ID W9WP11_9EURO Unreviewed; 842 AA.
AC W9WP11;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|EMBL:EXJ69907.1};
GN ORFNames=A1O5_06980 {ECO:0000313|EMBL:EXJ69907.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ69907.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ69907.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ69907.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) 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:EXJ69907.1}.
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DR EMBL; AMGX01000010; EXJ69907.1; -; Genomic_DNA.
DR RefSeq; XP_007745759.1; XM_007747569.1.
DR AlphaFoldDB; W9WP11; -.
DR STRING; 1182543.W9WP11; -.
DR GeneID; 19191686; -.
DR eggNOG; KOG3719; Eukaryota.
DR HOGENOM; CLU_013513_4_0_1; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000019471; 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; PS00439; ACYLTRANSF_C_1; 1.
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:UP000019471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXJ69907.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 83..728
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 842 AA; 93500 MW; 95EDF478519B043F CRC64;
MSSSGTGARY FARPKSLDAT LNNSSRENGV HANMSNGQVE RSLEAAKETT DAYTKVEKEP
LSLKKELSKQ GITFAAQDKL PKLPIPELES TMKKYLDALA PLQSPSEHNE TKAAVRDFVE
NEGKDLQDRL KKYATGRTSY IEQFWYDSYL NYDNPVVLNL NPFFLLEDDP TPARNNQVTR
AASLVISALC FVRAVRKEEL PPDTLRGTPL CMYQYSRLFG TARVPTENGC IIGQDSDSKH
VVVMCRGQFY WFDVLDDNND LIMTEKDFAI NLQVIVDDAQ QTPIQEAAKG AIGVLSTENR
KVWSHLRDLL TREEGSNNAD CLSIVDSALF MVCLDYTEPA DVSQLCGNML CGTSEVERGV
QVGTCTNRWY DKLQIIVCKN GSAGINFEHT GVDGHTVLRF ASDVYTDTIL RFAKSINGQA
PTLWTSQSPD PSKRDPNSFG DVSTTPHKLE WDMHPELQIA LRFAETRLAD LINQNEFQTL
DFAGYGKNFI TSMGFSPDAF VQMAFQAAYY GLYGRVENTY EPAMTKTFFH GRTEAIRTVT
PECVEFVKTF WADNPAQKKV DALTTATKKH TAITKESSKA QGPDRHLYAL YCVWQRKVND
ESAEVGSTAG FSSNGYSSPT DMSDLGSPKR LEETSSPISR SRTGTESSRS PAPALQHMPA
LFSDPGWDKI NNTIISTSNC GNPSLRHFGF GPTSGDGFGI GYIIKDDSIS VCASSKHRQT
QRFVDSLESY LHEIRRLLKA TKTKDIAASK ITRAREAEEK AGKDGRLKSR GRVIKTEASK
VDGFQTPTSL DTAEVEDDGL GGYGFFDAGM LLQALKKDQP KPSEQIVQRR RTVGKKLALS
EY
//
