ID A0A084QS84_STAC4 Unreviewed; 739 AA.
AC A0A084QS84;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN ORFNames=S40285_06822 {ECO:0000313|EMBL:KFA66819.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA66819.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA66819.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA66819.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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; KL660354; KFA66819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QS84; -.
DR STRING; 1283841.A0A084QS84; -.
DR HOGENOM; CLU_023525_0_0_1; -.
DR InParanoid; A0A084QS84; -.
DR OMA; RSYWAVH; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000028524; 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; 1.10.238.10; EF-hand; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000028524};
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 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..58
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 349..466
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 500..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 84282 MW; A1F7726E588B1EBD CRC64;
MGEGQPSMGS SPSPRTEANV KYLDDDEIKQ FVDDLDHNGD GFISYAEVEQ KLDQAHDDLV
AKPGKHHVVQ RDHDNCDDRA RHTFLRGIMG GADRIPRDEF TRAVREWKIP SLKQSKKEEQ
DEKSYFKRLP GWRKVRAYMA VHGPEFGFIG LVVSMQLAFG IWQLVRYQTT PQYRAAFGWG
VVMAKTCAGA LYPTLFFLIL SMSRYVSTYL RRSYHLSRFF NWDLSQKFHV RISCVTILLA
TLHAIGHLTG SFVSGSNPSN QDAVAVLLGP DAVPRPYINY VRSTPGFTGI TALGLFYVLS
LLSIPQVRRW NYEVFQLGHL LMYPIVGLLM AHGSAQLLQW TMLPYFLAVP TLFVLIERVT
RIALGFHHIK AILKVLDNET VEITAVIPSE RLWKYKAGQY IFLQVPQISF FQWHPFTISF
CRGNKMMVHI KTDGNWTGKL RDLGGESGES EIKVGINGPF GAPAQRFYDF NHSVVIGSGI
GVTPFSGILA DLQYKDDLDH GSAHGHEKNL PAREKVPGAV DEDNGPVPRH QPLSSDPSLE
TTKPDPHRAH SFAEDYRRVD FHWIVRDRNY LLWLADLLND VSRSQEWHRQ NDDQPHLDIH
INTHVTAKKK DIVTHVYRWL LELHRTKEHP ASPLTGLLNP THFGRPDFDK ILDEHYEEML
RFQASKRRRM EDELNAQGSD DAEHSSVSSI YDEELKIGVF YCGAPVVGEI LSDKCRELTI
RGRHDGSKIE YHFMIEVFG
//
