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Database: UniProt
Entry: F8NS50_SERL9
LinkDB: F8NS50_SERL9
Original site: F8NS50_SERL9 
ID   F8NS50_SERL9            Unreviewed;       357 AA.
AC   F8NS50;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=SERLADRAFT_464454 {ECO:0000313|EMBL:EGO26883.1};
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1] {ECO:0000313|EMBL:EGO26883.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S7.9 {ECO:0000313|EMBL:EGO26883.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA   Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA   Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA   Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA   Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA   Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "Evolution of plant cell wall degrading machinery underlies the functional
RT   diversity of forest fungi.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL945432; EGO26883.1; -; Genomic_DNA.
DR   RefSeq; XP_007317056.1; XM_007316994.1.
DR   AlphaFoldDB; F8NS50; -.
DR   GeneID; 18818743; -.
DR   KEGG; sla:SERLADRAFT_464454; -.
DR   HOGENOM; CLU_026673_29_2_1; -.
DR   OrthoDB; 179761at2759; -.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05288; PGDH; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR041694; ADH_N_2.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR045010; MDR_fam.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43205:SF19; AGL360WP; 1.
DR   PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR   Pfam; PF16884; ADH_N_2; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          24..352
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   357 AA;  38697 MW;  CB880A87A7372829 CRC64;
     MSHLPTTTKA WILQNPPVKN IILGNSESST FSIQEQTLPP LDKGDLLVQP IYLSNDPAQR
     GWIQRKLDEG RLYVTPVLQG QAMATHAVAR VLATAGPTST WKEGDLVYTT TTGWRQYAVV
     KEEDVRSLRS IPGLSPSLYV GLFGVPGLTA YFGVTEVLKL QRGQSLVVSA AAGAVGNVVV
     QYAKKVIGAS KVIAIAGTPE KCAWIKEMGA DIALNYKAPS FKQDLNAATE GFVDAYFDNV
     GGEILDQMLT RIKQHGRVAA CGAISNYTHD NLDAANLRNW FEIITSRLTV KGFIVLDYFP
     RAGEAVEALS KAVEEGKMTV EGAETLVETD FSNIPEVWLR LFQGQNVGKL VTQIAGA
//
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