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Database: UniProt
Entry: A0A168G996_CORDF
LinkDB: A0A168G996_CORDF
Original site: A0A168G996_CORDF 
ID   A0A168G996_CORDF        Unreviewed;       356 AA.
AC   A0A168G996;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Ornithine carbamoyltransferase, mitochondrial {ECO:0000256|ARBA:ARBA00021536};
DE            EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007};
DE   AltName: Full=Ornithine transcarbamylase {ECO:0000256|ARBA:ARBA00033269};
GN   ORFNames=LEL_05878 {ECO:0000313|EMBL:OAA76194.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76194.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA76194.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76194.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAA76194.1}.
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DR   EMBL; AZHF01000004; OAA76194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168G996; -.
DR   STRING; 1081108.A0A168G996; -.
DR   OrthoDB; 2782890at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProt.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   NCBIfam; TIGR00658; orni_carb_tr; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          31..175
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          191..346
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  37829 MW;  9C70D3B8FBF889E2 CRC64;
     MSASPALRSA ARGAAHRLQQ RPYSSSTAAP RHLMSIADLS PTEFANLVRN GAARKTQVKS
     GQAPATLRDG MAGQTVAMMF SKRSTRTRVS TEAAVTLLGG HPMFLGKDDI QLGVNESLYD
     TSKVISSMTS CMVARVGPHS DVAGLARDSS VPVINALSED FHPLQTIADF LTLHEAFPSS
     SATSGGSLGL EGRKVAWVGD SNNVLFDLAI GCVKMGVDIA VASPQGYGIP DSMKAVINAA
     AQGVSSPGKL TETSVPEEAI KDADVLVTDT WISMGQESEK KKRLDAFAGY QITNELAKRG
     GAKDGWKFMH CLPRHAEEVA DEVFYSARSL VFPEAENRLW AAIAALEGFV VNKGKF
//
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