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Database: UniProt
Entry: D7KFN6_ARALL
LinkDB: D7KFN6_ARALL
Original site: D7KFN6_ARALL 
ID   D7KFN6_ARALL            Unreviewed;       537 AA.
AC   D7KFN6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=FAD-binding domain-containing protein {ECO:0000313|EMBL:EFH67152.1};
GN   ORFNames=ARALYDRAFT_890629 {ECO:0000313|EMBL:EFH67152.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|ARBA:ARBA00004191}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; GL348713; EFH67152.1; -; Genomic_DNA.
DR   RefSeq; XP_002890893.1; XM_002890847.1.
DR   AlphaFoldDB; D7KFN6; -.
DR   EnsemblPlants; scaffold_103423.1; scaffold_103423.1; scaffold_103423.1.
DR   GeneID; 9326955; -.
DR   Gramene; scaffold_103423.1; scaffold_103423.1; scaffold_103423.1.
DR   KEGG; aly:9326955; -.
DR   eggNOG; ENOG502QVGN; Eukaryota.
DR   HOGENOM; CLU_018354_6_0_1; -.
DR   OrthoDB; 1094055at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR32448:SF93; BERBERINE BRIDGE ENZYME-LIKE 12; 1.
DR   PANTHER; PTHR32448; OS08G0158400 PROTEIN; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..537
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003101375"
FT   DOMAIN          76..253
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   537 AA;  60450 MW;  B387CC7581A7EE32 CRC64;
     MDKIYLFFLL FFAASSSISL SSADSVTIYE DFVRCFKNVT TISDDDLSAV VLPRTSVSFT
     PTLRAYIRNA RFNTSSTPKP SIIIVPRVDS HVQAAVICAK TLNLQLKIRS GGHDYDGLSY
     VSAVTFLVLD LSNFRNITVD ITDDGAGSAW VQTGATLGEL YYRIWEKSEV HAFPAGVCPT
     VGVGGHVSGG GYGHMIRKFG LTIDHVVDST IVDANGQIHD RKSMGEDLFW AIRGGGGGSF
     GVILAFKVKL VTVPKTVTVF RVDKSVDENA LDMVHKWQFV APRTDPGLFM RVLLSSPTQN
     KTRTVNAKLR ALYLGRADDV VLKMTEEFPE LGLKKEDCKE MTWIQSLLWW MNHVDVDKVK
     PEILLEREPD SAKFLKRKSD YVEKEMTKPE LNRLFQKLAT LDRTGLVLNP YGGNLNVTAV
     NETAFPHRHK LYKIQHSATW PDAGPEAERL YIGNLRTTYK FMTPFVSKNP RSSYLNYRDI
     DIGVNDHGED SYRKGEIYGR KYFGENFDRL VRVKTAVDPE NFFRNEQSIP TLPSNRR
//
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