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Database: UniProt
Entry: A0A1E3HG96_9TREE
LinkDB: A0A1E3HG96_9TREE
Original site: A0A1E3HG96_9TREE 
ID   A0A1E3HG96_9TREE        Unreviewed;       616 AA.
AC   A0A1E3HG96;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN   ORFNames=L202_06542 {ECO:0000313|EMBL:ODN75383.1};
OS   Cryptococcus amylolentus CBS 6039.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN75383.1, ECO:0000313|Proteomes:UP000094065};
RN   [1] {ECO:0000313|EMBL:ODN75383.1, ECO:0000313|Proteomes:UP000094065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN75383.1,
RC   ECO:0000313|Proteomes:UP000094065};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) 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   -!- 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:ODN75383.1}.
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DR   EMBL; AWGJ01000010; ODN75383.1; -; Genomic_DNA.
DR   RefSeq; XP_018991033.1; XM_019141058.1.
DR   AlphaFoldDB; A0A1E3HG96; -.
DR   STRING; 1295533.A0A1E3HG96; -.
DR   GeneID; 30157851; -.
DR   OrthoDB; 367877at2759; -.
DR   Proteomes; UP000094065; 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; IPR000778; Cyt_b245_heavy_chain.
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   PRINTS; PR00466; GP91PHOX.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 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:UP000094065};
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        86..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        217..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          299..426
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  70363 MW;  FE3D7CA721D241C9 CRC64;
     MPPKVRMARA SNLSFDSGPP PQYNPDVPVA NGPTFLQRNK TERTRLQGLV STMSNLKPNP
     EGKVARAVGM GEKLKVWMVN EGGRRIFFFT WLFVHALAFA FAVVNYSLKD SFTGARATFQ
     WTYPAARGAA QVLHIDIIFI LFPVCRNFIS MLRRTPLNDI IPFDKNITFH KQVAWMIVLF
     TFIHVAAHIR NFIVLTINTN VGIVGFLEFN FITGPGLTGW VMTIALIVMV WFAMEKRRRA
     HFERFWYSHH LFIIFFLGWQ LHGMFCLIQP DRPPFCSAGQ IGVFWKYWLP GGLVWISERI
     LREVRARHVT YISKVIQHPS KVLEVQIKKE HTTRRAGQYI FLNCPEVSYW QYHPFTLTSA
     PEEDYISVHI RCVGDWTTAF AKSLGANFDA KPSKSDEAGG KVVSPPINKV LPRVMVDGPF
     GSASEDFTKF ETVLLADPIV SAGIGVTPFA SILKSIWYRM NNFGKEGKTR LSKVYFVWVI
     RDFGSAEWFH SLLQAVEAED VEGRIEIHIY LTAKIDEDKM NNLVIQDVGA EKDTITNLRA
     PTHFGRPNWD RVFESIANKH PDTDCGVFFC GPSVLSRTLH QMSNKYTSPM GCRFFFGKEV
     SSVRSRHRTT TDWRVI
//
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