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Database: UniProt
Entry: A0A1Y2W9F6_9PEZI
LinkDB: A0A1Y2W9F6_9PEZI
Original site: A0A1Y2W9F6_9PEZI 
ID   A0A1Y2W9F6_9PEZI        Unreviewed;       848 AA.
AC   A0A1Y2W9F6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN   ORFNames=M426DRAFT_57019 {ECO:0000313|EMBL:OTB05436.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB05436.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB05436.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB05436.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; KZ111543; OTB05436.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2W9F6; -.
DR   STRING; 1001833.A0A1Y2W9F6; -.
DR   InParanoid; A0A1Y2W9F6; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000242955; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          73..718
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          20..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   848 AA;  94246 MW;  C0553CE084EE6C3D CRC64;
     MPTQVRIFAM PKSLGETLSA SSSAPVSLLT ERTKPEKPAS PEIKSLVPIM ETIPEKPKEG
     GITFASQDSL PKLPIPELEQ TCKKYLAALK PLQGAREHSE TKFAVQDFLK KDGPELQKKL
     QEYAVGKTSY IEQFWYDSYL NFDNPVVLNL NPFFLLEDDP TPARNNQVTR AASLVVSALE
     FVRAVRREEL PPDTVKGTPL DMYQYSRLFG TARVPTENGC QIEQDPDSKH IVALCHGQIY
     WFDVLDDNSD LIMSERDIAI NLQTITDDAA QTPIQEAAKG ALGILSTENR KTWSGLRDVL
     TKEEGSNNAD CLGIVDSALF VLCLDYTEPS TAAALCQNML CGTNDVVKGV QVGTCINRWY
     DKLQIIVCKN GSAGINFEHT GVDGHTVLRF ASDLYTDTIL RFARTINGKA PSLWKTTSPD
     PSKRDPESFG DVTTTPHKLE WDISPELNIA IRFAETRLAD LISQNEFECL DFAGYGKNYI
     TSAGFSPDAF VQMAFQAAYY GLYGRIESTY EPAMTKAFLH GRTEAIRTVT EESVNFCQTF
     WADNSAEAKA EALRKACQQH TNSTRECSKG RGCDRHLYAL FCLWQRYLEG DASRSNSSLG
     YSSPVENGSE QGGSVVGSPG KESVLSNEEF RTRQRGDSTN SRYQENMVPA IFADNGWDKL
     NNTILSTSNC GNPSLRQFGF GPTSGGGFGI GYIIKEEGIN ICVASKHRQT KRFVDTLESY
     LLEIRRILRI TNRKGTTSRQ TRAREIDPDK PRTSHHRVKT RGRMITGTES LRALARSSTG
     TRSPTEESLM MSEDDELGGY GFFDAGMLLQ ALKARGEALD HQNESKAERA AANARRREIG
     KKLRLVEY
//
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