ID E3RU84_PYRTT Unreviewed; 840 AA.
AC E3RU84;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN ORFNames=PTT_12632 {ECO:0000313|EMBL:EFQ90716.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ90716.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ90716.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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DR EMBL; GL535102; EFQ90716.1; -; Genomic_DNA.
DR RefSeq; XP_003301189.1; XM_003301141.1.
DR AlphaFoldDB; E3RU84; -.
DR STRING; 861557.E3RU84; -.
DR EnsemblFungi; EFQ90716; EFQ90716; PTT_12632.
DR KEGG; pte:PTT_12632; -.
DR eggNOG; KOG3719; Eukaryota.
DR HOGENOM; CLU_013513_4_0_1; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:EnsemblFungi.
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:UP000001067};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 74..714
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 25..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 840 AA; 93214 MW; D50E3890FD0D53DD CRC64;
MAVRTFTQPS SLEDTLVKAS AMSGSENIAV RSEESAKNST QSYSSEAQAP LASHTNPNSR
PGITFAHQDS LPKLPIPELD SSCKKYIAAL KPLQSPKEHS DTIHSVEDFL KSDGVVLQEK
LKKYANGKAN YIEQFWYDSY LNFDNPVVLN LNPFFLLEDD PTPARNNQVT RAASLVVSAL
SFVRAVRREE LPPDTIKGQP LCMYQYSRLF GTARIPTEHG CQIGQDPTSK HVVVMCYGQF
YWFDVLDDNH DLIMTEKDIA LNLQVIVDDA QEIPIQDAAK GALGVLSTEN RKVWAGLRDV
LHREEGSNNS DCLNIVDSAL FVLCLDYTEP QTGADLCMNM LCGTSKIERG VQVGTCTNRW
YDKLQIIVCK NGSAGINFEH TGVDGHTVLR FASDVYTDTI LRFARTINGS APSLWASSSP
DPAKRDPDSF GDVQTTPHKL EWDMLPELST ALRFAETRLA DLIQQNEFAT LEFPHYGKNF
MTSMGFSPDA FVQMAFQAAY YGLYGRIECV YEPAMTKIYY HGRTEAIRSV TEESVEFLKT
FWGENPAAQK IEALRKACQK HTENTKVCSK AQGPDRHLYA LYCIWQRAID ESQDFASSDG
WDSTRPSSPD ASSPNRNSLL SETGSISSSP PPPSHHQHQV QHSMPALFAD AGWDKINTTI
LSTSNCGNPS LRQFGFGPTS ADGFGIGYII KDGSISICAS SKHRQTSRYI DALESYFLET
RKLLRQIQRS RGASGDKTAT RAREAEDRPS LMKQRGVKSR GRIILGDGAG KLQTPSESLV
DDDEEDDGLG GYGFFDAGML RQALSANRDY NNQGGSGGME PVERDVVRRN IGRRLRLAEY
//
