ID G1WYJ9_ARTOA Unreviewed; 1163 AA.
AC G1WYJ9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=AOL_s00004g359 {ECO:0000313|EMBL:EGX54326.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX54326.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX54326.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EGX54326.1}.
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DR EMBL; ADOT01000005; EGX54326.1; -; Genomic_DNA.
DR RefSeq; XP_011117311.1; XM_011119009.1.
DR AlphaFoldDB; G1WYJ9; -.
DR STRING; 756982.G1WYJ9; -.
DR GeneID; 22888226; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_003662_1_0_1; -.
DR InParanoid; G1WYJ9; -.
DR OMA; MIVAVNW; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF01558; POR; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT DOMAIN 775..1006
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 127894 MW; 7DD8FAB7336D9BAA CRC64;
MASISRTPSP SPSPTFATGL RTGSFSSLQT LSRPGLQHSH SSSSSAAANL LLFNPMYLQA
PDAPAPASAG PVSITNGETS KFALSQEHRP DQPQLSILNG SAAFPFGTPH DVSKITGQAY
LTSQQLVQHV GYSLSDNVFS YSPETFDLDT AAKEWSGKSQ ANAYGRPTTI TSLETRTGAA
SVLLGYVFSN DRELSKRNIP QTVIASTATL LEMRNALEQL SMLYAVSSPF VAHVAAVDYS
PFQYNLVADY TSALQVAQDA GIGLISSRSA HDAQHMALFS TLVSSVLPTV HIYDGVRAGR
ETAKVVDVLD QAGIYQTYQS ILNEQKTIGK KVDPEAKVAK ILENLNSELG TSYKLFEYAG
HSEPEAVLVV FGSVESSVSA QVATRLAAGG EKIGVISVRV YRPFSETHFL EALPKSVKRV
AVLGQVIDQA AVDDASVQSS LYADVLAALT MAEDWTITPP VIDVKYPREQ GWVPSDFAWI
FDQIVKQKST SISPPEEALA AEASHIAGFE IFEAEAVSQY VFWDLDVSTG EEAPSSITRL
LASDSSRNVT YSSIYDNLSQ AGITYSWIRS AKETVQAHYD VTQADVVVVN DSKITLSYDV
ASGVKTSGTL LLRSPIKDED LEAKLPAQLK KALAHKKAKF YILDVPQDAG LSPEKENLLL
QLAFLRVSGE VDKVSAISEK LANIDKGVEP QTIQEVAALI DTYVREVPVP ESWLETEVIG
EPLPSSFDPN SFAINTAKSE EDPKYLLKKS IHSAIILSFR EAFELQNALR PDLPVTNFIV
RVQENKRLTP LSYDRNIFHI EFDLTGTGMT YDIGEALGIH AHNDPEEVNQ FIKFYGLEAN
DVVEVPSRDD PDQLEMRTIY QALSQNIDIF GRPPKKFYEA LSEFATDEKE KKELLTLGSA
EGAVEFKRRA EVDTVTYADV LLEFGSAHPS FHDLAKIVSP MKRREYSIAS SQQVHQNSVH
LLIVVVNWVD PKGRDRFGQA TRYLSGLKIG SEVTVSVKPS VMKLPTESTK PLIMAGLGTG
LAPFRAFVQY RAWQKEQGIP IGSVLLYMGS RHQREEYLYG EEWEAYEAAG VVTYIGKAFS
RDQPEKVYIQ DKMRQSLEKI VKAYGEEEAG SFYLCGPTWP VPDVQEVLME AIAVEATRKG
VKVDTRRRIE ELKDDGRYVL EVY
//
