ID A0A0E0K621_ORYPU Unreviewed; 1087 AA.
AC A0A0E0K621;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G32380.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC02G32380.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC02G32380.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR AlphaFoldDB; A0A0E0K621; -.
DR STRING; 4537.A0A0E0K621; -.
DR EnsemblPlants; OPUNC02G32380.1; OPUNC02G32380.1; OPUNC02G32380.
DR Gramene; OPUNC02G32380.1; OPUNC02G32380.1; OPUNC02G32380.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_003108_0_0_1; -.
DR OMA; NWVPSEN; -.
DR Proteomes; UP000026962; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd06410; PB1_UP2; 1.
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; IPR000270; PB1_dom.
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:SF980; KINASE SUPERFAMILY WITH OCTICOSAPEPTIDE_PHOX_BEM1P DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 826..1077
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 698..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 853
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1087 AA; 120086 MW; FDCF05BFA36E575C CRC64;
MAPAAAPASV SAGSAEADGA PRMAKFLCSF GGSILPRPLD GRLRYVGGET RIVMLPRDVS
YADLAARMRE LYEDADIIKY QQPDEDLDAL VSVVNDDDVV NMMEEYDKLI AAGEGFTRLR
IFLFSQHLDD EAAAAAVRYN GDERETERRY VDALNSLGDV RTPSSPVSVE QLFGIGGNES
GIPDIAGLRH LNVPRPSHSQ RYGEMDSPWS PAYISPGHYG VHDPRDFPIS PRFQVGAEDF
DERIPDDFVR HSPKYRHYEV HSPQHVDNLV WLPPGAAVQQ NAGFPGNLGR PGNFLDGSSM
YDHCRSPFHK GQGDPRYVDP RWRPIQNFDQ TSMTNEYSGH PTNSCPDCSR PGERFVLNQD
VRLENGVYVK EQTGGHPPPM FYNESHSHDR AWHAHANQSH QRYEDPRLHL PGSGRAMEPY
IVDNSSVNSA FAPNKTYEVH SASLSRSSHE SPHYFHGSSE HVNDTYHNQQ VGVGGPYVQT
PGFEESTGQH YGHSSTYGAD PFYQMQQNLP PLQSLRRRAN SPVHTGSPYE SPHLPIPNGN
FVRNTGDVSP RIPGMPAYDR IPNPWPSPNG SIPYRVVGHD IPAVVEHRSN PNSGQYVQPL
FAPESVQNQP GVPLMEIHPE RACAGSVLSS QVDGRVVASA LPLTDQLSRI DINPLKKLEG
PEHEKFTRNA SETTSLHAMN DPSALTHHIG VIPEVDPKQR KPVEHETGTS KVHEGGATAL
QECGDISEDR LNFLPELVAS VKKAALEDSE EKEKAQQDAC PALLLTCDEE GNGKKLDETP
TGNTGTDQDS DVHGSGEQQK SSGIEATTAE AEALSKGLQT IKNDDLEEIR ELGSGTYGAV
YHGKWRGCDV AIKRIKASCF AGRPSERERL IADFWKEAQI LSSLHHPNVV SFYGVVRDGP
DGSLATVTEF MINGSLKQFL RKKDRTIDRR KRVILAMDAA FGMEYLHGKN IVHFDLKCEN
LLIGDLGLSK VKQHTLVSGG VRGTLPWMAP ELLSGKSNMV SEKIDVYSFG IVMWELLTGE
EPYSDMRAAA IIGGIVNNSL RPQIPSWCDP EWKSLMESCW ASDPADRPSF TEISQRLRKM
AAAMNVK
//