ID A0A2C5XE15_9PEZI Unreviewed; 567 AA.
AC A0A2C5XE15;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Probable metalloreductase AIM14 {ECO:0000256|ARBA:ARBA00039704};
GN Name=noxA {ECO:0000313|EMBL:PHH54850.1};
GN ORFNames=CFIMG_007688RA00001 {ECO:0000313|EMBL:PHH54850.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH54850.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH54850.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH54850.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH54850.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH54850.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
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:PHH54850.1}.
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DR EMBL; APWK03000018; PHH54850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5XE15; -.
DR SMR; A0A2C5XE15; -.
DR STRING; 1035309.A0A2C5XE15; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000222788; 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; 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; 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:UP000222788};
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 52..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 274..399
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 567 AA; 64785 MW; 609C5D7E6F1F7185 CRC64;
MDSFYEKPME RSRGTPLTRM LLSGEMTQER QSELTSKERF DRWMINEGYR RFFVFVFAVL
QVLVFSFAAV NFSRKENLVT ARNTFGFTFV IARSAALVLH VNIALILFPV CRTLISLARQ
TPLNGIIQFD KNITFHIVTA WSIVFWSWVH TVAHWNNFAQ ISAKNNLGFY GFLVANLVSG
PGWTGYVMLV ALMGMVMTSM EKPRRANYER FWYTHHMFIV FFFFWSIHGA FCMIQPDFAP
FCSSVGPSAI GVFWQYWMYG GFAYLAERIA REVRGRHRTV ISKVVQHPSN VCEIQIKKAN
TKTRAGQYIF LCCPAVSLWQ YHPFTLTSAP EEDYISIHMR IVGDFTRELA TVLGCELGGK
DKVKGSNVVG TGADGIDPAL RRVLPRVYVD GPFGSASEDV FKYEISMLVG AGIGVTPFAS
ILKSIWYRMN YPKERTRLSK VYFFWICRDF GSFEWFRSLL LAIEAQDVDQ RIDIHTYLTA
RIKADDAVNI MINDANAEKD AITGLRSPTN FGRPNWDMIF RGVRKLHTPA ECGVFFCGPK
GLGSALHIFC NKYSDPGFSF VWGKENF
//
