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Database: UniProt
Entry: A0A0E0KN46_ORYPU
LinkDB: A0A0E0KN46_ORYPU
Original site: A0A0E0KN46_ORYPU 
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};
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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
//
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