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Database: UniProt
Entry: A0A0D2CRT4_9EURO
LinkDB: A0A0D2CRT4_9EURO
Original site: A0A0D2CRT4_9EURO 
ID   A0A0D2CRT4_9EURO        Unreviewed;       345 AA.
AC   A0A0D2CRT4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=PV05_08336 {ECO:0000313|EMBL:KIW52712.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW52712.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW52712.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW52712.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN847321; KIW52712.1; -; Genomic_DNA.
DR   RefSeq; XP_013313296.1; XM_013457842.1.
DR   AlphaFoldDB; A0A0D2CRT4; -.
DR   STRING; 348802.A0A0D2CRT4; -.
DR   GeneID; 25330244; -.
DR   HOGENOM; CLU_043846_3_0_1; -.
DR   OrthoDB; 2782890at2759; -.
DR   Proteomes; UP000054342; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:UP000054342};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          27..168
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          179..330
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   345 AA;  37753 MW;  243A28580F40FCEC CRC64;
     MAALRSIVRP IQQPSRALST SSSSNPRHLL SLSNVTSTEL ATLVNNATYH KTHRADTSWP
     LRDALSGQTI ALLFSKLSTR TRVSTEGAVA SMGGHPMFLG KNDIQLGVNE SLYDTSVVIS
     SMVSSIVARV GPHADIANLA KDSSVPVINA LCDTYHPMQI IADFATLTQT FKQPAEKLKG
     LKIAWVGDAN NVLFDMCIGA KKLGIDMAVA TPKGYEIPGK MKQEIKDTEG QGTLSETNQP
     EEAVKSCDII VTDTWISMGQ EEEKAKRLKE FEGFQVTEEM ARRGGAGKEW KFMHCLPRHA
     EEVSDEVFYG KRSLVFPEAQ NRLWSAIATL EGFVANKGVI RQAEK
//
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