ID A0A0E0BH91_9ORYZ Unreviewed; 972 AA.
AC A0A0E0BH91;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM11G07960.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM11G07960.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM11G07960.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR AlphaFoldDB; A0A0E0BH91; -.
DR STRING; 40148.A0A0E0BH91; -.
DR EnsemblPlants; OGLUM11G07960.1; OGLUM11G07960.1; OGLUM11G07960.
DR Gramene; OGLUM11G07960.1; OGLUM11G07960.1; OGLUM11G07960.
DR eggNOG; ENOG502QQH6; Eukaryota.
DR HOGENOM; CLU_000288_14_1_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45974:SF266; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE HPCA1; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000026961};
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|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..972
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002355086"
FT TRANSMEM 578..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 652..924
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 933..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 972 AA; 106735 MW; 67D56226ECBFF454 CRC64;
MGHSPTSWRI IHLLVFLIIV LDHALIISAD TDPQDTSALN GIAASWDNAK SKLSEWVGND
PCGEKWPGVY CTQNRVTSIR LSSFGLSGSL SGDIQSLSEL QYLDLSYNNL SGPLPPNIGS
LSNLESLSVV GCQFSGDIPK ELSQLPKLRF LSLNNNRFTG SIPPSIGNLS NMYWLDLGEN
RLTGSLPVSD GTNTGLDNLT NALHFHFGVN QLSGTIPSQL FKSNMKLIHL LLDNNNFTGG
IPPTLTLLTK LEVLRLDRNY QLTGPVPASI NSLTKLQELH LENNKLTGPL PDLTGMDSLY
VVSMGNNNFS SSNVPTWFTA LSALTSLNLE NLHITGELPQ PLFKLPAIQT LGLKGNNFNG
TLTIGSDYSS TLSLIDLQDN QITTLAVSGA QYNKKLILVG NPICVQGNNE ALYCKSSQQA
NPAAKPYSTQ SICPGLPPTC LSDQYLSPNC TCAVPYMGTL HFRSPPFFDL SNDTFFVLLE
ENMKEAFLGK QLPVESIALD NPAFGPSNNL DINLRVFPSG KIRFGKEDIS YIGFMLNNQT
YKPHAPGINY GPYYFIGQSY PFAETLSAPR QTKKNQSLII GVSAGGAFVV VSLLVLFTVL
FFRRNKRPKL QPQPRSPSYA SWDIKSTSIS TPHLQGTRVF TFDELKKITN SFSDANDIGT
GGYGKVYRGV LPNGHLIAVK RSEQGSLQGN LEFRTEIELL SRVHHKNLVS LVGFCFDQGE
QMLVYEYVPN GTLKDSLTGK SGVRLDWKRR LRVVLGAAKG IAYLHELADP PIVHRDIKSS
NILLDGNLHT KVSDFGLSKP LNQDGRGQVT TQVKGTMGYL DPEYYMTQQL TEKSDVYSFG
VLLLEVITAR KPLERGRYIV REVKGAMDRT KDLYGLHELL DPMLAPTSLA GFELYVDLAL
KCVEEAGMDR PSMSEVVAEI EKIMKMAGVN PKVDSASNSM SYNSRTPRHP YSGESQFDYS
GGIPSSSRVE PK
//
