ID   A0A0D9WR33_9ORYZ        Unreviewed;      1062 AA.
AC   A0A0D9WR33;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR06G14840.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR06G14840.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR06G14840.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR06G14840.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   AlphaFoldDB; A0A0D9WR33; -.
DR   STRING; 77586.A0A0D9WR33; -.
DR   EnsemblPlants; LPERR06G14840.1; LPERR06G14840.1; LPERR06G14840.
DR   Gramene; LPERR06G14840.1; LPERR06G14840.1; LPERR06G14840.
DR   eggNOG; ENOG502QQWK; Eukaryota.
DR   HOGENOM; CLU_008585_1_0_1; -.
DR   Proteomes; UP000032180; Chromosome 6.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 2.
DR   Gene3D; 3.40.462.20; -; 2.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 2.
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:SF32; OS06G0549600 PROTEIN; 1.
DR   PANTHER; PTHR32448; OS08G0158400 PROTEIN; 1.
DR   Pfam; PF08031; BBE; 2.
DR   Pfam; PF01565; FAD_binding_4; 2.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 2.
DR   PROSITE; PS51387; FAD_PCMH; 2.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1062
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002348962"
FT   DOMAIN          73..249
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          606..784
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1062 AA;  115302 MW;  E6351C0C97AE6118 CRC64;
     MAVSTCLAFV LAVCCCYAAA IGLPTTADST GEDFLRCLAA SGVPSKLVVT QDSPSFTSTL
     TSSVRNPRFL EPGTVRPLCI VTPTNSSHVQ DAVVCGRRHN IRIRVRSGGH DYEGLSYRSV
     RPEAFAVFDL AALRAVRVDR VAATAWVDSG ATVGELYYVV AKADPELAFP AGLCPTIGIG
     GHFSGGGIGM MMRKYGLSSD NVLDATVVDA NGRLLDKKAM GEDLFWAIRG GGGESFGIVL
     SWKVMLVAVP RTVTVSLIVK SMEQGAVDLV TKWQTLVPVL PDELTIRVFV QDKQARFQTL
     YLGTCDKLLP LMSSQFPELG MTRADCQKMS WVQSMLYLNG GTGSTPLEDL LNKTTSLTSF
     SKYKSDYVNQ AISKASWEKI FPWFDGADAG LIILEPQGGR VGSIGDDDTP YPHRAGVLYN
     IQYISFWPTN ATAAVPDWIR NVYGFMEPFV SCNPRAAYVN YRDLDLGENE VTAGGVTSYE
     SGRVWGEKYF GVANFRRLAL TKGMVDPGDY FRNEQSVPPL VTSNSINPRQ TKEIEMATFF
     RNLALAFTVS FLSCHFLSVP STASPDGFVQ CLLQKIPGEL VLTQSSSSFT DVLVSTIHNP
     TFFNNATARP LCIVTPTDAS HVQAAVRCGR AEGVRLRARS GGHDYEGLSF RSARGGEVFA
     VVDVGARLRA VNVSVDDATA WVESGATLGD LYYAVAKASP ELAFPAGVCP TIGVGGHFTG
     GGISIMSREY GLSVDNILDA KLVNAHGALV DRAAMGEDYF WAIRGGGGES FGIVVSWKIH
     LVKVPPTVAV FGITKTVDEG AADVVATWQH VTQRLPNELS IRVTVRGQSA TFQSLYLGSC
     DQLLALMSSK FPEMEMTSAD CHEMSWLQSV AFIQFMDLTT PVEALLNRTV SQRVATKPKS
     DFVRRAIPKN VWTNIFSWFA MNGSGMMLLE PMGGFMDGVP AAATPYPHRA GVLYNIQYIA
     FWLGDDTAAA AKRWVNDLYA FMEPYVSSNP REAYVNFRDL DIGENAVAND GVSTFESGKV
     WGEKYFAGNF ERLAAVKAAV DPTDYFRNEQ SIPPLLGQSK SK
//