ID A0A0D2BG06_9EURO Unreviewed; 629 AA.
AC A0A0D2BG06;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN ORFNames=PV06_11318 {ECO:0000313|EMBL:KIW36427.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW36427.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW36427.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW36427.1,
RC ECO:0000313|Proteomes:UP000053342};
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 Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable cell surface metalloreductase. May be involved in
CC iron or copper homeostasis. {ECO:0000256|ARBA:ARBA00037386}.
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. AIM14
CC subfamily. {ECO:0000256|ARBA:ARBA00038065}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847358; KIW36427.1; -; Genomic_DNA.
DR RefSeq; XP_016256643.1; XM_016412968.1.
DR AlphaFoldDB; A0A0D2BG06; -.
DR STRING; 215243.A0A0D2BG06; -.
DR GeneID; 27363392; -.
DR VEuPathDB; FungiDB:PV06_11318; -.
DR HOGENOM; CLU_023525_0_0_1; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Gene3D; 2.40.30.10; Translation factors; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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:UP000053342};
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 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 310..415
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 629 AA; 71159 MW; 101A9855D01C5F3C CRC64;
MSKSSMLKYK TNTFLTDDYE LPSRPRTVAD EEDIDPRSTT QYLGISQLGE SSSILSLPQP
SPCGSTHQLI HHLHGDVLAR ARYIDYVRAW CRIRGPELLF LAMVVSLQIA LGVWQCYEYS
THAEYQSAFG WGVAMAKGCA GALYPTLFFM LMSMSRWVQS AMTRFNIGTR FINWDKKRSF
HIRLALCVMV LSFAHSIGHL TGSFVHASQE QNHAADRQVL GNKINGLSYG AFVTSRPGWT
GIAALIIFVT ISFCSINFVR TRWFEVFQCC HLMFFPMAAL LMAHGSSALL QYPALAFVIM
VPTTLILLEK LSRAFRLTRD YRGIIEKLNE EMIRVTIDLG RRPRTWWSFV PGQFVFLQIP
RISKFEWHPF TVARISNHDL CLYVKTSGKW TRRLGEMHGF GRVCLDGPFS APTQRFFQYD
HNIMIGLGAG ITPSLGILDA LLNSPGHRWT RPQSSGVETG RSGMKSASEK NYTVDFHWAL
KTSSGMLPIF QLLYDVQNCS HNSLVDTNAI IHLTSSKKLQ QAALENMDTA RLAGAVNEIS
PSSSFSGNIE RGRPDFGKIL VQHYEKLSAL QQDHALMNGY MRSKPMKIGV FYCGAANVKP
FLRRLCLENT LRGILDHFDI EYHFHPEVF
//
