ID A8PFR2_COPC7 Unreviewed; 784 AA.
AC A8PFR2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Carnitine acetyl transferase {ECO:0000313|EMBL:EAU80725.2};
GN ORFNames=CC1G_04835 {ECO:0000313|EMBL:EAU80725.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU80725.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU80725.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU80725.2}.
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DR EMBL; AACS02000002; EAU80725.2; -; Genomic_DNA.
DR RefSeq; XP_001840991.2; XM_001840939.2.
DR AlphaFoldDB; A8PFR2; -.
DR STRING; 240176.A8PFR2; -.
DR GeneID; 6017649; -.
DR KEGG; cci:CC1G_04835; -.
DR VEuPathDB; FungiDB:CC1G_04835; -.
DR eggNOG; KOG3719; Eukaryota.
DR HOGENOM; CLU_013513_4_0_1; -.
DR InParanoid; A8PFR2; -.
DR OMA; HILVMRR; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000001861; 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; 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:UP000001861};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 82..694
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 13..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 784 AA; 86886 MW; B74B4BFEEDF14597 CRC64;
MLNSTFLTSL ARVFSPSSSS PTSSSSTVPP SQSQPQPITS QTTETAMPGL VINGTAPSTS
TAMVKDKPAG KTFAYQDRLP KLPIPPLEDT CKRYLRALVA LQDPEEHEAT KTAVKDFLEN
EGPVIQQKLI DWAKTKDSYI EEFWYESYLS HSDPVVLALN PFFVLENDPT PDRGAQLPRA
ASLIISSLGF IHDLRAGLLE PDMIRSTPLD MDQYTRLFGA ARIPTSRGCK MDVHPESRHI
VVLRRGQFYW FDVIDEDNRP LLTEREILRN LQAIVSDADK IDPCQVARNS IGVLTTENRK
TWSTLREMLI ADRNNQACLE VVDDALFIVC LDDTAPENLA DLCSNFLCGT YRLEGGEQVG
TCTNRWYDKL QIIVCADGAA GINFEHTGVD GHTVLRFAAD VFTEGLMLLA RSINPSAPTM
FHAKLSPYAK SYKPPRGDSP VSPRESIDTT PKKLEWKLSR ELRAGVRFAE TRLSDLICQN
DCQALEFKGY GKNFITSHGF SPDAFVQMAF QAAYFGLYGR IECVYEPAMT KAFLHGRTEA
IRSVQPESVA FTKTFYSDAT PHEKVNALRK ACERHSKLTK ECAQGLGQDR HLYALYCLLQ
RELQGNINPS PDDPAPKPAA ASKMPAIFTD PGWPQLCTSI LSTSNCGNPA LRLFGFGPVA
AEGYGLGYII KEDGISICAS SKHLQTRRYL DTLKNYLLEI QRMLVQLHRA ANARPAPFVD
HLGVLRDGKT GRPINGATSD SSDEEEIVPM PGYSFFDSGS VELLGRKKKS PFCDIGKVIP
LAEY
//
