ID G1XRL8_ARTOA Unreviewed; 463 AA.
AC G1XRL8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=AOL_s00210g73 {ECO:0000313|EMBL:EGX44201.1};
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:EGX44201.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX44201.1, 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 -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:EGX44201.1}.
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DR EMBL; ADOT01000306; EGX44201.1; -; Genomic_DNA.
DR RefSeq; XP_011127177.1; XM_011128875.1.
DR AlphaFoldDB; G1XRL8; -.
DR STRING; 756982.G1XRL8; -.
DR GeneID; 22898454; -.
DR eggNOG; ENOG502SNP1; Eukaryota.
DR HOGENOM; CLU_018354_0_2_1; -.
DR InParanoid; G1XRL8; -.
DR OMA; MENLELH; -.
DR OrthoDB; 1068078at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT DOMAIN 35..206
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 463 AA; 51154 MW; D5D67F0CA9C14461 CRC64;
MENLELHSSE LKQRLLEGTT IVRREGKVIR YDESSAPNPL LTIFPRSEND VAEIVKYCRE
KGLQCFAQSG GHNWRVRNHK KIDVVICMRT LNNISIDETA QTVTLGGGTI IGELVEAVTA
KKLEVATGVC NTVGVLGTLL HGGTGRYTGK YGLGIDNLLS INIVDASGKL HQDINRVTDP
ELWWAICGAG SSFGIVTQAT IKAYPQSNDG LSWNCTMIFT DPSAPELERI LEAISKTPMD
ENMSLQCSFA CLPPTGLPSL IVMPWYYGSE SEAEKVWGRL LDPSFKPSVK NAVILPGNKV
NEGNDAICTM GGRKPGVGMG IERLDLAAFL EVWNLWTEFT KIEGAEGSAI LIERFSKAKS
LSIPDSATVF PHSHRGIAYE VVCFPIYKDE TLDIKADAFS QRIRDIWIQK CGNPEKPRCY
GACAGFDEPL EIIFGGKERV QKLMKIKKKW DSENYWGALF EIV
//
