ID F9F5J4_FUSOF Unreviewed; 1408 AA.
AC F9F5J4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=FOXB_01669 {ECO:0000313|EMBL:EGU87812.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU87812.1};
RN [1] {ECO:0000313|EMBL:EGU87812.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU87812.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RSE1 family.
CC {ECO:0000256|ARBA:ARBA00038266}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
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:EGU87812.1}.
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DR EMBL; AFQF01000539; EGU87812.1; -; Genomic_DNA.
DR STRING; 660025.F9F5J4; -.
DR PaxDb; 5507-FOXG_01360P0; -.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR CDD; cd08249; enoyl_reductase_like; 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; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR010730; HET.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR PANTHER; PTHR10644:SF1; SPLICING FACTOR 3B SUBUNIT 3; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF06985; HET; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00022728};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT DOMAIN 12..349
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 1408 AA; 155172 MW; 9E91EF68075412C0 CRC64;
MTTNVPGPAL YADNEGNVVV RRDLPVPTPA EGEILIEVLF SGSNPSDLRI VNYLGFRNFV
LGYDFCGRVL ETPGPNGSGL KVGDIVAGYT SYEDDQPIRW GTHQSYISRP PIGIFKVPAN
LPLPDAAALT TVVQTANDAL FHLFKLPLPS SGHGHIEGTL VVWGGGTAVG MSAIQLARAV
GITSIIVTAS ASRHGVLREL GATQCFDYHD ESVIEQVKRA VQEAGNTQVW GFDTAGTPDS
SRLLMDSLAS CQGDVQFAFV GLIVGDRPAS EMCLAVRHHK LAFDMPGAPE PYVFPAKPAE
AEKMWQATEW VVAHYGKEFR LPGLRVFEGR AEEALDHLQT VARQGTFGTP PPWKIIGTGT
HVQPEVMSPE TWDMIRGWVG DCINDHEDCK VVSEDRPFPT RVVAVGGEDT EPHLFIPSSD
DRGRYIALNF ARFPKTFQDA IIVCRKLNIK YLWIESLCII QDDEHDWAVE SPKMCDVYQN
AYLTIAAAAA HNSSEGLFHP RPFSVQKMFP TASRNDDKVE EVEIFARPWT LETDYSESDQ
DSSGQVSAHV ELVYYELDLG LNRVVRKWSE TVDPTASLLS QVLGGDDGPG SVLVFAEESI
TYHHLNQDPL RVPIPRRRGA TEDLPRKRTI IGGVMHKLKN TADAFFFLLQ TEDGDLLKLT
FDMHDSEGSL AGEVRRIKIK YFDTVPVASS LCILKTGFLF VAAEFGNHHF YQIEKLGEDD
DAEPVITSDD FSTGPRGAYQ PVYFDPRPLK NLALLESIDS LSPLLDCEVA DPTGEGPPQI
YSESGNGARS HFWMLKHGLE INKVASSDLP GTVSGVWTTR MTRHDKFDSY IILTSSDGTV
VMSVGDEVEQ VSDSGFLTTV TTLAIQQIGD DGIVQIHSKG IRHLRAGQIN EWPAPQHRSI
VAVTTNKRQI AIALSSGEIV YFEVDSDGSL AEYDETKVIS TTVTCLSLGP VPEGRLRSPL
LVVGCEDCTV RILGLNPDSM LESNSIKTLT AVPSALIIMA MEHPLTSSSG LCLHIGLSSG
VYLRTGMNEI TGELSDTQTR FLGLKAIKLF QVTVKGQTCV LALGSKPWMG YIDPKRGFTM
TPLECEELHW ASSFSSEQCQ EGIIAIHANF LHIFSVENLH NNVVRKSIPL TYTPRHFVKH
PAEPYFYTIE VDNNTLSPEL RAQLLAVDDH GDDKVLPPEL FGYPRGNGRW ASCISIIDPI
GEQVLQRIDL EGNEAAISIA VAPFTSQDGE IFLLVGTGKD MILNPRQSSG GYIHVYRFHQ
NGRELQFIHK TKVEEPPMAL VAFRDRLAVG LGKDLCIYDL GLKQLLRKAH IEAAPQLIVS
LDTQGDRIVV GDVQQGMTMV MFNHEEQRLI PFVDDIIARW TTCTTMVDYE SVVGGDKFGN
IWIVRCPKKT SHHVGDYARN YLNGAKPI
//
