nnwA Crystal structure of mycobacterium tuberculosis argf in complex with methyl 4-hydroxy-3-iodobenzoate.
51% identity, 85% coverage: 44:303/307 of query aligns to 36:305/308 of 7nnwA
- active site: R102 (= R109), H129 (= H136), Q132 (= Q139), D225 (= D224), C265 (= C263), R293 (= R291)
- binding methyl 3-iodanyl-4-oxidanyl-benzoate: I46 (≠ V53), T52 (= T59), R53 (= R60), F56 (≠ V63), L79 (= L86), L92 (= L99), Y95 (= Y102)
7nnvA Crystal structure of mycobacterium tuberculosis argf in complex with carbamoyl phosphate.
51% identity, 85% coverage: 44:303/307 of query aligns to 36:305/308 of 7nnvA
- active site: R102 (= R109), H129 (= H136), Q132 (= Q139), D225 (= D224), C265 (= C263), R293 (= R291)
- binding phosphoric acid mono(formamide)ester: S51 (= S58), T52 (= T59), R53 (= R60), T54 (= T61), R102 (= R109), H129 (= H136), C265 (= C263), L266 (= L264), R293 (= R291)
P9WIT9 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
51% identity, 85% coverage: 44:303/307 of query aligns to 35:304/307 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)
51% identity, 85% coverage: 44:303/307 of query aligns to 35:304/307 of 2i6uA
- active site: R52 (= R60), T53 (= T61), R80 (= R88), R101 (= R109), H128 (= H136), Q131 (= Q139), D224 (= D224), C264 (= C263), R292 (= R291)
- binding phosphoric acid mono(formamide)ester: S50 (= S58), T51 (= T59), R52 (= R60), T53 (= T61), R101 (= R109), C264 (= C263), L265 (= L264), R292 (= R291)
- binding norvaline: L123 (= L131), N160 (= N167), D224 (= D224), S228 (= S228), M229 (= M229)
8qevA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with carbamoyl phosphate (see paper)
41% identity, 98% coverage: 4:304/307 of query aligns to 2:296/297 of 8qevA
7np0A Crystal structure of mycobacterium tuberculosis argf in complex with (4-nitrophenyl)boronic acid.
51% identity, 85% coverage: 44:303/307 of query aligns to 36:302/305 of 7np0A
7nnzB Crystal structure of mycobacterium tuberculosis argf in complex with 5-methyl-4-phenylthiazol-2-amine.
49% identity, 85% coverage: 44:303/307 of query aligns to 35:294/297 of 7nnzB
7novA Crystal structure of mycobacterium tuberculosis argf in complex with (4-methyl-3-nitrophenyl)boronic acid.
50% identity, 85% coverage: 44:303/307 of query aligns to 36:299/302 of 7novA
- active site: R96 (= R109), H123 (= H136), Q126 (= Q139), D219 (= D224), C259 (= C263), R287 (= R291)
- binding (4-methyl-3-nitro-phenyl)-oxidanyl-oxidanylidene-boron: R53 (= R60), F56 (≠ V63), E77 (= E90), V85 (= V98), Y89 (= Y102), L260 (= L264), A284 (= A288), R287 (= R291)
P00481 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Rattus norvegicus (Rat) (see 2 papers)
42% identity, 94% coverage: 4:291/307 of query aligns to 40:330/354 of P00481
- R92 (= R60) mutation to L: Strong decrease in ornithine carbamoyltransferase activity.
- C303 (= C263) 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
P00480 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Homo sapiens (Human) (see 31 papers)
42% identity, 94% coverage: 4:291/307 of query aligns to 40:330/354 of P00480
- R40 (= R4) to H: in OTCD; late onset; dbSNP:rs72554308
- L43 (= L7) to F: in dbSNP:rs72554309
- K46 (≠ S10) to R: in dbSNP:rs1800321
- Y55 (≠ A19) to D: in OTCD; late onset; dbSNP:rs72554319
- L63 (≠ R27) to P: in OTCD; late onset; dbSNP:rs72554324
- K88 (= K56) modified: N6-acetyllysine; alternate; to N: in OTCD; late onset; dbSNP:rs72554339
- STRT 90:93 (= STRT 58:61) binding
- G100 (≠ A68) to D: in OTCD; late onset; dbSNP:rs72554349
- F101 (≠ I69) to L: in dbSNP:rs1133135
- L111 (= L79) to P: in dbSNP:rs1800324
- T125 (≠ A93) to M: in OTCD; neonatal; dbSNP:rs72554356
- D126 (= D94) to G: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; 0.9% of wild-type activity; dbSNP:rs72554358
- R129 (= R97) to H: in OTCD; early onset; decreased ornithine carbamoyltransferase activity; 2.1% of wild-type activity; dbSNP:rs66656800
- A140 (≠ V108) to P: in OTCD; late onset; dbSNP:rs72556260
- R141 (= R109) binding ; to Q: in OTCD; most common variant; loss of ornithine carbamoyltransferase activity; activity is 100-fold lower; dbSNP:rs68026851
- H168 (= H136) binding
- Q171 (= Q139) binding
- I172 (= I140) to M: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; dbSNP:rs72556280
- Y176 (≠ L144) to C: in OTCD; late onset; dbSNP:rs72556283
- TL 178:179 (≠ TI 146:147) natural variant: Missing (in OTCD; neonatal)
- Y183 (≠ G151) to D: in OTCD; late onset; dbSNP:rs72556292
- G188 (= G156) to R: in OTCD; neonatal; dbSNP:rs72556294
- G195 (= G163) to R: in OTCD; loss of ornithine carbamoyltransferase activity; dbSNP:rs67294955
- D196 (= D164) to V: in OTCD; neonatal; decreased ornithine carbamoyltransferase activity; 3.7% activity; dbSNP:rs72556300
- L201 (= L169) to P: in OTCD; neonatal; dbSNP:rs72558407
- S207 (≠ A175) to R: in OTCD; neonatal; dbSNP:rs72558415
- A209 (≠ G177) to V: in OTCD; neonatal; dbSNP:rs72558417
- M213 (≠ F181) to K: in OTCD; late onset
- H214 (≠ D182) to Y: in OTCD; neonatal; dbSNP:rs72558420
- P220 (= P188) to A: in OTCD; late onset; dbSNP:rs72558425
- P225 (vs. gap) to T: in OTCD; late onset; dbSNP:rs72558428
- L244 (≠ A205) to Q: in OTCD; late onset; dbSNP:rs72558436
- T262 (= T223) to K: in OTCD; mild; dbSNP:rs67333670
- T264 (= T225) to A: in OTCD; late onset; decreased ornithine carbamoyltransferase activity; 8.9% activity; dbSNP:rs72558444; to I: in OTCD; late onset; dbSNP:rs67156896
- W265 (= W226) to L: in OTCD; mild; dbSNP:rs72558446
- G269 (= G230) to E: in OTCD; neonatal; dbSNP:rs72558450
- Q270 (= Q231) to R: in dbSNP:rs1800328
- E272 (≠ H233) natural variant: Missing (in OTCD; late onset; dbSNP:rs72558452)
- R277 (vs. gap) to Q: in OTCD; late onset; dbSNP:rs66724222; to W: in OTCD; late onset; dbSNP:rs72558454
- H302 (= H262) to L: in OTCD; female; late onset; dbSNP:rs67993095; to Y: in OTCD; neonatal; dbSNP:rs72558463
- C303 (= C263) to R: in OTCD; neonatal; dbSNP:rs67468335
- CL 303:304 (= CL 263:264) binding
- E309 (= E270) natural variant: Missing (in OTCD; late onset)
- R330 (= R291) binding
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
- 333 natural variant: T -> A
- 340 S → P: in OTCD; late onset; dbSNP:rs72558489
- 343 T → K: in OTCD; late onset; dbSNP:rs72558491
1othA Crystal structure of human ornithine transcarbamoylase complexed with n-phosphonacetyl-l-ornithine (see paper)
41% identity, 94% coverage: 4:291/307 of query aligns to 7:297/321 of 1othA
- active site: R59 (= R60), T60 (= T61), V87 (≠ R88), R108 (= R109), H135 (= H136), Q138 (= Q139), D230 (= D224), C270 (= C263), R297 (= R291)
- binding n-(phosphonoacetyl)-l-ornithine: S57 (= S58), T58 (= T59), R59 (= R60), T60 (= T61), R108 (= R109), L130 (= L131), H135 (= H136), N166 (= N167), D230 (= D224), S234 (= S228), M235 (= M229), C270 (= C263), L271 (= L264), R297 (= R291)
1c9yA Human ornithine transcarbamylase: crystallographic insights into substrate recognition and catalytic mechanism (see paper)
41% identity, 94% coverage: 4:291/307 of query aligns to 7:297/321 of 1c9yA
- active site: R59 (= R60), T60 (= T61), V87 (≠ R88), R108 (= R109), H135 (= H136), Q138 (= Q139), D230 (= D224), C270 (= C263), R297 (= R291)
- binding phosphoric acid mono(formamide)ester: S57 (= S58), T58 (= T59), R59 (= R60), T60 (= T61), R108 (= R109), C270 (= C263), L271 (= L264), R297 (= R291)
- binding norvaline: L130 (= L131), N166 (= N167), D230 (= D224), S234 (= S228), M235 (= M229)
Query Sequence
>Ga0059261_3206 FitnessBrowser__Korea:Ga0059261_3206
MTYRNFLSLSDAGADGIAAMLADAIDRKRARAGQPKGAVDADAPLAGRTLAMVFEKNSTR
TRVSFEMAIRQLGGSAVVLDAATSQLGRGETVADTARVLSGYCDAIMVRTDDHAKLLEMA
QYATVPVINGLTDDSHPCQIMADLQTILESGKALPGLKVAWLGDGNNVLASIVEAAGLMH
FDVVAACPQSFALPEEAMALGKGRARTVNDPVEAVAGADVVVTDTWISMGQAHADVKLAA
LAPYQVTEALMAQASPDAKFLHCLPAHRGEEVTDAVIDGPQSLIWPEAENRLHAQKAVLR
WCFGQIG
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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