ID A0A0D2AV87_9EURO Unreviewed; 848 AA.
AC A0A0D2AV87;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN ORFNames=PV07_05017 {ECO:0000313|EMBL:KIW29187.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW29187.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW29187.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW29187.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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DR EMBL; KN847042; KIW29187.1; -; Genomic_DNA.
DR RefSeq; XP_016249403.1; XM_016391884.1.
DR AlphaFoldDB; A0A0D2AV87; -.
DR STRING; 569365.A0A0D2AV87; -.
DR GeneID; 27344211; -.
DR VEuPathDB; FungiDB:PV07_05017; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000054466; 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; 2.
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:UP000054466};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 89..734
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 25..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 395
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 848 AA; 94169 MW; DC07369CACD5E422 CRC64;
MIQILTMSST GTGTRYFARP KSLDETLKSS SPENGAHANM SSNQVERSLE AAKEATSSYT
KAEKEPVSSK MEVSKQGITF AAQDKLPKLP IPELDSTMKK YLDALAPLQS PHEHNETKAA
VRDFLENEGK DLQERLKKYA TGRTSYIEQF WYDSYLNYDN PVVLNLNPFF LLEDDPTPAR
NNQVTRAASL VISALCFVRA VRKEELPPDT LRGTPLCMYQ YSRLFGTARV PTENGCIIGQ
DSDSKHVVVM CRGQFYWFDV LDDNNDLIMT EKDLAINLQV IVDDAEQTPI QEAAKGAIGV
LSTENRKTWS HLRDLLTRDE GSNNAECLSI VDSALFMICL DYTEPADVSQ LCGNMLCGTS
EVERGVQVGT CTNRWYDKLQ IIVCKNGSAG INFEHTGVDG HTVLRFASDV YTDTILRFAK
SINGQAPTLW TSQSPDPSKR DPDSFGDVST TPHKLEWDMI PELQIALRFA ETRLADLINQ
NEFQTLDFAG YGKNFITSMG FSPDAFVQMA FQAAYYGLYG RVENTYEPAM TKTFFHGRTE
AIRTVTPECV DFVKTFWADN AAQKKVDALR TATQKHTSIT KESSKAQGPD RHLYALYCVW
QRKVNDESAE IGSTTGFSSN GYSSPTDMSD MGSPKRLEES SSPISRSRTG TESSRSPAPA
LQQMPALFSD AGWDKINNTI ISTSNCGNPS LRHFGFGPTS GDGFGIGYII KDDTISVCAS
SKHRQTQRFV DSLESYLHEI RRLLRATKTK DAAASKITRA REAEEKAGKD GRLKSRGRII
KTEASKVDGF QTPTSLDTAE VEDDGLGGYG FFDAGMLLQA LKKDQTKPSE QIAQRRRTVG
KKLALSEY
//
