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Database: UniProt
Entry: S3DX89_GLAL2
LinkDB: S3DX89_GLAL2
Original site: S3DX89_GLAL2 
ID   S3DX89_GLAL2            Unreviewed;       823 AA.
AC   S3DX89;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=CoA-dependent acyltransferase {ECO:0000313|EMBL:EPE36576.1};
GN   ORFNames=GLAREA_08739 {ECO:0000313|EMBL:EPE36576.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE36576.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE36576.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; KE145352; EPE36576.1; -; Genomic_DNA.
DR   RefSeq; XP_008075891.1; XM_008077700.1.
DR   AlphaFoldDB; S3DX89; -.
DR   STRING; 1116229.S3DX89; -.
DR   GeneID; 19467787; -.
DR   KEGG; glz:GLAREA_08739; -.
DR   eggNOG; KOG3719; Eukaryota.
DR   HOGENOM; CLU_013513_4_0_1; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000016922; 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   ECO:0000313|EMBL:EPE36576.1};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   Transferase {ECO:0000313|EMBL:EPE36576.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          77..720
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        383
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   823 AA;  91091 MW;  17D58C8BFFBC18FE CRC64;
     MPTSTTAVRT FTMPKSLNES LAQPGQPQKA SENGRSHEKV KKVSESFTKE QKDPLASNQP
     NYKQGITFAA QDKLPKLPIP ELEQSMTRYL AALKPLQSPR EHAESTQAVE EFLKSEGPEL
     QERLKKYATG KTSYIEQFWY DSYLNFDNPV VLNLNPFFLL EDDPTPARNN QVTRAASLVV
     SALSFVRAVR REELPPDTIR GTPLCMYQYS RLFGTARVPT ENGCHIGQDP EAKHIVVLCH
     GQFYWFDVLD DNSDLIMTEK DVSINLQTIV DDAQKTPIQD AAKGALGVLS TENRKIWSGL
     RDVMTRDEGS NNADCLGIVD SALFILCLDY TEPASGADLC QNMLCGTSQI EKGVQVGTCT
     NRWYDKLQII VCKNGSAGIN FEHTGVDGHT VLRFASDLYT DTILRFARTI NGQAPSLWAS
     TSPDPSKRDP ASFGDVNTTP HKLEWDMVPE LGIALRFAET RLADLIQQNE FQTLDFNHYG
     KNFMTSMGFS PDAFVQMAFQ AAYYGLYGRV ECTYEPAMTK MFLHGRTEAI RSVTPASVDF
     VQTFWGEVPP QQKVDALKKA CQEHTANTRE CAKAQGCDRH MYALFSVWQR GVDDDGAEAA
     SSNGLSSNGY SSPIEGSVVG SPPRSTDLTE ALSTHSRNNS SSSPRRHRAP PHIFQDAGWD
     KLNNTILSTS NCGNPSLRHF GFGPTSGDGF GIGYIIKDEG ISICASSKHR QTKRFVDALE
     SYLLEIRRIL RSTQRRGTSP KASRAREASA RPKAGSRLKS RGRVIKATGM EKEIVQDSTS
     NTASDDEGLG GCKYSLRATP VFMCRFEVVI GTDELVFAAD GFF
//
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