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Database: UniProt
Entry: J3MLR7_ORYBR
LinkDB: J3MLR7_ORYBR
Original site: J3MLR7_ORYBR 
ID   J3MLR7_ORYBR            Unreviewed;       663 AA.
AC   J3MLR7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:OB07G23490.1};
OS   Oryza brachyantha (malo sina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB07G23490.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB07G23490.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB07G23490.1};
RX   PubMed=23481403;
RA   Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA   Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA   Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA   An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA   Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA   Chen M.;
RT   "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT   Oryza genome evolution.";
RL   Nat. Commun. 4:1595-1595(2013).
RN   [2] {ECO:0000313|EnsemblPlants:OB07G23490.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2013) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   AlphaFoldDB; J3MLR7; -.
DR   EnsemblPlants; OB07G23490.1; OB07G23490.1; OB07G23490.
DR   Gramene; OB07G23490.1; OB07G23490.1; OB07G23490.
DR   eggNOG; ENOG502QWDY; Eukaryota.
DR   HOGENOM; CLU_000288_35_7_1; -.
DR   OMA; NINECFD; -.
DR   Proteomes; UP000006038; Chromosome 7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR002902; GNK2.
DR   InterPro; IPR038408; GNK2_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27002:SF428; OS07G0541900 PROTEIN; 1.
DR   PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01657; Stress-antifung; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51473; GNK2; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..663
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003773663"
FT   TRANSMEM        292..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..132
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          142..253
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          356..628
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         383
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   663 AA;  72605 MW;  48C2D97219E5A62E CRC64;
     MRRRFFSVHA VLLLAAVALP LAASQPWPVC DSGSGTYAAG STYATNLENL ALTLRANASS
     SATAPTLFAS GSLGSAPDTV YGLLLCRGDL SSSDCADCGT NVWRDAGPTC NRTKGAILVY
     NQCYAQFSDK GDFLASTNNS GKYSLLVSGT NISSTDVAGY DRAVTELLNA TVRYAAESSP
     RLFATGQRVG TDPGFRNIYS MAQCSRDLTA AQCRTCLDDL VGRWWQTFPF PLNGEGARFA
     GPRCYLRSEL GSFYTGDPMV RLPAKVDGLT PAPAPDVVPA TPGGKKNSGS KILVIILPTV
     AVAIIAVTSL CIWNVRKKSR LTRAELLSGL DTSEDFESVK STLLSLASLQ VATDNFHESK
     KLGEGGFGAV YRGILSGQEV AVKRMTKGSN QGLEELKNEL VLVAKLHHRN LVRLVGFCLE
     EGERLLVYEY MPNKSLDNFL FDSEQRKRLD WMTRFRIIEG VARGLQYLHE DSQKKIVHRD
     MKASNILLDA DMNPKIGDFG LARLFAQDQT REVTSRIAGT FGYMAPEYVM RGQYSTKSDV
     FSFGILVIEI VTGRRRNSGP YLSEQNDEDI LSIVWRHWEE RTTAKMIDHS LGRNYPEAEV
     LKCINIGLLC VQQNPVDRPT MADVMVLLNS DTTCSLLAPA PRPTYLVDGI SGYSQTITQW
     SGR
//
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