ID A0A2C5ZGJ5_9HYPO Unreviewed; 1208 AA.
AC A0A2C5ZGJ5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CDD80_6028 {ECO:0000313|EMBL:PHH78910.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH78910.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH78910.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH78910.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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}.
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:PHH78910.1}.
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DR EMBL; NJES01000063; PHH78910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5ZGJ5; -.
DR STRING; 2004952.A0A2C5ZGJ5; -.
DR OrthoDB; 1386446at2759; -.
DR Proteomes; UP000226431; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProt.
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 Pfam; PF20775; Tag1; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000226431};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 429..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..172
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 187..338
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT REGION 371..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 130040 MW; 47001253D099C640 CRC64;
MRTSASRAAR CAAQRLQTRA YSQATRPRHL LSISDLSAGS LSSLVRNAAS RKEAVKAGRT
PPAFAQALAG KAVAMMFSKR STRTRVSTEA AVAMMGGHAM FLGKDDIQLG VNESLYDTSV
VISSMTSCMV ARVGPHSDVV NLAKDSSVPV INALSDDFHP LQTIADFLTM YETLASARSS
GPGLGLEGLK LAWIGDSNNV LFDLATGCIK LGVDIAVASP KGYSIPQPMK ELILSAADGV
KSPGRLSETT APEEAVKDAE VLVTDTWVSM GQESEMKKRL DAFSGYQITN ELAKRGGAKE
GWKFMHCLPR HQEEVDDEVF YGPRSLVFPE AENRLWAAAY TLTPQSLQID QAIQGLSKTY
RTASCRQDLS FIMPESEPTS PVPRDDEADA PSESTPLLSQ NDDSQNDPSS EPAKESADES
KNRWRWPSII AIIVLALLTL VVIGLGFVTP PAVREYVEKA AVLEPTSLSI ENLTADGVRA
RIQANFHLDS SRVSDDGARR IGRFVTGAVR RLEADVSPVA LRLPGFDNAL LGTAVVPALS
IDLVEGHHNR FDFVTDVNPG DSDVVRRIVN QWLAGELKQL KITGATELRL NSGIFPLGTH
QVAESVVLQA KDAPSMPEYN ISRLVVYDEP VGHHGKMVLA ANASVSLYNE YLIGFDIPPV
GLDVLVPNCN ASESNIQVAT ILADTIHVRP ESDVVVDAHA TVSKIPESLT RACPDTKLSP
LDSLMGRFLH GENAHVFVRG KVPAGSDLPD WAGSILESVV IPLPLGGHSF GNLLRNFSFS
DVHFKLPSPF ADPDDDSGKP RVSGTVQVLA ALPAKLDVDL AVDSLRANGD LFYHGDKFGQ
LRLDKWQNAN STMGSEDGQQ TIAIVSRVAD APIDILDGQV FGEIMQKLLF GDDDIVLDVK
AAVDISVATV LGKLVLRSIP AEGKIPVKRP PGDIFGAMKP QIEDVKIMNT SETGVSLRAS
ANLTNATPYT ADIPFLSVHI MKEGHQVGEA IIKDVALRAG HNSGLSGYAT WDPQTLGGES
AREAGRRLLS DYLSGKKTSV ELQAHRGSIP TAPALGEALS RLNLTLRTPR LKLPDDEEDE
HTTGFLRAAT FHVIRSTASF TLASPLQHDS VRILHVDATA LYNHSEPLGR IVHDEPFDVA
PGLSESPRLP VQWSGGRVGF DKLKKMLGGS LKLDAVANVT VALGEWTEEV EYRGRGIGAK
VALFMEDG
//
