SitesBLAST
Comparing CCNA_02325 FitnessBrowser__Caulo:CCNA_02325 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)
51% identity, 84% coverage: 49:310/311 of query aligns to 47:313/315 of Q51742
- Y228 (≠ V226) mutation to C: Becomes active at low temperatures; when associated with G-278.
- A241 (≠ H238) mutation to D: Becomes active at low temperatures; when associated with G-278.
- E278 (= E275) 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
- 22 W→A: Decreased heat stability.
- 26 E→Q: Increased dissociation of dodecamers into trimers.
- 30 M→A: Increased dissociation of dodecamers into trimers.
- 34 W→A: Increased dissociation of dodecamers into trimers.
Q81M99 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Bacillus anthracis
45% identity, 84% coverage: 49:310/311 of query aligns to 47:312/316 of Q81M99
4nf2A Crystal structure of anabolic ornithine carbamoyltransferase from bacillus anthracis in complex with carbamoyl phosphate and l- norvaline
46% identity, 83% coverage: 49:307/311 of query aligns to 43:305/307 of 4nf2A
- active site: R55 (= R61), T56 (= T62), R83 (= R89), R104 (= R110), H131 (= H137), Q134 (= Q140), D226 (= D228), C265 (= C267), R293 (= R295)
- binding phosphoric acid mono(formamide)ester: S53 (= S59), T54 (= T60), R55 (= R61), T56 (= T62), R104 (= R110), H131 (= H137), Q134 (= Q140), C265 (= C267), L266 (= L268), R293 (= R295)
- binding norvaline: L126 (= L132), N162 (= N168), D226 (= D228), S230 (= S232), M231 (= M233)
8qeuA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with ornithine (see paper)
43% identity, 98% coverage: 5:308/311 of query aligns to 2:303/304 of 8qeuA
8qevA Crystal structure of ornithine transcarbamylase from arabidopsis thaliana (atotc) in complex with carbamoyl phosphate (see paper)
42% identity, 98% coverage: 5:308/311 of query aligns to 2:296/297 of 8qevA
P9WIT9 Ornithine carbamoyltransferase; OTCase; EC 2.1.3.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
47% identity, 83% coverage: 49:307/311 of query aligns to 40:304/307 of P9WIT9
7nouA Crystal structure of mycobacterium tuberculosis argf in complex with (3,5-dichlorophenyl)boronic acid.
47% identity, 83% coverage: 49:307/311 of query aligns to 41:305/308 of 7nouA
- active site: R102 (= R110), H129 (= H137), Q132 (= Q140), D225 (= D228), C265 (= C267), R293 (= R295)
- binding [3,5-bis(chloranyl)phenyl]-oxidanyl-oxidanylidene-boron: I46 (= I54), T52 (= T60), R53 (= R61), R53 (= R61), F56 (= F64), F56 (= F64), L79 (= L87), D82 (≠ G90), E83 (= E91), V91 (= V99), Y95 (≠ M103), L266 (= L268), R293 (= R295)
7nosA Crystal structure of mycobacterium tuberculosis argf in complex with 4-bromo-6-(trifluoromethyl)-1h-benzo[d]imidazole.
47% identity, 83% coverage: 49:307/311 of query aligns to 41:305/308 of 7nosA
7norA Crystal structure of mycobacterium tuberculosis argf in complex with 2-fluoro-4-hydroxybenzonitrile.
47% identity, 83% coverage: 49:307/311 of query aligns to 41:305/308 of 7norA
7nnyA Crystal structure of mycobacterium tuberculosis argf in complex with naphthalen-1-ol.
47% identity, 83% coverage: 49:307/311 of query aligns to 41:305/308 of 7nnyA
- active site: R102 (= R110), H129 (= H137), Q132 (= Q140), D225 (= D228), C265 (= C267), R293 (= R295)
- binding 1-naphthol: T52 (= T60), R53 (= R61), F56 (= F64), E83 (= E91), V91 (= V99), Y95 (≠ M103)
7nnwA Crystal structure of mycobacterium tuberculosis argf in complex with methyl 4-hydroxy-3-iodobenzoate.
47% identity, 83% coverage: 49:307/311 of query aligns to 41:305/308 of 7nnwA
- active site: R102 (= R110), H129 (= H137), Q132 (= Q140), D225 (= D228), C265 (= C267), R293 (= R295)
- binding methyl 3-iodanyl-4-oxidanyl-benzoate: I46 (= I54), T52 (= T60), R53 (= R61), F56 (= F64), L79 (= L87), L92 (= L100), Y95 (≠ M103)
7nnvA Crystal structure of mycobacterium tuberculosis argf in complex with carbamoyl phosphate.
47% identity, 83% coverage: 49:307/311 of query aligns to 41:305/308 of 7nnvA
- active site: R102 (= R110), H129 (= H137), Q132 (= Q140), D225 (= D228), C265 (= C267), R293 (= R295)
- binding phosphoric acid mono(formamide)ester: S51 (= S59), T52 (= T60), R53 (= R61), T54 (= T62), R102 (= R110), H129 (= H137), C265 (= C267), L266 (= L268), R293 (= R295)
2i6uA Crystal structure of ornithine carbamoyltransferase complexed with carbamoyl phosphate and l-norvaline from mycobacterium tuberculosis (rv1656) at 2.2 a (see paper)
47% identity, 83% coverage: 49:307/311 of query aligns to 40:304/307 of 2i6uA
- active site: R52 (= R61), T53 (= T62), R80 (= R89), R101 (= R110), H128 (= H137), Q131 (= Q140), D224 (= D228), C264 (= C267), R292 (= R295)
- binding phosphoric acid mono(formamide)ester: S50 (= S59), T51 (= T60), R52 (= R61), T53 (= T62), R101 (= R110), C264 (= C267), L265 (= L268), R292 (= R295)
- binding norvaline: L123 (= L132), N160 (= N168), D224 (= D228), S228 (= S232), M229 (= M233)
7np0A Crystal structure of mycobacterium tuberculosis argf in complex with (4-nitrophenyl)boronic acid.
47% identity, 83% coverage: 49:307/311 of query aligns to 41:302/305 of 7np0A
7nnzB Crystal structure of mycobacterium tuberculosis argf in complex with 5-methyl-4-phenylthiazol-2-amine.
46% identity, 83% coverage: 49:307/311 of query aligns to 40:294/297 of 7nnzB
7novA Crystal structure of mycobacterium tuberculosis argf in complex with (4-methyl-3-nitrophenyl)boronic acid.
46% identity, 83% coverage: 49:307/311 of query aligns to 41:299/302 of 7novA
- active site: R96 (= R110), H123 (= H137), Q126 (= Q140), D219 (= D228), C259 (= C267), R287 (= R295)
- binding (4-methyl-3-nitro-phenyl)-oxidanyl-oxidanylidene-boron: R53 (= R61), F56 (= F64), E77 (= E91), V85 (= V99), Y89 (≠ M103), L260 (= L268), A284 (= A292), R287 (= R295)
P00481 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Rattus norvegicus (Rat) (see 2 papers)
44% identity, 79% coverage: 49:295/311 of query aligns to 80:330/354 of P00481
- R92 (= R61) mutation to L: Strong decrease in ornithine carbamoyltransferase activity.
- C303 (= C267) 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
1othA Crystal structure of human ornithine transcarbamoylase complexed with n-phosphonacetyl-l-ornithine (see paper)
43% identity, 79% coverage: 49:295/311 of query aligns to 47:297/321 of 1othA
- active site: R59 (= R61), T60 (= T62), V87 (≠ R89), R108 (= R110), H135 (= H137), Q138 (= Q140), D230 (= D228), C270 (= C267), R297 (= R295)
- binding n-(phosphonoacetyl)-l-ornithine: S57 (= S59), T58 (= T60), R59 (= R61), T60 (= T62), R108 (= R110), L130 (= L132), H135 (= H137), N166 (= N168), D230 (= D228), S234 (= S232), M235 (= M233), C270 (= C267), L271 (= L268), R297 (= R295)
1c9yA Human ornithine transcarbamylase: crystallographic insights into substrate recognition and catalytic mechanism (see paper)
43% identity, 79% coverage: 49:295/311 of query aligns to 47:297/321 of 1c9yA
- active site: R59 (= R61), T60 (= T62), V87 (≠ R89), R108 (= R110), H135 (= H137), Q138 (= Q140), D230 (= D228), C270 (= C267), R297 (= R295)
- binding phosphoric acid mono(formamide)ester: S57 (= S59), T58 (= T60), R59 (= R61), T60 (= T62), R108 (= R110), C270 (= C267), L271 (= L268), R297 (= R295)
- binding norvaline: L130 (= L132), N166 (= N168), D230 (= D228), S234 (= S232), M235 (= M233)
P00480 Ornithine transcarbamylase, mitochondrial; OTCase; Ornithine carbamoyltransferase, mitochondrial; EC 2.1.3.3 from Homo sapiens (Human) (see 31 papers)
43% identity, 79% coverage: 49:295/311 of query aligns to 80:330/354 of P00480
- K88 (= K57) modified: N6-acetyllysine; alternate; to N: in OTCD; late onset; dbSNP:rs72554339
- STRT 90:93 (= STRT 59:62) binding
- G100 (≠ A69) to D: in OTCD; late onset; dbSNP:rs72554349
- F101 (≠ M70) to L: in dbSNP:rs1133135
- L111 (≠ S80) to P: in dbSNP:rs1800324
- T125 (≠ E94) to M: in OTCD; neonatal; dbSNP:rs72554356
- D126 (= D95) to G: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; 0.9% of wild-type activity; dbSNP:rs72554358
- R129 (≠ K98) to H: in OTCD; early onset; decreased ornithine carbamoyltransferase activity; 2.1% of wild-type activity; dbSNP:rs66656800
- A140 (≠ I109) to P: in OTCD; late onset; dbSNP:rs72556260
- R141 (= R110) binding ; to Q: in OTCD; most common variant; loss of ornithine carbamoyltransferase activity; activity is 100-fold lower; dbSNP:rs68026851
- H168 (= H137) binding
- Q171 (= Q140) binding
- I172 (= I141) to M: in OTCD; early onset; loss of ornithine carbamoyltransferase activity; dbSNP:rs72556280
- Y176 (≠ I145) to C: in OTCD; late onset; dbSNP:rs72556283
- TL 178:179 (≠ TI 147:148) natural variant: Missing (in OTCD; neonatal)
- Y183 (≠ R152) to D: in OTCD; late onset; dbSNP:rs72556292
- G188 (= G157) to R: in OTCD; neonatal; dbSNP:rs72556294
- G195 (= G164) to R: in OTCD; loss of ornithine carbamoyltransferase activity; dbSNP:rs67294955
- D196 (= D165) to V: in OTCD; neonatal; decreased ornithine carbamoyltransferase activity; 3.7% activity; dbSNP:rs72556300
- L201 (≠ C170) to P: in OTCD; neonatal; dbSNP:rs72558407
- S207 (≠ A176) to R: in OTCD; neonatal; dbSNP:rs72558415
- A209 (≠ P178) to V: in OTCD; neonatal; dbSNP:rs72558417
- M213 (≠ F182) to K: in OTCD; late onset
- H214 (≠ E183) to Y: in OTCD; neonatal; dbSNP:rs72558420
- P220 (= P189) to A: in OTCD; late onset; dbSNP:rs72558425
- P225 (≠ A194) to T: in OTCD; late onset; dbSNP:rs72558428
- L244 (≠ V209) to Q: in OTCD; late onset; dbSNP:rs72558436
- T262 (≠ A227) to K: in OTCD; mild; dbSNP:rs67333670
- T264 (= T229) to A: in OTCD; late onset; decreased ornithine carbamoyltransferase activity; 8.9% activity; dbSNP:rs72558444; to I: in OTCD; late onset; dbSNP:rs67156896
- W265 (= W230) to L: in OTCD; mild; dbSNP:rs72558446
- G269 (= G234) to E: in OTCD; neonatal; dbSNP:rs72558450
- Q270 (vs. gap) to R: in dbSNP:rs1800328
- E272 (≠ T236) natural variant: Missing (in OTCD; late onset; dbSNP:rs72558452)
- R277 (= R241) to Q: in OTCD; late onset; dbSNP:rs66724222; to W: in OTCD; late onset; dbSNP:rs72558454
- H302 (= H266) to L: in OTCD; female; late onset; dbSNP:rs67993095; to Y: in OTCD; neonatal; dbSNP:rs72558463
- C303 (= C267) to R: in OTCD; neonatal; dbSNP:rs67468335
- CL 303:304 (= CL 267:268) binding
- E309 (= E274) natural variant: Missing (in OTCD; late onset)
- R330 (= R295) 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
- 40 R → H: in OTCD; late onset; dbSNP:rs72554308
- 43 L → F: in dbSNP:rs72554309
- 46 K → R: in dbSNP:rs1800321
- 55 Y → D: in OTCD; late onset; dbSNP:rs72554319
- 63 L → P: in OTCD; late onset; dbSNP:rs72554324
- 333 natural variant: T -> A
- 340 S → P: in OTCD; late onset; dbSNP:rs72558489
- 343 T → K: in OTCD; late onset; dbSNP:rs72558491
Query Sequence
>CCNA_02325 FitnessBrowser__Caulo:CCNA_02325
MTQPRHFIDLWKLDGATLRLLLDDAHARKAARKGWPQGKVDADAPAKDRVLSMIFQKNST
RTRFSFDAAMRQLGGSAIISTASDMQLGRGETIEDTAKVLSRMVDAVMIRANSHADVERF
AQVSTVPIINGLTDKSHPCQIMADILTIEEHRGPIAGKTIAWVGDGNNVCSSFIHAAPLL
GFELKIACPAVYHADLHDLARAEGLQGKVSMTTDPKAAVSGADVVVADTWVSMGDTDHDE
RLAALEPYQVDDRLMDLAAGNGVFLHCLPAHRGEEVTDAVLDGPRSLVWDEAENRIHAQK
SVLAWCFGAIG
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