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Database: UniProt
Entry: A0A0P0WKX1_ORYSJ
LinkDB: A0A0P0WKX1_ORYSJ
Original site: A0A0P0WKX1_ORYSJ 
ID   A0A0P0WKX1_ORYSJ        Unreviewed;       881 AA.
AC   A0A0P0WKX1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Os05g0318700 protein {ECO:0000313|EMBL:BAS93343.1};
GN   OrderedLocusNames=Os05g0318700 {ECO:0000313|EMBL:BAS93343.1};
GN   ORFNames=OSNPB_050318700 {ECO:0000313|EMBL:BAS93343.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:BAS93343.1, ECO:0000313|Proteomes:UP000059680};
RN   [1] {ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RA   Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA   Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA   Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA   Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA   Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA   Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA   Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA   Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA   Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA   Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA   Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA   Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA   Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA   Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA   Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA   Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA   Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA   Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA   Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA   Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA   Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA   Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA   Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA   Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA   Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA   Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA   Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA   Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA   Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA   Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA   Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA   Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA   Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA   Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA   Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA   Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA   Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA   Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA   Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA   Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2] {ECO:0000313|EMBL:BAS93343.1, ECO:0000313|Proteomes:UP000059680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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DR   EMBL; AP014961; BAS93343.1; -; Genomic_DNA.
DR   RefSeq; XP_015640125.1; XM_015784639.1.
DR   RefSeq; XP_015640126.1; XM_015784640.1.
DR   AlphaFoldDB; A0A0P0WKX1; -.
DR   SMR; A0A0P0WKX1; -.
DR   STRING; 39947.A0A0P0WKX1; -.
DR   PaxDb; 39947-A0A0P0WKX1; -.
DR   EnsemblPlants; Os05t0318700-01; Os05t0318700-01; Os05g0318700.
DR   EnsemblPlants; Os05t0318700-02; Os05t0318700-02; Os05g0318700.
DR   GeneID; 4338403; -.
DR   Gramene; Os05t0318700-01; Os05t0318700-01; Os05g0318700.
DR   Gramene; Os05t0318700-02; Os05t0318700-02; Os05g0318700.
DR   KEGG; osa:4338403; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   InParanoid; A0A0P0WKX1; -.
DR   OMA; DDGHWTP; -.
DR   OrthoDB; 339541at2759; -.
DR   Proteomes; UP000059680; Chromosome 5.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   CDD; cd12087; TM_EGFR-like; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045272; ANXUR1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024788; Malectin-like_Carb-bd_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; PTHR34590; OS03G0124300 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR34590:SF16; OS05G0318600 PROTEIN; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 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   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Proteomics identification {ECO:0007829|ProteomicsDB:A0A0P0WKX1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059680};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..881
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006056786"
FT   TRANSMEM        443..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          530..803
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          414..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         558
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   881 AA;  96200 MW;  07648509D62196F7 CRC64;
     MMHPSLLATI QWLTLSALLS IAMAADNNST ASAPIFLNCG ASGVQPDSYN RSWDGDASSK
     FAPSVKGNVA RASYQDPSLP SPVPYMTARF FTSNYTYSFP VSPGRMFVRL HFYPTNYNGN
     LDSANAYFGV TTNNLILLDN FNASQTALAT SSAYFFREFS VNVTSSSLKL TFAPSTRNGS
     YAFVNGIEIV PTPDIFTTPT PTSANGGDNV QYGIDPVMGL QTMYRLNVGG QPISPQGDSG
     FYRSWDNDSP YIYGAAYGVT FSKDGNVTIK YPNTEPNYTA PVAVYATARS MGPTAQINLN
     YNLTWILPVD AGFTYLLRFH FCEIQYPITK VNQRSFFIYI NNQTAQNQMD VIVWSGGIGR
     TTYTNYVVTT VGSGQTDLWV ALHPDLSSKP EYFDAILNGL EVFKLQDLGR NNLAGLNPPL
     PPKPGVNPNG GSSRGKSKSV APAAIGGAVG GLAVLLIACV GLCIICRRKK KVAKDTGKSD
     EGRWTPLTDF TKSQSATSGK TTNTGSHSML PANLCRHFSF AEIQAATNNF DKSFLLGKGG
     FGNVYLGEID SGTRVAIKRG NPLSEQGVHE FQNEIEMLSK LRHRHLVSLI GYCEDRNEMI
     LVYDYMAHGT LREHLYNTKN PPLSWKQRLE ICIGAARGLY YLHTGAKQTI IHRDVKTTNI
     LLDDKWVAKV SDFGLSKAGP NVDNTHVSTV VKGSFGYLDP EYFRRQQLTE KSDVYSFGVV
     LFEVLCARNA LSPSLPKEQV SLADWALRCQ KKGVLGEIID PLLKGKIAPQ CFLKFAETAE
     KCVADRSVDR PSMGDVLWNL EFALQLQEST EDSSSLTEGT SASTSPLVVA RLHSDEPSTD
     VTTTTTTTTS LSITDRSIAS VESDGLTPSN IFSQLMTPDG R
//
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