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Database: UniProt
Entry: G7DVB6_MIXOS
LinkDB: G7DVB6_MIXOS
Original site: G7DVB6_MIXOS 
ID   G7DVB6_MIXOS            Unreviewed;      1552 AA.
AC   G7DVB6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN   Name=Mo01178 {ECO:0000313|EMBL:GAA94526.1};
GN   ORFNames=E5Q_01178 {ECO:0000313|EMBL:GAA94526.1};
OS   Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC   Mixiales; Mixiaceae; Mixia.
OX   NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA94526.1, ECO:0000313|Proteomes:UP000009131};
RN   [1] {ECO:0000313|Proteomes:UP000009131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC   {ECO:0000313|Proteomes:UP000009131};
RX   PubMed=21478649; DOI=10.2323/jgam.57.63;
RA   Nishida H., Nagatsuka Y., Sugiyama J.;
RT   "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL   J. Gen. Appl. Microbiol. 57:63-67(2011).
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:GAA94526.1}.
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DR   EMBL; BABT02000037; GAA94526.1; -; Genomic_DNA.
DR   STRING; 764103.G7DVB6; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_003645_0_0_1; -.
DR   InParanoid; G7DVB6; -.
DR   Proteomes; UP000009131; 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   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
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   Pfam; PF13426; PAS_9; 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; SSF55785; PYP-like sensor domain (PAS 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:UP000009131};
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        94..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        136..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        441..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          313..434
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          778..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          910..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        920..934
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1552 AA;  172388 MW;  F3A52C72A4180C21 CRC64;
     MDEERENVPD RDIMNEYGLG RLASYDRPEL LEEDVKPDYL TRNKSERLRL QGLLLSKMSR
     PPSRLDVDER VLDAPVTRGE AFALWMVNEG RRRIFFGVFL IVQTLVFVLG FVNYAYSDNF
     DNARATFHIT YPIARAAALT LHFDLALILL PVCRNMISFL RNTPLGAVIP FDSNITFHKA
     VAWSMVFFTA VHVTAHMVNF AQLGIASGTN VVGFLGANFA TGPGITGWIM TLALAVMVWT
     AIEKNRRANF ERFWYAHHLG LVFFLMWSIH GMFCMIQPDR PPYCSASSIG IFWRYWLVGG
     TIYSYERILR ELRSRHKTYI TKVIQHPSNV VEIQFQREGA VSRPGQYIFL NCPAISLWQW
     HPFTLTSAPE HGYLSVHIRM VGDFTRALGE ALGCDLEGDK GGAAKAGSQE IQVTNKQVLP
     RIMIDGPFGS SSEDYRKFDT VVLVGAGIGI TPFASILSSI WYQKNEARRR GKKTRLTKVY
     FFWICRDTTT LSWFQNLLSA IEDQDDEGYV EIHTYVTQRL KEAELNNLMI ADVGSERDSI
     TGLKAPTHFG RPNWSAIFQS LQHRHPSTEV GVFFCGPKPL GSALHLLGNF ACSDTIMDKL
     RKRSWLRPVK SKNALQGATD AVSTASQISV EVSHQQTSAR ERSWPSLSIR ATLDSRFMSS
     RASSIPQATS PSYMGSDAHS LSTLTSSCRP EPRYLVAGEI PRPTLVIEDV QLFDVCNASP
     AYDDAREDQD SVASPASVLG RQSTVCLRRM GIDTDAESGA DPDLKRFSFP LPASTSVGSR
     ASLVKEPAGS RVLTPASSPA VASPSSRSPQ SRSPTGYGPS SALARRPSTS AALSLMPKHP
     TTEYLADQLN SKQEYASSES AMTEPRRPSS PAPLGRADQV LIPARRDSVD SAEEALRDLN
     LTSTDETVSR PVAFSYGPTR PVRTKQSPDL STQWRRVDEL TAARSSDPSK SPQKPSGREH
     TLRSPASADN IVQIHRDPAL ASSGNRLSKS GVSINSTSTE SLSMWPRTDS FPATLHREAM
     HDRSDLPANM PEWSRLQADE PTSYPNNKIV RDLDFAMRKL LSEAVFKDFL EDPLARWRFR
     EYLKTTRGDP PYLLDCWWDA ELFARQFRAL RQGAHDFGQL YLQPTVAISD KVGVSSDKMS
     DASLVLDSIA TASNPVARIQ DDMLRTMFKT DFQSFVKTRL VEQARVKLGS FTLRDKEKGQ
     GLGDCFVITN PRQRDHPIIG ASDAFVELTG YSRQAICSRN CRFLQGPSTS REAVARIRVA
     LNTGQACTEL LLNYRQNGQP FFNLLCIFPL RDTDGSVSYY CGGQINVSGP LKSSKSLRFL
     VGIEDEEPNG AGSEVEPSPT MSQYLTHKRS NLESPAQCNP LFPSAAGYQP SSAELSRHTS
     ARSAIVLDSL ANGKEPQQTP GPGAEQQFRV KEAKGIDEAS REFESVYSKA IFLEPHRCKI
     LFATEPFLEY LGLPTSTAKE RFNSAVLRQD LTDLLHSPKP EGTKRLRDQV RAAIAEGQAF
     SVLTDIKISS TSLSHIIPRK KTLARQRGML HATPIKDTSG SIFAFVALFG TD
//
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