ID G4UH27_NEUT9 Unreviewed; 581 AA.
AC G4UH27;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative phthalate 4, 5-dioxygenase oxygenase reductase subunit {ECO:0000313|EMBL:EGZ74619.1};
GN ORFNames=NEUTE2DRAFT_148024 {ECO:0000313|EMBL:EGZ74619.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ74619.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ74619.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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DR EMBL; GL891107; EGZ74619.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UH27; -.
DR STRING; 510952.G4UH27; -.
DR eggNOG; ENOG502SEJJ; Eukaryota.
DR HOGENOM; CLU_003827_17_2_1; -.
DR OMA; QPRVTCY; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR005163; YiiM-like_3-alpha_domain.
DR PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR PANTHER; PTHR30212; UNCHARACTERIZED; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF03475; YiiM_3-alpha; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:EGZ74619.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT DOMAIN 42..189
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT DOMAIN 250..366
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 496..581
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 581 AA; 64207 MW; 95A648A72033B899 CRC64;
MTESQSKIDL YAPFERDTIL EVRASKMKKM RGLEVMSGID KTIINGPVYV GRTGLEGDES
DPTFHGGVDK AVHGYCSSHY PTWATEHPSA AAAFVPGGFG ENLVTAHMNE RNVCIGDTMI
VGSPSALTSN PESCLLLQVS LPRQPCFKLN HRFQLKKFAP LTWKHSRTGW YYRVLRPGFV
QAGDEIRLVS RPHPQWTIER IQEYLHRNQD DEAMNAELAS IEELGAESRD AFKARVARSA
AKKKRAEKLA RWRDFRVVER RQETSRILSF ILEAIDPIIP PPGDEKSILL KPGAHARVKL
GNGLVRAYSI VGPSSCSTIN RFQLGIALEP HSRGGSAYFH SHVFEGHVLS VSTTFTNALS
GNNNNNNNNS AGGISHHIYV AGGVGLTAFL TSLEQLQSIH VSCELHYAVR SNEDIPFRDR
LSQLNPGTVK IYDKTQGERL NIEEIVRQIP WNTMIYFCGP KSLMLEAARQ VKQYGVPEGE
VHFEAFEADV GGDPFEAVVA NRNDKMVLQV GGDETLLVVL QREFGDEEVE GSCCVGNCGT
CKVILKGGRV EHRGTALTAE EKGEVMLACV SRGVGRIVIE I
//
