ID A0A0E0KN46_ORYPU Unreviewed; 1540 AA.
AC A0A0E0KN46;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
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:OPUNC04G03660.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC04G03660.1}
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:OPUNC04G03660.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 4537.A0A0E0KN46; -.
DR EnsemblPlants; OPUNC04G03660.1; OPUNC04G03660.1; OPUNC04G03660.
DR Gramene; OPUNC04G03660.1; OPUNC04G03660.1; OPUNC04G03660.
DR eggNOG; ENOG502QQEW; Eukaryota.
DR HOGENOM; CLU_000288_116_9_1; -.
DR OMA; YNETECR; -.
DR Proteomes; UP000026962; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd01098; PAN_AP_plant; 2.
DR Gene3D; 2.90.10.30; -; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47976:SF101; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE LECRK1; 1.
DR PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00108; B_lectin; 2.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50927; BULB_LECTIN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000026962};
KW Signal {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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1540
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002365654"
FT TRANSMEM 1212..1236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..153
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 490..764
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 773..900
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 1274..1540
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 440..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1540 AA; 172307 MW; 04C9AC39651D38ED CRC64;
MAHLLFLPFL LLLLLYCTKS AQAQLNITIG SSLTPQGVNN TWVSPSADFA FGFRAVDGNS
SSYLLTVWFN KIADKTVVWY AKTSSNGQDD TIPVQVQSGS ILKLADGALS LRDPSGNEVW
NPRVTDVGYA RMLDTGNFRL LGTDGTTKWE SFGDPSDIIL PTQVLPLGMT LHSRLLATDY
SNGRFQLNVQ DDGNLVLYLV AVPSAYYHDP YWASNTVGNG SQLVFNETGR IYFTLTNGSQ
INITSAGVDS MGDFFHRATL DTDGMFRQYI YPKSKQARSL WQEQWRAVDA LPENICQTIL
TKVGSGVCGF NSYCTFDGTK NTTSCLCPQR YKFFDNERTY KGCRPDFEPQ SCDLDETAAM
LQYEMTPIDR INWPLSDYEQ YSPIDETECR RLCVIDCFCS VAVFNKPSNT CYKKKLPLSN
GNMDSSLQAT VLLKVPRSTN STSMLSSGSS KWKKDKNITS RKKTQLSQPP SNSGLPSKIF
TYSELEKATG GFHEVLGTGA SGVVYKGQLQ DECGTNIAVK KIEKLQQEAQ KEFLVEVQTI
GQTFHRNLVR LLGFCNEGTE RLLVYEFMTN GSLNTFLFND THPHWSLRVQ VALGVSRGLL
YLHEECNKQI IHCDMKPQNI LLDENFAAKI SDFGLAKLLP VNQTQTNTGI RGTRGYVAPE
WFKNIGITSK VDVYSFGVIL LELVCCRKNV ELEVTNEEQT ILTYWANDCY RCGRIDLLVG
GDDEAIFNIK KVERFVAVAL WCLQEEPSMR PTMHKVTQML DGALLSPTCA QAQKNITLGS
TLAPQGPASS WLSPSGDFAF GFRPVEGNTS FYLIAVWFNK ISDNTVVWYA KNTNQDPLVV
EVPSDSFLQL TNDGALSLKD RSGQEVWNPQ VTGVAYGSMR DTGNFVLLGV DDTTKWQTFD
MLSDTILPTQ VIPCNKTRNK SLRARLDIDD YSSGRFLLDV QTDGNLALYL VAVPSGSKYQ
QYWSTDTTGN GSELVFSETG KVYFALTDGT QINISSGAGI GSMADYFHRA TLDPDGVFRQ
YVYPKKANAG ILGGETWIAV SMQPQNICHA IVSDVGSGVC GFNSYCTFDG TRNQIASCQC
PPWYRFFDEQ RKYKGCKQDF QPHSCNLDEA AALTQFELRP IYGVDWPLSD YEKYEPIGQD
DCGRLCVIDC FCAMAVYNQS TSTCWKKKLP LSNGNMADYV QRTVLLKVPS SNSSQSVIST
SSNKWKRNRK HWVLGSSLIL GTSILVNFAL ISIFIFGTYC RITRKKNIPL SQASSKSQLP
LKTFTYKELE RATAGFHEIL GAGASGVVYK GQLEDELKTN IAVKKINKLQ PETEKEFMVE
VETIGQTFHK NLVRLLGFCN EGTERLLVYE FMTNGPLNRL LFDNDRAHWN TRVHIALGVA
RGLLYLHEEC SKQIIHCDIK PQNILLDDNL VAKISDFGLA KLLLTNQTRT NTGIRGTRGY
VAPEWFKNIG ISTKVDVYSF GVILLELVCC RRNVEPEVVD EEQTILTYWA NDCYRSGRID
LLVEGDDEAI YNIKKVERFV TVALWCLQED PSMRPNMLKP
//