ID A0A1B9FV84_9TREE Unreviewed; 575 AA.
AC A0A1B9FV84;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=I302_08319 {ECO:0000313|EMBL:OCF22668.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF22668.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF22668.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF22668.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000256|ARBA:ARBA00006278}.
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DR EMBL; KI894025; OCF22668.1; -; Genomic_DNA.
DR RefSeq; XP_019043738.1; XM_019194902.1.
DR AlphaFoldDB; A0A1B9FV84; -.
DR STRING; 1296100.A0A1B9FV84; -.
DR GeneID; 30212718; -.
DR VEuPathDB; FungiDB:I302_08319; -.
DR OrthoDB; 1776577at2759; -.
DR Proteomes; UP000092730; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
DR GO; GO:0000041; P:transition metal ion transport; IEA:UniProt.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR32361:SF23; FERRIC-CHELATE REDUCTASE-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092730};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 39..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 146..261
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
FT DOMAIN 325..396
FT /note="FAD-binding 8"
FT /evidence="ECO:0000259|Pfam:PF08022"
FT DOMAIN 405..562
FT /note="Ferric reductase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF08030"
FT REGION 481..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63843 MW; FA743D21F6CBCE35 CRC64;
MDAGVTPGQI DSQGRYVPTS AERTAYQAAR IPWADQVVYG YYTLAFLCGI LALYAILYGL
WKLRIRYRYG IRSKAYIKLS AISRLLTYPQ LPHRGWVSYI WTFGPLGPNI LLGAGLIFAT
GFTFINEYYY YPPFYGSAPL YLRSEWIAMA TLPFVYVLGS KRNLISILTG ISHEKLQVLH
QGSAFNFTYM SLVHTVAACI RAIRERGMKG TLAVNQVYVS GFVALAPLLV LFAGALPPFR
KSFYELFYWI HITMAVFFAG AMFWHGYKTL DSDAYMITTL VLFLSSATTR LILIILNNPT
LHSAHVELLD EDTLKITIST IYINWSDSHP FTIANAPPLA QQTQSSDIEK TDRSMATREM
IFLLKPLSGF TRTLFNQVQN GQTKYKVLID GPYGDANVGG DLRGFDKILI VAGGTGITWA
LSVLQDLVGN REGRGGMGRE VVLVWAVKRI SSMKWFENEL QAIRTHHPNV SIEHYITEES
IDDFSRPSPP ESGPSSADGH GEDDTPSTEK GLQLSIKAKA DCHRGRPDLP YLIERTVAST
HGFLAVATCG PPAFLTDCAN AVTKAQIGIL TDPHG
//
