ID A0A316VC33_9BASI Unreviewed; 656 AA.
AC A0A316VC33;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acyltransferase ChoActase/COT/CPT {ECO:0000313|EMBL:PWN35227.1};
GN ORFNames=FA14DRAFT_160464 {ECO:0000313|EMBL:PWN35227.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN35227.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN35227.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN35227.1,
RC ECO:0000313|Proteomes:UP000245771};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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DR EMBL; KZ819603; PWN35227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316VC33; -.
DR STRING; 1280837.A0A316VC33; -.
DR InParanoid; A0A316VC33; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000245771; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
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:SF115; CARNITINE O-ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:PWN35227.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245771};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PWN35227.1}.
FT DOMAIN 70..622
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 9..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 656 AA; 73408 MW; D611F85132271FBE CRC64;
MQYLLRRVPG QARHQIGATS QSSTTTGRSG IQIGLQQQLQ QQKRNMILRA STTANGTGPL
WAGQNSLPSL PVPPLEETIP KYLRTTLPHQ DASSKAVTEK AVESALKGKD AALFKQLQER
LVARSKDPES DGNWLAAWWN DAAYMGYRDP VVPFVSYFYI HKDDLARRTY ATRAASQLKA
ILRFRDLVES EQLAPEKIKT GPLCSGSYPW MFNSVRIPEI PLDQAKKYPS AENNHVVVLH
NGRYFEFEVR HNGEELSAKE IEAQLEKIVT SSPEPSAFPV GALTSQNRDA WTHGREALLK
VAGAGAEQNK ATLQRIESSI IVICLDDLKP HTTEERAWEY WWGDGKNRFY DKQQLIVSQN
GKTGFMGEHS TMDGTPTLRM NDFVLSGIAA NKIDFGTSSR TDLPAPKELT FVLDQNVEGL
VTKAIQDFEA LKSEHDLAVL EFTAYGKEAI KKFKCSPDAW AQMVLQLAYF RLMGKVAPTY
ESAQTRKFKW GRTETIRSCS PESKAFCEAM ESNDVSDEER FEKFQAACKQ HLNYAKAAAD
GHGVDRHLFG LKKLLKEGEE LPDLYKDPMF GESGTWRMST SNVTSESFDA WGFGEVVPDG
FGCAYAIKGE SLTFSFTSRK LGASHLRHYV QQSALDLRDM HVRLANKQSG EGKPKL
//
