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Database: UniProt
Entry: A0A1V6T2U9_9EURO
LinkDB: A0A1V6T2U9_9EURO
Original site: A0A1V6T2U9_9EURO 
ID   A0A1V6T2U9_9EURO        Unreviewed;       459 AA.
AC   A0A1V6T2U9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Acyltransferase 3 domain-containing protein {ECO:0000259|Pfam:PF01757};
GN   ORFNames=PENSTE_c013G09043 {ECO:0000313|EMBL:OQE20461.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE20461.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE20461.1}.
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DR   EMBL; MLKD01000013; OQE20461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6T2U9; -.
DR   STRING; 303698.A0A1V6T2U9; -.
DR   OrthoDB; 1824368at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR23028:SF53; O-ACYLTRANSFERASE HOMOLOG; 1.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        284..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        418..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..430
FT                   /note="Acyltransferase 3"
FT                   /evidence="ECO:0000259|Pfam:PF01757"
SQ   SEQUENCE   459 AA;  53294 MW;  029012F702E3F780 CRC64;
     MERTTWLDGL RGIAAAIVAF DHYFMSDVWH PFVSFWTEPP EYNRHIVQLP PIRILFSAHG
     MVTLFMVISG YAISISLLKA RDGPQFIQRM SSAIVRRVFR IYLPVIITAS IAQIFYFFDL
     YHWEFDQGLI DDLPKPWSNP WAHFCWLMNY MAESINVVAS EYRGGLNGQL WTMPLEFRGS
     NIVYLLIIGL SGWRRKVRLI VLPILGAFFI WWGNWDVFGF IWGLWLAEKA HGVDNSRENF
     DINTELEMAE FESTSSSSIS LSERLGLCSG KRRYKPLRLN SSKLFILSRV GIALVFVAGY
     YLLCLGNDGH LPPGYQFLNY IQSPRWKDRW HIYHFCWKEL GSAMVVYAIS EFRFLQRPLN
     TRIVQYLGKV SFALYLLHET IYQLFRNPLR DFIYSSLSGN VYEASGQAWS ADPFSFHVAW
     WVSGIFLGSL SVLAAHGYTK YVDDRCVAFS KRIDQWLSI
//
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