ID A0A061HBF9_9BASI Unreviewed; 1271 AA.
AC A0A061HBF9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=PFL1_02482 {ECO:0000313|EMBL:EPQ29809.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ29809.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ29809.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ29809.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KE361629; EPQ29809.1; -; Genomic_DNA.
DR RefSeq; XP_007878190.1; XM_007879999.1.
DR AlphaFoldDB; A0A061HBF9; -.
DR GeneID; 19316602; -.
DR KEGG; pfp:PFL1_02482; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_003662_0_0_1; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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 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:UP000053664}.
FT DOMAIN 827..1058
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 65..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 134247 MW; 97202EFBCEE4D99E CRC64;
MAATHQSLYQ SAAIFAGGLA IGAGAFALSR NAFAPAHKPT KAIKRKLSDA ANAATNKAKA
AAIAPAANDD KAAASPAPVA PASNNDKQAK ETLDAAAAAL EAAPGRVDPP LAQVLDAVDQ
KGPGPVQPAK PQAEGNVAPS GPDATAGGQK LKGLVNEQPK LDAEPEPSPL NRVSHLDTRA
DLSLVSGPSA DELAKHAAAQ AWLTGIPSPN TTSTGVIDAI AYANSTAVFS YESEANGGFG
AHSEAQAAEA LDKGWTQGRP KVFKMQTRSG AGNAIVGYLS GAKKGSSSSG PTRVVTALTN
AAGFVAMAPT LAALDDVATD AGKIVLQVSA ASQSTDDDLA IKNDYAAVLA ATAALGDAFE
VVFSSTRQEA VDSAQYAYQS AKNVVHVFDG AFAGREVGLL SVPQKGAAVA APEHFHYTGP
AKATAVLVVP NGSHSQSARA VLVTLPPAVR HNIGVLSVKV VRPWSDAELR KAIPETVQSL
HVLEEIPSGS TSGLVYEDVM GSLFSDAFLG AGSAPRNVFS VALEAGQNLV AAEWFELLKT
VAASPAAPVK LGDVFDAATQ QPDLLALSGA SLASGLVRSD LILTGRPESA SDAPIELVGD
DNSSKVLVVS DPAVTLKSLA PFQSLVRGGT VIVNVPGWDA AELESKLRAE DKKVLADKGA
RLLLVDAAAV VEQLNTKTAN ARGGKAKAGD DVVPKEIAAA VLLVAFLRTQ LDLGGDALAA
FVTRILGTAP VGVDGVAGLV QATEAAVERF AFSNAEWANA EPLEGESASA PRPTHIRYNG
FTRSADAALA GVEVAPSRNT WALPAWQQLF SEAYETDTSA IRPDLPEKTW VIEVTENRRL
TPVDYDRNVF HMELSTKGTD LRYEVGEALG VHGWNDDDEV ADFIRWAGFD ADEVVSVPSL
AKPAKFETRT VFQVLQQNLD IFGKPPKRFY EALSKIATNR DEARWLRFIS SAEGSATFKK
YSEVETLTYA DVLRMFPSAR LPLDLLLTEV EPIKPRHYSI ASAQAAVGES VHLLVVTVDW
KTPSGSPRYG QCTRYLSKLK PGAKVTVSLK PSVMKLPPID SQPIIMAGLG TGAAPFRAFI
QARAVKRAQG IDVGPLVYYF GSRYRSAEYL YGEELEAYLQ DGVLSHVGLA FSRDTSKKVY
IQHKIQQDGE MLTNYLAPEI EALKKLGGSA EVAIRDGALD DHVDEGKKGY FFVCGPTWPV
PDIHEAIVSA FVERGWTQER AEQRIEELKE EEMDFGGVLM ALSVVDDADD GDENEDLTIA
TISGRAWWCR R
//
