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Database: UniProt
Entry: A0A1V6T934_9EURO
LinkDB: A0A1V6T934_9EURO
Original site: A0A1V6T934_9EURO 
ID   A0A1V6T934_9EURO        Unreviewed;       409 AA.
AC   A0A1V6T934;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Serine aminopeptidase S33 domain-containing protein {ECO:0000259|Pfam:PF12146};
GN   ORFNames=PENSTE_c010G04651 {ECO:0000313|EMBL:OQE22504.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE22504.1, 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:OQE22504.1}.
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DR   EMBL; MLKD01000010; OQE22504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6T934; -.
DR   STRING; 303698.A0A1V6T934; -.
DR   OrthoDB; 2403795at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR022742; Hydrolase_4.
DR   PANTHER; PTHR43139:SF5; MESODERM-SPECIFIC TRANSCRIPT PROTEIN; 1.
DR   PANTHER; PTHR43139; SI:DKEY-122A22.2; 1.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..223
FT                   /note="Serine aminopeptidase S33"
FT                   /evidence="ECO:0000259|Pfam:PF12146"
SQ   SEQUENCE   409 AA;  44418 MW;  7ED2B146639F7EF8 CRC64;
     MALYHQTVDF LSDSWANQRT QLPLLAVSGA SFTLGLLIRS LLNGRESTQT VLPSPRARIS
     NDVAEDEKHN HPLPNDVLPG ARDVASPYGS IRVYEWGRED GPKVLLVHGI TTPCIALGGV
     AHALVDRGCR VMLFDLFGRG YSDCPADLPQ DNRLFATQIL LALASSPIAW TGKESGKFCL
     AGYSLGGGIA AGFASYFPQM LSSLVLLAPA GLVRDSQISF QSRLLYSRGL MPENLLGYLV
     GRRLRAGPLV TPKKSNHKKL NAADALTEEL PSQDAAEIQL LSREYPYVNI PSAVSWQVNH
     HSGFVHAFMS SMRHGPILGQ RQWTTWARLG EYLSAQNSIS PSSEGEKGLP CDKVHILCGN
     TDGIIIKDEL VTDATAALGG NAAFKFYDAG HEFPSTKYED VAAYIQKLL
//
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