ID A0A0D9WZY2_9ORYZ Unreviewed; 1249 AA.
AC A0A0D9WZY2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:LPERR07G15020.4};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR07G15020.4, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR07G15020.4, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR07G15020.4, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR07G15020.4}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR AlphaFoldDB; A0A0D9WZY2; -.
DR EnsemblPlants; LPERR07G15020.4; LPERR07G15020.4; LPERR07G15020.
DR Gramene; LPERR07G15020.4; LPERR07G15020.4; LPERR07G15020.
DR Proteomes; UP000032180; Chromosome 7.
DR GO; GO:0016020; C:membrane; 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; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
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; PTHR27002:SF428; OS07G0541900 PROTEIN; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01657; Stress-antifung; 3.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51473; GNK2; 4.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000032180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1249
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002349662"
FT TRANSMEM 291..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 928..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..131
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 139..250
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 355..638
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 664..768
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 778..888
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 992..1221
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1019
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1249 AA; 135653 MW; CF68D700EEF309C8 CRC64;
MRRPYPIANA VHLILAVAVV ALPLAAAQPW PICGTGGNYT AGSTYESNLL KLATTLRANA
SASPTLFATG VRGTAPDAVY GLLLCRGDVS ASDCADCGTR VFQDVGQVCN RTRDASLVYN
QCYAQFSDRG DFLAATNNSG DVSLLISGTN ISSNDVAGYD RAVTELLNAT VRYAVENSTR
LFATGQRVGN DPGFRNIYSM AQCSPDLSPA LCRRCLDGLV GQWWETFPLN GEGARVAGAR
CYLRSELGTG PFYTGAPMVL LRADGLSPAS APAPDLVPAT TGGSNNSATK ILVIVLPIVA
VAIVAAISLC LWNMRKNIRS TKAEHFSGLD SSEDLESVKS TLLTLASLQV ATDNFDESKK
LGEGGFGAVY KGLLYGQEVA VKRMSKGSNQ GLEELKNELV LVAKLHHKNL VRLVGFCLED
GERLLVYEYM PNKSLDTFLF EQVRQLDWAT RFRIIEGVAR GLQYLHQDSQ KKIVHRDMKA
SNVLLDVDMN PKIGDFGLAR LFGQDQTRDV TNRIVGTFGY MAPEYVIRGQ YSTKSDVFSF
GILVLEIVTG QRNSGPCFSE QNEDLVWRHW TEGNIVEMID YSLRRNYPEA EVLKCVNIGL
LCVQQNPVER PTMADVVVLL NTDATCSLPA PAAHRPTFFL DGSSGYSQTI TQLSPRPKQA
ELAPLPWPVC GSSANSYTVG STYETNLGNL AFDLRTNASS STLFASGTVG STPDTVYGLL
LCRGDVSTSD CADCGSRVIQ DIGQFCNRTK DKILVYNQCY AQFSDNDFLA ATNNSGGYSL
LISGTNISSG ADVVAYDRAV IDLLNATVRH AVGNPNRRLF ATGKRVGTDP AFGAIYSLAQ
CSPDLSPAQC QRCHDDLLAQ WWETFPVNGR GARVAGPRCY LESELGPFYT GDPMVLLLAD
ELTPVPAPAP PDGVPATTGG KNNSARKILV IILPIVAVAI VAAVSLCIWN MCRKNRSVKS
EHFSGHDRDE DFESVKSTLL SLASLQVATD NFHESKKLGE GGFGSVYKGL LFGQEVAVKR
MSKGSNQGLE ELKNELVLVA KLHHKNLVRL VGFCLEDGER LLVYEARKTA RLGNTDSQKK
IVHRDMKASN VLLDVDMNPK IGDFGLARLF GQDQTRDVTN RIVGTFGYMA RYVIRGQYST
KSDVFGFGIV VLEIVTGQRN SGPYFSEQNE DLVWRHWTEG NIVEVLKCVN IGLLCVQQNP
VERPTMADVM VLLNSDATSS LPAPAAHRPT VFLDGSSGYS QSITQLSPR
//
