ID A0A1X7S4E0_ZYMTR Unreviewed; 708 AA.
AC A0A1X7S4E0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=ZT3D7_G9660 {ECO:0000313|EMBL:SMQ54505.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ54505.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ54505.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; LT853701; SMQ54505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7S4E0; -.
DR STRING; 1276538.A0A1X7S4E0; -.
DR Proteomes; UP000215127; Chromosome 10.
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:SF12; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14340)-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; 2.
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:UP000215127};
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 49..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..555
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 483..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 79225 MW; A90A616395C23EC7 CRC64;
MAPRDADALP DAMPIPRPVV TDFGDALNLT AAASPFSHGL NGVDQYMNYL FANAIVGSFL
ALLGLTLIYR WIKMGNAHMR HLFTMNRDSD QRYFMHNHGD FWPKVKRSIL YAPLWKNRHN
KEIQITQAVT IGTLPSRFHT VLLLAYVLSN IAYCLALDWT KPDYEVVAEL RGRTGVLAAL
NLIPTVLFAL RNNPLISILK VSYDTFNLLH RWCARIMVFE SIIHTIMWAV NAVKAGGYDQ
ISISLSTSMS YTWGMVGTGL FTFMALSAFG PLRHAAYETF INSHRLMVLV SIIAVYLHLD
LANLPMLPYV QLSLAFWAAE VVWRIGRILY HNASRKRGLT KVTVEWLPND ACRVTFELSR
PWKWRPGCHV HAYIPTLALW SSHPFSIAWA ENRSQGAPME IEMEKFDKMP ASSTGIFDPA
AAQRNSHFGA RSSVFASPLR NSVVAPRTSV FAQPVRSSNY MSPIVESPTS SIHKLPKLAP
TTTLTQTTSH ASSNHDHPTP DLTLPRDANV TSLSLVIRAR TGMTRHMYNR VAASPTRSFT
TWGAIEGPYG GHESLSSYGT VILFAGGVGI THCIGYIRHL LLQYQAGTTS TRKILLVWSV
PTTESLEWVR AWMDTILRME CRREVLRIQL FVTKPRHRGE VVSSTGSVQM FPGRCNPTTI
LKREVPERIG AMGVTVCGPG AFADNVRAAC RSVVREVQLD FVEEAYTY
//
