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Database: UniProt
Entry: A0A1F5LXW9_9EURO
LinkDB: A0A1F5LXW9_9EURO
Original site: A0A1F5LXW9_9EURO 
ID   A0A1F5LXW9_9EURO        Unreviewed;       293 AA.
AC   A0A1F5LXW9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Ig-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENARI_c001G05462 {ECO:0000313|EMBL:OGE58002.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE58002.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE58002.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE58002.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT   high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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:OGE58002.1}.
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DR   EMBL; LXJU01000001; OGE58002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5LXW9; -.
DR   STRING; 1835702.A0A1F5LXW9; -.
DR   OrthoDB; 1701404at2759; -.
DR   Proteomes; UP000177622; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43008; BENZIL REDUCTASE; 1.
DR   PANTHER; PTHR43008:SF9; OXIDOREDUCTASE; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177622}.
SQ   SEQUENCE   293 AA;  31233 MW;  C7C4915352BC4EE1 CRC64;
     MAPSISLDHT TPAVVPESNE TPAAFAPAND LFSLAGRTVM ITGGGRGLGM TLTTAVLEAG
     GDVACLDLLA EPSQEEWAAV QKTAKLRGLQ ATYASCDITN EEATKKALED IAAEAMRRNK
     PLRGAITCAG IQQMVPALDY PVEGYRKMLD VNVLGTFIPA KHCARIFIEQ KTPGSIVMIA
     SMSGQIANRG LTCTAYNSSK AAVHQMCRSV AQEWGQHNIR VNTLSAGYIR TAMTDALLKE
     KPEVEETWMR GALLGRLGAP EDFKGPTIYM LTDSSAWMTG ADLRVDGGHC ASA
//
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