ID A0A367YAX1_9ASCO Unreviewed; 695 AA.
AC A0A367YAX1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Putative ferric reductase transmembrane component {ECO:0000313|EMBL:RCK62988.1};
GN Name=CFL1_30 {ECO:0000313|EMBL:RCK62988.1};
GN ORFNames=Cantr_09761 {ECO:0000313|EMBL:RCK62988.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK62988.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK62988.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK62988.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-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:RCK62988.1}.
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DR EMBL; QLNQ01000024; RCK62988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367YAX1; -.
DR STRING; 5486.A0A367YAX1; -.
DR Proteomes; UP000253472; 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:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-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.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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:UP000253472};
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:ARBA00022448}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 421..526
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 695 AA; 80205 MW; 12119D91143FF65E CRC64;
MIFATIYIVF VYFVAFVAAL GGKLTIMGEG LVYWACDYQL DDVATFECEE LKYTACTCSN
KNSLASIAGC MAYNNRNTTS VIKAATDICY DFGNITLKDG WFEESYQYYL DNAVWPSDIP
DFNKSEPFDL PVKFNGTYIE LYYSAYDHWF GNLDNSFYYG AGALGYWLLV MFLEGVVNWS
KILFPGLVKK LTFAPITWWR AYVSMPATFR KRKAQEFPIL KIFDCLIPSR YESLVILGFY
AYIIAVHCIK LHYVKEVPIY ESVSQFRLKN IGDRTGIIAT VMMPLVFLFG GRNNILQWLT
GMSYNQFMTY HRHIARVMVA LVIIHSVNYT VFLKSFYAEE AEEPWFYWGI IGTLAGGLIL
FQAMLYFRRR WYEMFLLIHI TMAALYIVGT WIHVDIFGYV YFCYGTIAPW CFDRLVRIIR
MFWFGFPKAQ ITLISNETIK VVIPKPRYWY SIPGGHAYIS FFRLSCFWQN HPFTFVDAPT
DKNIVMYCKV KGGMTHGLYQ YLAKQPNQTA SIRVGVEGPY GEPTAARYAD SAVFIASGNG
IPGLYSEVMY GARKLLSTSK RVMKLIWIIR EYSALAWFQE ELESLKDTNI QTTIYVTRPV
LNLHSDEDKK IEAKDSTDDD SESIKSRLAH IEFIEGRPSI EEMVVDEINE SSGSVAFVTC
GHPAMVDEVR YFTAHNLRNP DHKRVDFYEQ LQVWA
//