ID A0A165EJ27_EXIGL Unreviewed; 751 AA.
AC A0A165EJ27;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acyltransferase ChoActase/COT/CPT {ECO:0000313|EMBL:KZV87048.1};
GN ORFNames=EXIGLDRAFT_621139 {ECO:0000313|EMBL:KZV87048.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV87048.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV87048.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV87048.1,
RC ECO:0000313|Proteomes:UP000077266};
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, ECO:0000256|RuleBase:RU003801}.
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DR EMBL; KV426137; KZV87048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EJ27; -.
DR STRING; 1314781.A0A165EJ27; -.
DR InParanoid; A0A165EJ27; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000077266; 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; 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; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 20..639
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 364..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 751 AA; 84301 MW; 4971F089BFE84C9A CRC64;
MAPASNKTPT FSLQHKLPRL PVPPLEDTLK RYLRALRALQ DDREHEQSKR VVEEFLAEDG
PRVQEMLIEY AKDKDSYIEE FWYESYLSHS DPVVLRLNPF FVLEDDPTPT RGTQLPRAAS
LIAASLGFIH DLRNEVLEPD TVRGIPLDMD QYRRLFGTAR IPTPMGCRMD VSPQSQHIVV
IRRGQFYWFD VLDEQSRLLM TEREILRNLQ AIVTDADQTP AEQAAQHAVG VLTTENRKTW
SHLRRTLHKN RNNDACLKVV DQALFIVCLD DAAPENLADI CSNFLCGSYD LTAGGVQVGT
CTNRWYDKLQ IIVCANGASG INFEHTGVDG HTVLRFAADI FTEGLMLLAR SINPSAPTMF
SAPLSPQAKS YKPPRGATAN GNGNGKQEDL PPIDTTPKKL EWTLTPELRT GIRFAETRIS
DLICQNDCQA LEFKGFGKNF ITRYGFSPDA FVQMAFQAAY FGLYGRIECT YEPAMTKSFI
HGRTEAIRTV QEHTVNFTKT FFSDASVDDK IKALRHACDG HVNLTKECSK GLGQDRHLYA
LYCLLQRELS DALSSSPPPS TSSSARKTLP AIFSDPGWSL LNTSILSTSN CGNPALRLFG
FGPVAEDGFG IGYIIKDEGI SVCASSKHLQ TRRYLDTLQG YLFDVQRMVL QLHRQANERP
RPFVDHAGVL RDARTGVPIS AAYIDTEEED EREADAGYSF FDSGEVDLLK RARTREHRFL
VGMCGFSRPL FRVRSSRLFL FAGKPLPIAE Y
//
