ID J6F6H8_TRIAS Unreviewed; 687 AA.
AC J6F6H8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN ORFNames=A1Q1_07900 {ECO:0000313|EMBL:EJT50927.1};
OS Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT50927.1, ECO:0000313|Proteomes:UP000002748};
RN [1] {ECO:0000313|EMBL:EJT50927.1, ECO:0000313|Proteomes:UP000002748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC 7654 {ECO:0000313|Proteomes:UP000002748};
RX PubMed=23104369; DOI=10.1128/EC.00237-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Draft genome sequence of CBS 2479, the standard type strain of
RT Trichosporon asahii.";
RL Eukaryot. Cell 11:1415-1416(2012).
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 -!- 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:EJT50927.1}.
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DR EMBL; ALBS01000080; EJT50927.1; -; Genomic_DNA.
DR RefSeq; XP_014182359.1; XM_014326884.1.
DR AlphaFoldDB; J6F6H8; -.
DR GeneID; 25991412; -.
DR KEGG; tasa:A1Q1_07900; -.
DR VEuPathDB; FungiDB:A1Q1_07900; -.
DR HOGENOM; CLU_023525_0_0_1; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000002748; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 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 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 112..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..40
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 320..436
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 467..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 79068 MW; 3E37C580BADEBA40 CRC64;
MVTPLNDDEI KTFVDDLDHN NDGQIDYSEV EAKLDAAYDE LQPDENDIEA RHDRHAFLRS
IIGSDAQRIP RDQFVQRVKE WQVPSLEQEK DEERLQDEYI KKMGIGRRLR SYWAVHGPSI
LFLCIVVGMM LAFGIWQLVK YLGPAYSGAL GWGVVVAKTC AGVLYPTLFF LLLSMSRIFS
TAMRSSYHLS RFINWDLSQA FHIYMAIFAT FLGTLHGIAH LTGDFIWIAN AYRPQQLESL
LGPKPWTYRD LIRSRPGITG IIALFCFYFI GLTSTPWLRR KNYEIFQLGH LLMYVIIGCL
MAHGTAALLQ WPMLGYFLAF PTLLVLIERV HRLAAGFHSI QAQIRTLDSE TVEIKATILP
ARIFKHRYCA GQYVFLQVPE LSFFQWHPFT VSACSGNSIQ LNIKTDGNWT KRLRSLAEQG
EIRIGIDGPY GAPAQRFYDF SHTILVGSGI GFTPFSGILA DLQAREDKRH GGPDDNIEKV
TSSRRSSDKS RSRSSLFLTR TFSNKSSKSD RARNPTPPEF PDDYRRVDLH WVVRSRNHLG
WFTDLLNSVC RSQDWHEEHD GLAHPHLDIR MHTHVTQKRD LVPHVYRYLL EKHRTKENPK
SPLTGLTNET LFGRPDFEAI LDQHYEDMRR YRAQLDEDCD DRVKVGVFFC GAPKVGEILA
DRCRLLTARG REDGSRIEYY FMMEVFG
//
