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Database: UniProt
Entry: A0A109FCF4_9BASI
LinkDB: A0A109FCF4_9BASI
Original site: A0A109FCF4_9BASI 
ID   A0A109FCF4_9BASI        Unreviewed;       642 AA.
AC   A0A109FCF4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acyltransferase ChoActase/COT/CPT {ECO:0000313|EMBL:KWU41891.1};
GN   ORFNames=RHOSPDRAFT_36591 {ECO:0000313|EMBL:KWU41891.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU41891.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU41891.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU41891.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-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; KQ954522; KWU41891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FCF4; -.
DR   STRING; 1305733.A0A109FCF4; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000062823; 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:SF115; CARNITINE O-ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:KWU41891.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KWU41891.1}.
FT   DOMAIN          36..620
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   642 AA;  71931 MW;  0EB768B1E09F9E35 CRC64;
     MPPVETPDWH DWRMQVPTVI PTDSVMFRNQ HKLPKLPLPK LDDTLSRLVR SCEALAERPE
     AAQQVKRKAE AFEQGPGSKL QTLLDQKRGQ PEMRNWLARD WDEQAYMAYR DSVVINVSYY
     FGFKRLPQSA QASPNAKPDP AYVAASIAAT ALEFRQLVTQ GLLEPELVGR SPEDGELCME
     SYKWAFNACR VPASPSDYAV KTREDDPAAQ CFVVVKRNRF YRIPFADEQG RPYSTEALRQ
     AIQTVIDAHA SASSSAAAPP VGILTGINRD HWAEAYGHLA AYPANIPSIR TIQQSAFVIC
     LDEAEPTEIV DFSRKLWTGE KEAGNRWWDK PLQWVVYRNG ESGFIGEHSC MDGTPTARLN
     DYLSKRLLSG ESPVRSDHEI SRVPAVKDLP FELDATSKQQ IEAAETEFAE HIKPYDVHYT
     LYTRYGKEGI KKMKTSPDGW VQMLFQMAYY LTFHRFCGTY EAAQTRRYQL GRTETVRILT
     PEVVAFVKAV VDESASTTDK LSLFRAAIAQ HGKDMKLASA GMGIDRHLFG LKMLTGKEFS
     DADRKAVMEG DGLFADPLVQ ASGTWKMSTS QIYIENAPSY GWGPVAEGGL GIPYMIHPHT
     LQLTVTCTND VPGAEFVRNF EKAADLLMDL HEAEAGQKSA RL
//
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