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Database: UniProt
Entry: R4X6C0_TAPDE
LinkDB: R4X6C0_TAPDE
Original site: R4X6C0_TAPDE 
ID   R4X6C0_TAPDE            Unreviewed;       749 AA.
AC   R4X6C0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Carnitine acetyl transferase {ECO:0000313|EMBL:CCG80555.1};
GN   ORFNames=TAPDE_000066 {ECO:0000313|EMBL:CCG80555.1};
OS   Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS   / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Taphrinaceae; Taphrina.
OX   NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG80555.1, ECO:0000313|Proteomes:UP000013776};
RN   [1] {ECO:0000313|EMBL:CCG80555.1, ECO:0000313|Proteomes:UP000013776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC   NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX   PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA   Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA   Overmyer K., Hauser P.M., Pagni M.;
RT   "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT   agent of peach leaf curl.";
RL   MBio 4:e00055-e00013(2013).
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:CCG80555.1}.
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DR   EMBL; CAHR02000002; CCG80555.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4X6C0; -.
DR   STRING; 1097556.R4X6C0; -.
DR   VEuPathDB; FungiDB:TAPDE_000066; -.
DR   eggNOG; KOG3719; Eukaryota.
DR   Proteomes; UP000013776; 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:UP000013776};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          22..645
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          362..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        328
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   749 AA;  83846 MW;  A86B69EF191D4217 CRC64;
     MPSAEHAEKS VTFAGQDDLK KLPIPDLSDT VSRYLSAVSP FQNAKELKRT EAAAQEFLKA
     DGPELQKLLI EYDKDQVSYI EQFWFDSYLN YDNPVVLNLN PFFLLEDDPT PARANQVTRA
     ASLTISSLCF IRCLRREELP PDMIRGKPLC MYQYSRLFGT SRIATDSGCK MQTNLTARHI
     AVLCRSQFYW FDVLDENNDI ILTEQYLAEN FRAIIDDAST IPPSQAAKSA MGVLTSESRS
     VWAGHRAKIN EDEDPNNKEC LDIIDSALFL VCLDDSEPVG KAAISENMLC GSYDIATGVQ
     VGTCTNRWYD KLQLIVCKNG SAGINFEHTG VDGHTVLRFV SDIYTDTIMR FAKTINPAAP
     NLWPSMSPDP SKRDPESFGD VDSTPHRLEW KLNSELSTAI RFAETRLSDL LLQNELQILE
     FTNYGSNFMK QSGFSPDAFV QMAFQAAYYG LYGRVQSVYE PAMTKSFRHG RTEAIRSTTN
     ESVNFVKRFC EDVNPQIKVD ALRKACTRHT AITRQASAGE GQDRHLYALF KMWEKQVADH
     KAGEHAKNPT SSNGDGSDVT RSPSDTSLSD AGHEMPALFA DCAWDRLNNT ILSTSNCGNP
     ALRMFGFGPT SLDGFGIGYI IKDNSISICA SSKHRQTSRF LETLSNYFLE IRGLIREVDE
     LRGVEKEKTR PEDKQKSRSR SGKPVTVTTA TEEADDDAGA GMLGGYGYFD FETLDKDILR
     QKANATKDED IGNVHRRHAI GRRLRLGEY
//
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