ID R0EVJ3_9BRAS Unreviewed; 545 AA.
AC R0EVJ3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=CARUB_v10026190mg {ECO:0000313|EMBL:EOA13167.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA13167.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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; KB870812; EOA13167.1; -; Genomic_DNA.
DR RefSeq; XP_006280269.1; XM_006280207.1.
DR AlphaFoldDB; R0EVJ3; -.
DR STRING; 81985.R0EVJ3; -.
DR GeneID; 17876305; -.
DR KEGG; crb:17876305; -.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR OrthoDB; 648708at2759; -.
DR Proteomes; UP000029121; 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:SF94; BERBERINE BRIDGE ENZYME-LIKE 24-RELATED; 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:UP000029121};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..545
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004349204"
FT DOMAIN 83..259
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 545 AA; 61562 MW; B2C3CE3583E6481B CRC64;
MGISKPPFTI SCISFLALYI SLYATITPTS SASLQDSFIE CLQRNTNVGF PLERTFFTHE
RNASLFKEVF ESTAQNQRFL TNSMPKPGFI FKPVHESHVQ ASIVCAKKLG IHFLVRSGGH
DYEGVSYVSQ IETQFVLIDL SKLRQVNVDI EDNSAWVQAG ATIGELYYRI AEKSKIHGFP
AGVFPSLGVG GHITGGAYGS LMRKYGLAAD NVLDAKIVDA NGKLLDRAAM GEDLFWAIRG
GSGGSFGIIL SWKIKLVPVP ETITVFTVTK TLEQDASFKI LSKWQRVADK LVEELFLRVF
FTVVGNNAYK TVKMAYIGQF LGEKGTLLEV MKKGFPELGL TQKDCIEMSW IESIVYNSGF
PTSPLPPLEI LLQAKSPIGK IYFKAKSDFA KEPIHILGLI GMVKKFLEED AVLVVWTPYG
GKMNKIPECE IPFPHRNGTI FMIQYYRSWS DNEKRPNRRI KWMRELYSYM TPYVSSNPRQ
AYVNYRDLDL GQNRNSSKSN FLEAKIWGAK YFKDNFSRLV RIKTKVDPDN FFRHEQSIPT
LPIRS
//
