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Database: UniProt/TrEMBL
Entry: M2T5E8_COCSN
LinkDB: M2T5E8_COCSN
Original site: M2T5E8_COCSN 
ID   M2T5E8_COCSN            Unreviewed;       959 AA.
AC   M2T5E8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   03-MAY-2023, entry version 43.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=COCSADRAFT_199855 {ECO:0000313|EMBL:EMD64471.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD64471.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD64471.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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DR   EMBL; KB445643; EMD64471.1; -; Genomic_DNA.
DR   RefSeq; XP_007700246.1; XM_007702056.1.
DR   AlphaFoldDB; M2T5E8; -.
DR   STRING; 665912.M2T5E8; -.
DR   GeneID; 19134112; -.
DR   KEGG; bsc:COCSADRAFT_199855; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   HOGENOM; CLU_012921_0_0_1; -.
DR   OMA; FANNGYR; -.
DR   OrthoDB; 5487555at2759; -.
DR   Proteomes; UP000016934; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08267; MDR1; 1.
DR   CDD; cd07389; MPP_PhoD; 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   Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR   Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR018946; PhoD-like_MPP.
DR   InterPro; IPR038607; PhoD-like_sf.
DR   InterPro; IPR032093; PhoD_N.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43606; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   PANTHER; PTHR43606:SF2; PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G08710)-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF09423; PhoD; 1.
DR   Pfam; PF16655; PhoD_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..959
FT                   /note="Enoyl reductase (ER) domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004026249"
FT   DOMAIN          629..943
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   959 AA;  105466 MW;  BBBEDC5785818503 CRC64;
     MLSVLFAAVP LASLVCASFD GNLNYDSPSR RHNDLGIDVP KVAKRTLSKR SAPLDPAQLN
     FTHGVASGDP YPDSVILWTR IAPSLEHDRS NVTVSGYVAL YNHETEKYIQ ASPNPICVDY
     RVGTDSDFST VVDEGQAYTT SDIDYTVKVE AKNLEPFTQY YYQFSVCGSS NKSPLGRTKT
     SPDHDDEVSK VGLAVFSCSN WQNGYFNAYG NAARKDQVDF FVHLGDYIYE STKGKLGKDP
     RATNPPREIV TLYDYRARIG QYRTDDDLKL AHQNFAWIPT WDDHEIANNG YRDGFSNMNN
     TEESFLKYGG ISVDSRKMNA VRAYFEWMPI RQVDLDDNLR IWRNFKMGKL FDLIILDTRN
     YDRSITTLNE NDDYIAEIRD DASRSLMGSR QENWFYNRLS ESHERGATWR IVGNQIIFSR
     MNNSAVYSDW LNADQWDGYT ANRNRTLHHL YSNKIPNTAF LAGDSHANWV SDLVWLDETP
     YDQATGEGAI GVEFAGTAVS SSGYGSGRSI ANSSDRSAAL VRDNRELQWT EGYYRGYYEL
     FISPEELNAQ YYGSPSVASR NPFDISLANF TVKAGANHLA RTNGSVVAAG GYVESGALQR
     GPTTPTNLTL NTVTGTWNIT GIEQITNGGI EKNLRINESA PLPFLHDEQI LVQVHAMALN
     PVDYKVTEGP MPLRLVGSNI TPGADFCGTV AKVGRKVDEF QIGEFVFGAK VGALTGGTLA
     QYVVVERTML AVLPEGVKVE EAAGVGIVGL TEYQALVPNV KSGDKVFING GSGGTGVFGI
     QIAKALGCHV TTSCSTPNIE FCKSLGADEV IDYKTTDIVE ALSAKGQVFS TVVDNVGAPD
     SLYKASSAFL LPEGKFVQVG MQPSLGGTKT LVGNMLLPSF LGGGKNSFQM IMAKPSAEQL
     RHMGKWLKQG SLKPIVDTVF EWEDAPKAFE KLKTGRAKGK IVIKVPQDRA KDKAADESS
//
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