ID A0A3E2HIT8_SCYLI Unreviewed; 1179 AA.
AC A0A3E2HIT8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
DE Flags: Fragment;
GN ORFNames=B7463_g3217 {ECO:0000313|EMBL:RFU33083.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU33083.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU33083.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU33083.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) 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}.
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:RFU33083.1}.
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DR EMBL; NCSJ02000041; RFU33083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HIT8; -.
DR STRING; 5539.A0A3E2HIT8; -.
DR Proteomes; UP000258309; 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 InterPro; IPR029526; PGBD.
DR PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF13843; DDE_Tnp_1_7; 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 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000258309};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1179
FT /note="FAD-binding FR-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017743039"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 403..566
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 488..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU33083.1"
FT NON_TER 1179
FT /evidence="ECO:0000313|EMBL:RFU33083.1"
SQ SEQUENCE 1179 AA; 133206 MW; 01EF0057659C708E CRC64;
MHLRYCLSVL ATASTIWPAS IAAARASSGL RDAPCFEACQ MTLRQVRFTD LDGAGANRRI
QACQSRLALT SLYLCSSVYC SVGERTAGLD AQNSTCRETV GLSILPFDII ANYTEGDIAQ
LRRLSRDNYV APIELAELAI PSEKFFDLAH DTLVSRITAV PSMLVQFAHE VMRHPGPGMF
FFWSVVVVIG LLNRIIVALG HRSTPQRRGW RSLPLSEPEE DIDSIPDKKS TLSSRPYVWL
KRFVTVPATF GYRNAQPFGC WPKVSTQIWR YLSDRTGIIS FANFPLIWLF GMRNNALIWL
TGWDFKTYSN FHRWVARVST VQAVIHSVGY TVLVVDRGGW HNFANYWVEM WWTTGELVCT
LSLSLLEKCN YTGLTEDASH VSIFKARYDG IAWICCIIWA LDRTSRMWRT LAFNRIFWNT
MAYAIYDPDA NIVRLSIPSS TSLYRPKPGT FYYIHWLNDS RFWESHPFTV ASVRDSDDYS
QSLLQDRSQQ LDLTEESSSL LPREGGDGTE VSRDRRSRGS APEIRFLIRP YDSFTRRLRE
AASRTDQKPV RFRVLVEGPY GHTLPFHRFD NIVFIVGGTG IVVPLSYLDV LCKSTSKTKA
VRIIWVVREA AFAAFVLLQD FGGLLENNNL SVDVYITGDE VVASRLGQEI KDVRVLHGRP
HIHGEVEDAI RDFPDQGSLA VVACGPAKMA DDARRAVKFT MVAPTNAVPD STDLGTLRPN
FEPVVEVGET FTPLICPEFN HKINLPPNIK PNDPLGIFTL FFSRPVVKEL VENTNKSYQE
ALGKGTVKES YPKWAPLTVE ELYLYLGIRV YMSLTVLKQL KYYWNTDPEK HCGLHYAITS
RMSRRRFEAI TRWFRVAPTT SKSTVFERLE PLNGHIQSMS RQLWIPGRDL AVDECMVRFQ
GRSYDTLKIP SKPIPEGKGP HFDHGHQPPR KMGLNPTAAV VPYLVQKVQR PPDPCVEYQH
ILWLDNLFMS VKLAKYLERL KIGCTGTART NSGIWSKLVQ KKKDDKKHDT IPWGTVIEKP
TVDGKVNMMA WKDNALVLML TSTSTSAKTA LKVFGNQPQK ELPIPIAIDL YNHHMNSVDL
GDQLRACNSG ARVIRRGGWQ ALFHFLFHTV LVNSWLLSKH GGGGFKGPEA FREALYKALF
TVGSKSPGKG KRPISQLISE EIDGPATSSG HRLQNFVKS
//
