ID A0A165TUE1_9APHY Unreviewed; 597 AA.
AC A0A165TUE1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acyltransferase ChoActase/COT/CPT {ECO:0000313|EMBL:KZT73967.1};
GN ORFNames=DAEQUDRAFT_721471 {ECO:0000313|EMBL:KZT73967.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT73967.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT73967.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT73967.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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DR EMBL; KV429035; KZT73967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165TUE1; -.
DR STRING; 1314783.A0A165TUE1; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000076727; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:KZT73967.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZT73967.1}.
FT DOMAIN 11..568
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 597 AA; 67090 MW; 0AB3B59B4D5682ED CRC64;
MLRFEASLPH LPVPPLASTT AKYLETVQPH LTPEQYSKTQ AAVKAFADSE LGKELQARLE
ARAREPGMQS WLADWWNDVA YMGYRDPVVV YVSYFYVHVD DKHRPSQAKR AAQLLKAILP
FRYLVESQQL EPEKVKGVPL AMHSYEYLFH SSRYPVKPSD TARKFDAETH NHVVFVRKNK
FFKVPLADKN GRELSATELE VQIERVIALA GSEKASPVGA LTSENRDTWA DARAALLAAS
PSNAASLEEV ESAMIIVPLD DITPITREDA SWACWVGDGR NRFYDKHQLI VFENGKSGFL
GEHSCMDGTP TLRLNEFLLA SLALGKVDLG PARTAETAKD LEAPKELTFV LDSKTEQYIK
QAESNFDGLV GKHDMEVLHY EGYGKEYIKK FKTSPDAWAQ LVKQLAFHKM FSRPGVCYES
AQTRKYQRGR TEVIRAASNE SKAWAEAMLN PSESDEKRAA LFRKAVTRHL QYAAWAADGQ
GVDRHLFGLK MMLKEGEPTP PIYTDEAYSK TNHWELSTSN LSSPFLDGWG YGEVVPDGYG
LSYSIGDEYI RWTITSLKRR TGELKHYLAE AATETRQMME RAAAAEASKQ GDGKAKL
//
