ID   A0A165M7V1_9APHY        Unreviewed;       748 AA.
AC   A0A165M7V1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Acyltransferase ChoActase/COT/CPT {ECO:0000313|EMBL:KZT65330.1};
GN   ORFNames=DAEQUDRAFT_752616 {ECO:0000313|EMBL:KZT65330.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT65330.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT65330.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT65330.1,
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, ECO:0000256|RuleBase:RU003801}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV429107; KZT65330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165M7V1; -.
DR   STRING; 1314783.A0A165M7V1; -.
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; 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:UP000076727};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          31..657
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   748 AA;  83515 MW;  69F0DABF96E405A7 CRC64;
     MPEDSQTPLT KFETDKPQSR TFARQHELPR LPIPSLEDTC RRYLTALEGL QDQKEHAKTK
     VAVEDFLRND GPKWQERLAK YAEDKASYIE EFWYESYLSH SDPVVLALNP FFVLENDPTP
     DRGSQLPRAA SLILSSLGFI HDLRAGMLEP DTIRGTPLDM DQYTRLFGTA RIPTDRGCRM
     EIHSESRHIV VLRRGQFYWF DVLDADNRPV LTEQEILRNL EAIVKDAEDV PLHEVARNSI
     GVLSTENRKV WSTLRTALSN NHNNESCLQI IDNALFVVCL DDATPENLAE LCNNFLSGTY
     NLKGGVQVGT CTNRWYDKLQ IIVCADGSAG INFEHTGVDG HTVLRFAADI FTEGLMLLAR
     SINPSAPTLF HAPLSPYAKS YKPPRGAATH TAARLPPPSY VIDTAPKKLE WALYPELRAA
     IRFAETHLSD LICQNDCQAL EFKGYGKNFI TSHGFSPDAF VQMAFQAAYY GLYGRIECTY
     EPAMTKHFLH GRTEAIRTVQ PQTVNFVKTF FSEAPLSQKI AALRNACQGH VKLTKECSQG
     LGQDRHLYAL YCLIQRDREA AVDAEAPPSP GGSMTSTSST SADKPPLPAI FTDPGWRTLG
     TSILSTSNCG NPALRLFGFG PVAADGYGIG YIIKDEGISV CASSKHLQTR RFLDTLEGYL
     LDIKRMLIQQ HLSANPKREP FVDHAGILRD SKTGRPINGQ AHGYGEYDDA LMPGYSFFDS
     GDVELLGRRK RMPSYYNTGK IIPLAEYS
//