ID A0A0E0BNQ5_9ORYZ Unreviewed; 1122 AA.
AC A0A0E0BNQ5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM12G02920.3};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM12G02920.3}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM12G02920.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0E0BNQ5; -.
DR EnsemblPlants; OGLUM12G02920.3; OGLUM12G02920.3; OGLUM12G02920.
DR Gramene; OGLUM12G02920.3; OGLUM12G02920.3; OGLUM12G02920.
DR Proteomes; UP000026961; 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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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 InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005:SF412; OS04G0307900 PROTEIN; 1.
DR PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR Pfam; PF13947; GUB_WAK_bind; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 785..1059
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 814
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1122 AA; 123858 MW; 8DFE8D27E026BA4E CRC64;
MGRRREVGRD ATAWSKAHPG RGPASSVRRQ IRLGTIVWLA DVSGYPKTTE VLAQGPLQWK
NVVGAVGISF LPSVTGGSAA PMLLRLLLLL QGLSSAVVLP CMVMAALDGE AQRRFQHRLE
VRDLAASSEL LAKGFGCGCC CWRSQRFEVA AAPQQFLGGL RLGDDASSST GGQVSRMMRR
GFGPPGPQNL RGHFYLPAKV TVQIKSTAKD SLTTSRKEKK MNLLCAIAIL PVILVALLDT
TLLAIASSSL MNHSQPSMAT LASCPKSCGQ LSIHYPFGIG AGCFRQPDFN LICDNSTQPP
KLFLHDGATE IIGDTDSSSD MDVGTTEWID VKISATIPML PAGIVHYNYS WNLSSFSIEY
AILNITGCNF DTYIINPDTD TRTRICRNSC PKEEITEAVA RQSCNGTGCC TFYIDNVANF
QLSFIRGDEG SDGATVLWSI IDQPTCASAK DNRTDYACVS ANSTCIDSFN SMEYLGYLCY
CNSGFIGDPC VLHGCTRDEG YYPVQQKANC SRRCGNISVP FPFGLEEGCA ARKLFQLNCT
NVTSSTLQFD RGHVVTDIDF AEGVVGIKLA SYFEEEEFSM YRSGEPDLYA SFGEAVISVH
WAAANLTCQE AQKNHSRYAC VSANSTCLGV DSTYGYVGYR CKCMDGFHGN PYVVNGCEDI
DECKKTLGIC KGICHNDIGS YHCMECPDKT EYDVTAMQCV SRKKQNLLIG IVIGLSVGFT
VLLFVLGGML LLRRWKRDIQ RQLRRNYFRK NQGLLLEQLI SSDENASDKT KIFSLEELEK
VTNNFDPTRI LGRGGHGMVY KGILCDQRVV AIKKSKIIKQ EEIDNFINEV AILSQINHRN
IVRLFGCCLE TEVPLLVYDF IPNGSLFGIL HADASSSFRL SWDDCLRIAT EAAGALCYLH
SAASVSVFHR DVKSANILLD ANCTAKVSDF GASRLVSINE THVVTNVQGT FGYLDPEYYH
TGQLNKKSDV YSFGVVLIEL LLRKEPIFTS ETGLKQNLSN YFLWEKKMKL IRDIVAGQVL
EEATDEEINI VASLAEDCLS LRRDERPTMK QVELALQFLL NKRLNSYRTV QANKEEMDPF
IMTKVQHSTE NSNVEFLSNK ATISSYQTGL EHEFMSSATI PR
//