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Database: UniProt
Entry: A0A0J6YB91_COCIT
LinkDB: A0A0J6YB91_COCIT
Original site: A0A0J6YB91_COCIT 
ID   A0A0J6YB91_COCIT        Unreviewed;       812 AA.
AC   A0A0J6YB91;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Carnitine O-palmitoyltransferase 2 {ECO:0000313|EMBL:KMP04063.1};
GN   ORFNames=CIRG_03754 {ECO:0000313|EMBL:KMP04063.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP04063.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; DS028094; KMP04063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6YB91; -.
DR   STRING; 404692.A0A0J6YB91; -.
DR   Proteomes; UP000054565; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR042572; Carn_acyl_trans_N.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589:SF29; MITOCHONDRIAL CARNITINE O-ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KMP04063.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          68..698
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        374
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   812 AA;  89859 MW;  1AFA53B0C374182F CRC64;
     MSHPPSPVRF FTMPKPLGDA LEGPSRPQVS SSTGAIPPSP KPSGEGNDGS VTNQTRVTFS
     KQDSLPRLPI PDLESTCRRY LESLAPLQSP SEHEETKASV QDFLKSDGPD LQEKLKLYAS
     SKTSYIEEFW YDSYLNYDNP VVLNLNPFFL LEDDPTPARN HQVTRAASLV VSALSFVRAV
     RREELTPDTV RGKPLCMFQY SRLFGTARVP TSNGCVIGQD SASKHLVIMC RGQFYWFDVL
     DENDDLIMSE KDISLNLSAI IEDAEQTPIQ EAAKGAIGVL STENRKVWSG LRDILNRQSG
     SNNADCLNIV DTALFVLCLD DAEPSNIAEI CGNMLCGTSE VVKGVQIGTC TNRWYDKLQI
     IVCQNGSAGI NFEHTGVDGH TVLRFASDVF TDTILRFAKT INGQAPSIWA STGPTPAKRK
     PNGYRHASTT PRKLEWDMGP ELSTAVRFAE SHIADLLHQH EFEALDFRAY GKNFITSMGF
     SPDAFVQMAF QAAYYGLYGR IENTYEPAMT KTYLHGRTEA IRTVSSESVD FVQTFWGDNP
     IAEKVNALRK ATQKHTAITR ECSQGQGHDR HLYALYSLWQ RSLDERQPSI CSGGSSPDGY
     SSPIEGGNSD DSHSSVSSRS GRSKMNHLPE IFKDPGWEKI NNTILSTSNC GNPSLRHFGF
     GPTSGDGFGI GYIIKDDSIS ICASSKHRQT SRFMQTLESY LLEIRKLLRA ASRPSEEPRA
     AAPPNAAQER LGTGTRTPRR GRLIHTDAAA REVDTPMTES GCFDDDGMGG YGFFDAGMLL
     QALQELQEVR ERGRDKKSRR RLVGKTLKLN DY
//
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