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Database: UniProt
Entry: I1P7T1_ORYGL
LinkDB: I1P7T1_ORYGL
Original site: I1P7T1_ORYGL 
ID   I1P7T1_ORYGL            Unreviewed;      1015 AA.
AC   I1P7T1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
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:ORGLA03G0042700.1, 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:ORGLA03G0042700.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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DR   AlphaFoldDB; I1P7T1; -.
DR   STRING; 4538.I1P7T1; -.
DR   EnsemblPlants; ORGLA03G0042700.1; ORGLA03G0042700.1; ORGLA03G0042700.
DR   Gramene; ORGLA03G0042700.1; ORGLA03G0042700.1; ORGLA03G0042700.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_006806_0_0_1; -.
DR   OMA; PFQIKGP; -.
DR   Proteomes; UP000007306; Chromosome 3.
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; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR23257:SF813; SERINE_THREONINE-PROTEIN KINASE EDR1; 1.
DR   Pfam; PF14381; EDR1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          733..992
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          992..1015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         761
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1015 AA;  111161 MW;  B0887E20D3828FF1 CRC64;
     MKNLFKSKIK WQHRSNDPAS SQGQGLPQQT PPSPSPASSP SGGAPALSVS TVSSSSPSAA
     ATPTGAAAAG AGGGGGGTGG EDYMLSEEEF QMQLAMALSA SNSECVGDLD GEQIRKAKLI
     SLGRGDRFAA VRDDEQTADA LSRRYRDYNF LDYHEKVIDG FYDIFGPSME SSKQGKMPSL
     ADLQTGIGDL GFEVIVINRA IDTTLQEMEQ VAQCILLDFP VANIAALVQR IAELVTDHMG
     GPVKDANDML TRWLEKSTEL RTSLHTSLLP IGCIKIGLSR HRALLFKILA DSVGIPCKLV
     KGSNYTGDDD DAINIIKMNE REFLVDLMAA PGTLIPSDVL SWKGNSLNSN ARLTQNPLAG
     SSSTTDSNLS ANALPPGHKG GQLPLFSSGD WISASQSGYE KDGATTSSQA SSSGTTSVAA
     GSAFDSSWTL VSHGQSDDPS TSAGMSAQQK VILPGGEHPW NENINARNEN IKLVSDLQGN
     SESINLFADL NPFGGREPKR TSVPLNGPDN RNNELQRRRE NVVPSTRRPQ QRLVMKNWSP
     YNDVSNNKQY NYVEDSFARR NIGDNAASSS QVPRPSAKNT NLNVGVRTDT PYMAAHNYDN
     SMAGSSAMKM TSTAGIGKVP DKVLYGDLDK GLTNSRLGDQ PPIERHKWGN SVEGRIPTGT
     VHNQAKEHKE NFDGKQDNKK LHPDPKKSPL DRFMDTSMPS RNPESVSPSF ARSHKLDTMF
     DDVSECEIHW EDLVIGERIG LGSYGEVYRA DWNGTEVAVK KFLDQDFYGD ALDEFRSEVR
     IMRRLRHPNI VLFMGAVTRP PNLSIVSEYL PRGSLYKILH RPNCQIDEKR RIKMALDVAK
     GMNCLHISVP TIVHRDLKSP NLLVDNNWNV KVCDFGLSRL KHSTFLSSKS TAGTPEWMAP
     EVLRNEQSNE KCDVYSFGVI LWELATLRMP WSGMNPMQVV GAVGFQDKRL DIPKEIDPLV
     ARIIWECWQK DPNLRPSFAQ LTSALKTVQR LVTPSHQESQ SPPVPQEIWV NSSTP
//
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