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Database: UniProt
Entry: A0A0G2FT73_9PEZI
LinkDB: A0A0G2FT73_9PEZI
Original site: A0A0G2FT73_9PEZI 
ID   A0A0G2FT73_9PEZI        Unreviewed;       818 AA.
AC   A0A0G2FT73;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative carnitine acetyl transferase {ECO:0000313|EMBL:KKY37342.1};
GN   ORFNames=UCDDA912_g02687 {ECO:0000313|EMBL:KKY37342.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY37342.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY37342.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY37342.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY37342.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY37342.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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:KKY37342.1}.
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DR   EMBL; LCUC01000090; KKY37342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2FT73; -.
DR   STRING; 1214573.A0A0G2FT73; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000034680; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR042572; Carn_acyl_trans_N.
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   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKY37342.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          23..675
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          545..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        329
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   818 AA;  90796 MW;  AFE2A60AC3C211EC CRC64;
     MGVNENRSYP GVTFAQQDKL PKLPIPELAS SCDKYLAALK PLQSPREHSD TKQAVQEFLN
     NEGPELQEKL KRYAEGRTSY IEQFWYDSYL NYDNPVVLNL NPFFLLEDDP TPARNNQVTR
     AASLVVSALE FVRAVRKEEL PPDTVKGTAM DMYQYSRLFG TARVPTEAGC QIEQDPESKH
     LVVMCHGQFY WFDVLDDNSD LIMTEKDVSI NLQTIIDDAA QMPIQDAAKG ALGVLSTENR
     KVWSGLRDVL TREQGSNNAD CLGIVDSALF IVCLDYTEPA TVSALCQNML CGTSEIEKGV
     QIGTCTNRWY DKLQIIVCKN GSAGINFEHT GVDGHTVLRF ASDVYTDTIL RFARTINGQA
     PTLWASTSPD PSKRDPDSFG DVNTTPHKLE WDMIPELKIA VRFAETRLAD LIEQNEFQCL
     DFQAYGKNFI TSMGFSPDAF IQMAFQAAYY GLYGRIECTY EPAMTKMYLH GRTEAVRTVS
     DESVNFVQTF WADNPAEQKV EALKRACQTH VNNTKECAKG QGCDRHMYAL FCLWQRLMDE
     TAVSRSTGSS GYTSPVDGAS SPEPGVASPT RDSAVSAGSE HTTQNMVTRA RGDSTNSRGG
     SQQQLPLIFA DSGWDKLNNT IMSTSNCGNP SLRQFGFGPV SGDGFGIGYI IKDDGIAICI
     SSKHRQTKRF VDTLESYLLE IRRILRITSR HPSAPKQTRA REIDRSTHHH HRKPTFNRLK
     SRGRLITGPT AETIRSQKLG SVAGTQSPTD ESVTLSEDDE LGGYGFFDAG MLLQALKARG
     EVDGGETKAS ERAAVQARRR DVGVERTVGD DEDGRVQQ
//
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