ID A0A0F4GK76_9PEZI Unreviewed; 732 AA.
AC A0A0F4GK76;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=FRE family ferric-chelate reductase like protein {ECO:0000313|EMBL:KJX97806.1};
GN ORFNames=TI39_contig459g00034 {ECO:0000313|EMBL:KJX97806.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX97806.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX97806.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX97806.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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}.
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:KJX97806.1}.
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DR EMBL; LAFY01000451; KJX97806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GK76; -.
DR STRING; 1047168.A0A0F4GK76; -.
DR OrthoDB; 2049651at2759; -.
DR Proteomes; UP000033647; 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:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 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 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:UP000033647};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..732
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002468774"
FT TRANSMEM 154..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 269..384
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
FT DOMAIN 585..712
FT /note="Ferric reductase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF08030"
SQ SEQUENCE 732 AA; 82527 MW; 8E55EAC90D114D63 CRC64;
MAGRAGLVAL LLLSSSPLSR AHTLPYVQES EYCAVSCAAV IGRVTFNGSK PENPPCSSNI
AVTSLFACTS KYCATPDEAQ YGLDYINWTC SHEGKPSLPE YYAIQLPIPD HISTVSAAQI
KKVHYNQTVI PTEDYYRLVY RSTDAKYKAS YYDWMFVFAI YGYWILVLLI GVLFHIVSSS
KAATSAISKS SLWKRAYCLL ILPRMGPDRL GGHCTSNALT RLVTLPLIIH AVLCFVLLFP
AYDTAPGPDD FYYGTVKIER GKYVANRIGT FTAAHIPIVW IFAARNNPFQ WLTGWSYATF
SQYHRWLART MTLLAVSHGV SYSVVDWYKN TYLTVWDDLY WRCGVLSVIT ICTLFVMALP
WVRSRSYEVF LVFHIALAAV LLAGLYYHWN ELTERRAYHG FLWPAVAMWS LDRFLRFSRL
MYLNIRPMLS NGVMALVSRD QESELVRVDV TNFFSTQTTT STPGHYYFVY EIGRWQGYQS
HPFTLCSWIS GADSSALRKE ADETKSPGFE VIDEVAKDAS QTGAKAREVR HTFLIRPRQG
VTQRLLSRAF SASNNEDEER QKLTRRARFL LEGPYGQVQY TPRHSSVLLL VGGSGISAMI
SRLHILLDSF DDAEKSIHLV WSVRMKGTAD DVCAHELSSI VGRPGFRLTV HLTTGSDNEK
VDEMSAHALY ELRKGRPDVK AVIENERAKC SDGLTVFCCG PQSLELDCRK AVQSVLHEDG
ADVSFCSEQF GW
//
