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Database: UniProt
Entry: I1P2F2_ORYGL
LinkDB: I1P2F2_ORYGL
Original site: I1P2F2_ORYGL 
ID   I1P2F2_ORYGL            Unreviewed;      1040 AA.
AC   I1P2F2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
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:ORGLA02G0215800.1, 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:ORGLA02G0215800.1}
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; I1P2F2; -.
DR   STRING; 4538.I1P2F2; -.
DR   EnsemblPlants; ORGLA02G0215800.1; ORGLA02G0215800.1; ORGLA02G0215800.
DR   Gramene; ORGLA02G0215800.1; ORGLA02G0215800.1; ORGLA02G0215800.
DR   eggNOG; ENOG502QV5Y; Eukaryota.
DR   HOGENOM; CLU_000288_22_9_1; -.
DR   OMA; CCNWVGI; -.
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:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR48056:SF77; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE FEI 1 ISOFORM X1; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51450; LRR; 2.
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   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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1040
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003648689"
FT   TRANSMEM        681..705
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          758..1029
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         786
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1040 AA;  113351 MW;  B4033C656BCF0424 CRC64;
     MAMAFFFCLF FHLLFLFPTN SLNQSYCDPG DASALLGFMQ GLSGSGSGWT VPNATSETAN
     CCAWLGVKCN DGGRVIGLDL QGMKLRGELA VSLGQLDQLQ WLNLSSNNLH GAVPATLVQL
     QRLQRLDLSD NEFSGEFPTN VSLPVIEVFN ISLNSFKEQH PTLHGSTLLA MFDAGYNMFT
     GHIDTSICDP NGVIRVLRFT SNLLSGEFPA GFGNCTKLEE LYVDLNSITG SLPDDLFRLS
     SLRDLSLQEN QLSGRMTPRF GNMSSLSKLD ISFNSFSGYL PNVFGSLGKL EYFSAQSNLF
     RGPLPSSLSH SPSLKMLYLR NNSFHGQIDL NCSAMSQLSS LDLGTNKFIG TIDALSDCHH
     LRSLNLATNN LTGEIPNGFR NLQFLTYISL SNNSFTNVSS ALSVLQGCPS LTSLVLTKNF
     NDGKALPMTG IDGFHNIQVF VIANSHLSGS VPSWVANFAQ LKVLDLSWNK LSGNIPAWIG
     NLEHLFYLDL SNNTLSGGIP NSLTSMKGLL TCNSSQQSTE TDYFPFFIKK NRTGKGLRYN
     QVSSFPPSLI LSHNMLIGPI LPGFGNLKNL HVLDLSNNHI SGMIPDELSG MSSLESLDLS
     HNNLTGSIPS SLTKLNFLSS FSVAFNNLTG AIPLGGQFST FTGSAYEGNP KLCGIRSGLA
     LCQSSHAPTM SVKKNGKNKG VILGIAIGIA LGAAFVLSVA VVLVLKSSFR RQDYIVKAVA
     DTTEALELAP ASLVLLFQNK DDGKAMTIGD ILKSTNNFDQ ANIIGCGGFG LVYKATLPDG
     ATIAIKRLSG DFGQMEREFK AEVETLSKAQ HPNLVLLQGY CRIGNDRLLI YSYMENGSLD
     HWLHEKPDGP SRLSWQTRLQ IAKGAARGLA YLHLSCQPHI LHRDIKSSNI LLDEDFEAHL
     ADFGLARLIC PYDTHVTTDL VGTLGYIPPE YGQSSVANFK GDVYSFGIVL LELLTGKRPV
     DMCKPKGARE LVSWVLHMKE KNCEAEVLDR AMYDKKFEMQ MVQMIDIACL CISESPKLRP
     LTHELVLWLD NIGGSTEATK
//
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