ID A0A1Y1UHE3_9TREE Unreviewed; 718 AA.
AC A0A1Y1UHE3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN ORFNames=BD324DRAFT_629122 {ECO:0000313|EMBL:ORX36505.1};
OS Kockovaella imperatae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cuniculitremaceae; Kockovaella.
OX NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX36505.1, ECO:0000313|Proteomes:UP000193218};
RN [1] {ECO:0000313|EMBL:ORX36505.1, ECO:0000313|Proteomes:UP000193218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX36505.1,
RC ECO:0000313|Proteomes:UP000193218};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (MAR-2017) 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:ORX36505.1}.
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DR EMBL; NBSH01000008; ORX36505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1UHE3; -.
DR STRING; 4999.A0A1Y1UHE3; -.
DR InParanoid; A0A1Y1UHE3; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000193218; 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; IPR011992; EF-hand-dom_pair.
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; SSF47473; EF-hand; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000193218};
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 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..67
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 352..472
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 82258 MW; D3619CEF39A5DD7E CRC64;
MSTDASSASN TLAPGPSSPS LFPHPDPEIQ PLSDDEIRAF VDELDTNHDG SISYDELEHR
LDLVHEEIAP DPAPHMLHHK SNSEKNARHA FLRSILGTSA DRIPRDEFAA RVKEWNIPSM
KQDDDEEEHE RDYIRHLSRW RRIRSWWSVH GPEAMFILLV VAMHLAFGLW QMIKYITIPG
YRAAFGWGVV MAKTCAGFLY STFFFLLLSM CRYLSTFLRR SYYMSRFINW YLSQKFHIYM
SILALCLATL HAIGHLSGSF VFGSMPSRAP AVEALGIPTP RPYIVYVRSV PGFTGLTALG
LFYLLAILSI PKVRRWNYEL FQLGHLLMFP IIGLLMAHGS AALLQWPMLG YFLAFPTLLI
LIERITRIFV GFRGIPATIR VLDSQTVEIR ATIPKIYIWS YRPGQYVFLQ VPRISRWQWH
PFTVSVCTGR HMRLHIKTDG NWTGQLRDLA TGEKSTDIKI GIHGPFGAPA QRFYDFTHTV
LVGAGIGVTP FSGILADLQA RDDAEHGGPE GRSEGIDEDE QDLRLSRRSS RISRVASRSL
SRVRSLTQRE YAPNYRRVDF HWMVRDRNHL SWFSDLLNRV STSQQYHRQQ VTPAAPHPHL
DIRLFTHVTQ KRKNISTHVY RWLLESHRTE SHPESPLTGL LNSTHFGRPD FVNILDAHYE
DMAKFAADQR LERLKVGVFF CGAPIIGEIL ADRCEQLTAR GRHEGTGIEY HFMIEVFG
//
