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Database: UniProt
Entry: A0A165IFN0_9BASI
LinkDB: A0A165IFN0_9BASI
Original site: A0A165IFN0_9BASI 
ID   A0A165IFN0_9BASI        Unreviewed;       366 AA.
AC   A0A165IFN0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=ornithine carbamoyltransferase {ECO:0000256|ARBA:ARBA00013007};
DE            EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007};
GN   ORFNames=CALCODRAFT_429120 {ECO:0000313|EMBL:KZT60510.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60510.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT60510.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60510.1,
RC   ECO:0000313|Proteomes:UP000076842};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805}.
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DR   EMBL; KV423930; KZT60510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165IFN0; -.
DR   STRING; 1353952.A0A165IFN0; -.
DR   InParanoid; A0A165IFN0; -.
DR   OrthoDB; 2782890at2759; -.
DR   Proteomes; UP000076842; 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   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:UP000076842};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          6..156
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          197..350
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
SQ   SEQUENCE   366 AA;  39987 MW;  7A8371E092F9B4A5 CRC64;
     MASPPHLLTL ADLSVKQLKS SLTHAAYLKR VSLPILQPRP HGSYTLFPPK TLSDKTIALL
     FSKRSTRTRL SAESAAHLLG GHPMFLSSAD IQLGVNESLQ DSARVIGGLV DGVFARVGDH
     SEIVTLAQHS PVPVLNALSS LWHPTQILAD LLTLLEHLPS PDPLPTAPIS SISPGHSIPA
     DAVPGDLPPK LDFDVLKGLT ISWLGDSTNV LHDMLVTYPR LGAKVRVAVP KEYPCPGEVW
     DRVVQLGCDK GIDWSDDPLR AVEGADIVVT DTWVSMGQES EKAARLRAFA GYQVTEALCK
     QGGAAEDWKF LHCLPRKPDE VDDGVFYGKR SLVWEEAENR KWTIMALFEY VPPFFLLVGC
     ASWSWS
//
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