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Database: UniProt
Entry: A6QWG5_AJECN
LinkDB: A6QWG5_AJECN
Original site: A6QWG5_AJECN 
ID   A6QWG5_AJECN            Unreviewed;       794 AA.
AC   A6QWG5;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN   ORFNames=HCAG_01722 {ECO:0000313|EMBL:EDN03857.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN03857.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; CH476655; EDN03857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6QWG5; -.
DR   STRING; 339724.A6QWG5; -.
DR   VEuPathDB; FungiDB:HCAG_01722; -.
DR   HOGENOM; CLU_013513_4_0_1; -.
DR   OMA; HILVMRR; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000009297; 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; 1.
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; 2.
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   ECO:0000256|RuleBase:RU003801};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          75..148
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   DOMAIN          154..672
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   794 AA;  87602 MW;  8D229969149E6F1B CRC64;
     MAVRFFTMPK PLGETLAENE NSRNPKSPNG VSENKEMSRS AMAATDPTNS TPKSHPPEKV
     QNGITFANQD SLPKLPIPDL ESTCNRYLEC LAPLQSAREQ EETKAAVNEF LKTDGPELQN
     KLKNYATSKS SYIEQFWYDS YLNYDNPAWW RIETRVPTEN GCIIGQDSAA KHMVVLCRGQ
     FYWFDVLDDN NDLLMSERDI SLNLQVIIED AEQTPIQEAA KGALGVLSTE NRKVWSGLRD
     ILTKDRKSNN AECLNIVDTA LFVLCLDSTE PSNTSELCAN MLCGTNEVVR GVQIGTCTNR
     WYDKLQIIVC KNGSAGINFE HTGVDGHTVL RFASDVYTDT ILRFARTING QAPSLWATTS
     PPPSKRSPES FASNVSTTPH KLEWDMGPEL SIALRFAESH LADLLHQHEF QVLDFKGYGK
     NFITSMGISP DAFVQMAFQA AYYGLYGRVE NTYEPAMTKF FLHGRTEAVR TVSHESVEFV
     RTFWDERPAA EKVAALRKAT EKHTATTKIC SQGKGQDRHL YALYCLWQRS FDDGHGIINS
     GPPSTNGYSS PAENGSSIDS SPAPAHGSTA VSRPSSPSDD GISSSYSANS SRNIRLQHLA
     HTPALFNDAG WDKINTTILS TSNCGNPSLR HFGFGPTSGD GFGIGYIIKD DSISICASSK
     HRQTTRFIQS LETYLYEIRK LLRATQRKPV GPSCVRERQM DAESPTAPVV VAPGERVKGK
     GRLVRVDPQL VGGAGTVETP TTDGGDVEDD GMGGYGFFDA GMLLHALKGL QADRDRDKPP
     KRKLVGKVLK LNEY
//
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