ID I1NRJ0_ORYGL Unreviewed; 1059 AA.
AC I1NRJ0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA01G0248000.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA01G0248000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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; I1NRJ0; -.
DR STRING; 4538.I1NRJ0; -.
DR EnsemblPlants; ORGLA01G0248000.1; ORGLA01G0248000.1; ORGLA01G0248000.
DR Gramene; ORGLA01G0248000.1; ORGLA01G0248000.1; ORGLA01G0248000.
DR eggNOG; ENOG502QQPF; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR OMA; EQTHQKC; -.
DR Proteomes; UP000007306; 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; 4.
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; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF29; SERINE-THREONINE PROTEIN KINASE, PLANT-TYPE; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-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}; 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..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1059
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003648194"
FT TRANSMEM 654..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 711..1013
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1015..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 745
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1059 AA; 113319 MW; 1568B028109A337E CRC64;
METMAKAPGP VYLLFLLLAL PCCLIPHRGA AQPAANEARL LLQIKRAWGD PAVLAGWNDT
AAPAAHCSWP YVTCDTAGRV TNLSLANTNV SGPVSDAVGG LSSLVHLDLY NNNINGTFPT
SVYRCVSLRY LNLSQNYLGG ELPADIGVGL GENLTTLVLS GNYFTGTIPK SLSRLQKLEW
LMLDNNNLTG TIPGELGDLT SLTTLTISTN KLGPGQLPES FKNLTKLTTL WASKCQLVGD
MPAYVADMPD LVTLDLAVNN LTGSIPPGIW SLKKLQCLYL FANKLTGDIV VADGAFAAVN
LVYIDLSANP KLGGPIPQDF GLLQKLEVIH LYFNNFSGEI PASIGRLPAL TEIRLFNNRL
TGVLPPELGQ KSPDLWDLEV DFNEFTGPIP EGLCDSGKFQ TFTAANNLLN GSIPERLAGC
TTLEILYLHN NNLSGEVPEA LWTATKLQYV ELQNNRLTGT LPSTMYSNLS SLTVENNQFR
GSIPAAAATL QKFIAGNNNF SGEIPESLGN GMPVLQALNL SGNQLSGGIP KSVSKLKVLT
QLDLSKNQFS GEIPAELGAM PVLNALDLSS NRLSGGIPSS LASLNLNSLN LSSNQLSGQV
PAKFAIGAYA RSFLDNPTLC TSGLGSSYLA GVRSCNAGSP GSASSGGVSP GLRAGLLVAG
AALLLVIVAL AFFAVRDIRR RRKRVAQRED WKITPFQTDL GFSEAAILRG LTEENLVGRG
GSGSVYRVAY TNRYTGGDGA VAVKKIRTGA AKVEEKLERE FESEARILGN VRHNNIVRLL
CCVSGDEAKL LVYDYMDNGS LDGWLHGRPV VAAVARARSA RGGAPALDWP TRLRVAVGAA
QGLYYMHHEC TPPIVHRDVK TSNILLDSEF RAKVADFGLA RMLAQAGTPD TVSAVAGSFG
YMAPECGYTR KVDEKVDVYS FGVVLLELTT GKAANDGGEH GSLADWARHH YQSGESIPDA
TDQCIRYAGY SDEIEVVFRL GVMCTGATPA SRPTMKDVLQ ILVKCSEQTH QKCKAESGQE
EYEVAPLLLP QRGSRRKQPA KAKGADDDAD ERSDFDSIV
//
