ID A0A0D2GHB8_9EURO Unreviewed; 613 AA.
AC A0A0D2GHB8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Unplaced genomic scaffold supercont1.4, whole genome shotgun sequence {ECO:0000313|EMBL:KIW80188.1};
GN ORFNames=Z517_06803 {ECO:0000313|EMBL:KIW80188.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW80188.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW80188.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW80188.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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; KN846972; KIW80188.1; -; Genomic_DNA.
DR RefSeq; XP_013283996.1; XM_013428542.1.
DR AlphaFoldDB; A0A0D2GHB8; -.
DR STRING; 1442368.A0A0D2GHB8; -.
DR GeneID; 25306293; -.
DR VEuPathDB; FungiDB:Z517_06803; -.
DR HOGENOM; CLU_010365_3_1_1; -.
DR OrthoDB; 2787294at2759; -.
DR Proteomes; UP000053029; 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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR32361:SF24; REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G10820)-RELATED; 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.
DR PROSITE; PS51384; FAD_FR; 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:UP000053029};
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 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 316..459
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 67970 MW; 11BBC832B0B285CE CRC64;
MAGSTSANST TPSSSSGHAE QNPETEKYLQ ALNHSLSTNY LYALVVLTAL VFAYHSAIRL
HRHARHLVSL GGNTRSQRYF SLVSPTIAWL KVHLVYAPLL YHRRAEEIKC GSRLILGTIP
TRFNTLFITS IIVYNVFACV YNIPWSSPEL EVLPILRNRT GTLATANLIP ICVLATIKNP
LINALDISYD SFNLVHRWLG RLSILQGVAH TICWMIAKVQ KSGWAAVQKS LTHSSFIMTG
LIATVGFVAL GLHSSKVFRS LAYEFFLHSH ILLVAMTFGG LWVHLEGLPQ QRFLMAAIVI
WVGCRLWRLC TLIYRSCGRG GTYATIEPLP RGSVRVSVTC VRPWKVRPGQ TLYLSIPSIG
WLTLHPFSVA WAESDRETSL NRWDSTNSKH SEYSDKTRLV GTVRAAKEGA PEPRSRTIDL
IIKRKTGFTS TLLTRAHQGG GRLVLPAFVE GPYGHETSLA SFGTLLLFAT GVGITHHMMY
IRSLVQGYTD GTVATQHITL VWAVPNCECL DWVREWMHEI LNMENRRDVL TVVIHVTRAS
MNQDVRSPSS RVKMVRGRPN VMSIVQRAAD DRVGCLGISV CGSGGLADEV RAATRVVIGQ
GVNASLMEEG FGW
//
