ID B0BES0_CLAPU Unreviewed; 574 AA.
AC B0BES0;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN Name=nox2 {ECO:0000313|EMBL:CAP12328.1};
OS Claviceps purpurea (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=5111 {ECO:0000313|EMBL:CAP12328.1};
RN [1] {ECO:0000313|EMBL:CAP12328.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=20.1 {ECO:0000313|EMBL:CAP12328.1};
RA Giesbert S., Schuerg T., Scheele S., Tudzynski P.;
RT "The NADPH oxidase Cpnox1 is required for full pathogenicity of the ergot
RT fungus Claviceps purpurea.";
RL Submitted (OCT-2007) 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}.
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DR EMBL; AM899999; CAP12328.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:CPUR_03617; -.
DR PHI-base; PHI:3934; -.
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 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 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 286..416
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 574 AA; 65603 MW; 9A3B7115EBA1925E CRC64;
MDSPLELPNA PFQRTWERRS SEQERWTELT RLLLSGKMTQ EKQQELSSRE KFDRWMINEG
QRRVFVFVFA LLHALIFVFA SIHYSLKDSL QGARDVFGFS FTVSRAAALV LHVDVALILF
PVCRTLVSLA RQTPLNGIIQ FDKHITFHIT TAWSMVFFSW VHVIAHWTNF ARLAAKNNLG
FYGWLLANFA SGPGWTGYVM LIALMGIVVT SIEKPRRANY ERFWYTHHLF VVFFLFWSLH
GAFCMIQPDV APFCSGVGTA AVGVFWKYWM YGGFVYLAER VAREIRGRHK TSILKVIQHP
SRVCEIQIRK EKTKVRAAGQ YILFCCPAVS LWQYHPFTLT SAPEEDYIXI HIRCQGDFTM
AVARALGCDW DRKGDIVDDT SKIVGVDKGT NGVHPALQRV LPRVYVDGPF GSASQDVFKY
ETSVLVGAGI GVTPFASILK SIWYRMNYPQ RTCRLSKVYF FWICRDFESF EWFRSLLLAV
EAQDISHRIE IHTYLTAKIT ADDASNIMIN DANAEKDTIT GLRSPTSFGR PNWDLIFRGI
RKLHYPGEAG VFFCGPKPLG SALHVCCNKY TEPG
//
