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
//