ID J3M898_ORYBR Unreviewed; 1549 AA.
AC J3M898;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
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:OB05G28220.1};
RN [1] {ECO:0000313|EnsemblPlants:OB05G28220.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB05G28220.1};
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:OB05G28220.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EnsemblPlants; OB05G28220.1; OB05G28220.1; OB05G28220.
DR Gramene; OB05G28220.1; OB05G28220.1; OB05G28220.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_246473_0_0_1; -.
DR Proteomes; UP000006038; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45974:SF229; OS05G0486100 PROTEIN; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1549
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003773556"
FT DOMAIN 631..901
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 582..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1549 AA; 168540 MW; CECA1769A230300A CRC64;
MAMARTLLLA AAAAVLLATT APTGLCDTNA IDADALRDLM QRWRNYPSSW SSGDPCEEWD
GVICSGGRVT SLRLSSINLQ GTLSSSVGLL TQLVFLDLSS NIGLSGPLPA EIGNLGQLTT
LILYGCSFTG EIPKEIGNLP KLWFLALNSN KFTGAIPPSI GLLSNLYYLD LADNQLTGHI
PISSPTSPGL DLLVQTKHFH FNKNQLTGTL TGLFNSNMTL LHILFDSNQL TGLIPAELGS
ITTLEVVRLD RNGFLGAIPS SISKLVGLKQ LNLASNKLTG SVPDLSSMTK LNVVDLSNNT
FYASVAPLWF TTLTSLTSVS MASGNLSGQV PKELFTLPQL QQVVLRNNAL NGTLEMTGTI
SSQLRTVNLR DNRIIYANIQ TYNDTLVQLV GNPLCADQDY SGRPFCSIRQ QDNTIAYTTS
TTQCSSSSSA AQCPDGQSLD PASCGCAFPY SGRMVFRAPF FADVTAAGGE PFRRLETSLS
AQLGLRPGAV YLSDVHWDSD SYLQVQVRLF PSSGVAFNMS ELLRIGFDLS NQTYVAPPNF
GPYFFNADPH SSSPPLLGAD GNKSKNTTLI KAVKAVGGVL AAPHEAAPPH PAPREEAPRR
DGDGDDDDEG APQVDWPRFT MDELNECTDS FSDGNKVGEG GFGSVYRGTL RDGTAVAIKR
AKAETAPDLA REIMAMHRLH HRNLIRLVGY YYEKGELMIV SEFVSNGNLQ ENLRVRSESM
NWHTRLRIAL DSARGLAYLH EHIHPAIIHR DIKSSNILLD DNREAKIADF GISKLLANTN
ESHVFTLVKG TLGYLDPEYV TTNELSKKSD VYSFGIVMLT LVSGREPVQD GENIADKVRR
AVENHDRDGL SDLVDRTIRD DSACTAPALQ RFLRLALRCA SSKAAARPFM GAVVKELEAI
LQSSSPAAGD SSSSSSSTSE SEGAGGSRRA RIPAASDAEG VGCSSGGSNT PDHTPFLRLT
TYRVRVLLLA NPSNSLANKR ASHTPAGHPI ESIDGDDDDD DASGRRRRRR SAGGGGGVRG
EDPYVFFDWK VTYGTKTLLD APQKVILING EFPGPRINCS SNNNIVVNVF NELDEPLLFT
WNGMQHRKNS WQDGLPGTQC PIAPGTNFTY KWQPKDQIGS FFYFPSIGMQ RAAGGYGGIS
VVSRLLIPVP FDPPADDHMV LVGDWYVKDH AAMAKMLDSG KNFGRPAGVL INGKGGKDAA
AAPMFTVEAG KTYRLRVCNV GIKASLNFRI QGHDMKLVEM EGSHTLQDMY DSLDVHVGQC
LSVLVDADQK PGDYYMVAST RFIHDAKSVS AVIRYAGSNT PPAANVPEPP AGWAWSGNQW
RSFRWNRPAS AARPNPQGSY HYGQINITRT IKLLISRGHI DGKLRYGFNG VSHVDADTPL
KLAEYFNVTD GVFRYNQMSD VPPAVNGPLH LVPNVITAEF RTFIEVVFEN PEKSMDSVHL
DGYAFFAAGM GPGKWTPAER KTYNLLDAVS RHSVQVYPRS WTAIMLTFDN AGMWNVRSNI
WERHYLGEQL YISVVSPARS LRDEYNMPEN GLRCGKVVGL PLPPSYLPA
//
