ID A0A1S3AY81_CUCME Unreviewed; 1304 AA.
AC A0A1S3AY81;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Leucine-rich repeat receptor protein kinase EMS1 {ECO:0000313|RefSeq:XP_008439189.1};
GN Name=LOC103484060 {ECO:0000313|RefSeq:XP_008439189.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008439189.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_008439189.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR RefSeq; XP_008439189.1; XM_008440967.2.
DR GeneID; 103484060; -.
DR KEGG; cmo:103484060; -.
DR eggNOG; ENOG502QRD1; Eukaryota.
DR InParanoid; A0A1S3AY81; -.
DR OrthoDB; 366616at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 7.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
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; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR PANTHER; PTHR48055:SF6; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR Pfam; PF00560; LRR_1; 16.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 10.
DR SMART; SM00369; LRR_TYP; 15.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_008439189.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|RefSeq:XP_008439189.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1304
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010386805"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1026..1304
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1055
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1304 AA; 142131 MW; EF73F8002F82DC90 CRC64;
MVFHMGMELK RFFFIFILCF ELCILSSNGA TVQNEIFIER ESLVSFKASL ETPEILPWNS
SLPHCFWVGV SCRLGRVTEL SLSSLSLKGQ LSRSLFNLLS LSVLDLSNNL LSGSIPPQIS
NLRSLKVLAL GENQFSGHFP IELTELTQLE NLKLRANLFS GKIPPELGNL KQLRTLDLSS
NAFVGNVPPH IGNLTKILSL DLGNNLLSGS LPLTIFTELT SLTSLDISNN SFSGSIPPEI
GNLKHLAGLY IGINHFSGEL PPEVGNLVLL ENFFSPSCSL TGPLPDELSK LKSLSKLDLS
YNPLGCSIPK MIGELQNLTI LNLVYTELNG SIPAELGRCK NLKTLMLSFN YLSGVLPPEL
SELSMLTFSA ERNQLSGPLP SWFGKWDHVD SILLSSNRFT GEIPPEIGNC SKLNHLSLSN
NLLTGPIPKE ICNAASLMEI DLDSNFLSGT IDDTFVMCKN LTQLVLVDNQ IVGSIPEYFS
DLPLLVINLD ANNFTGSLPR SIWNSVDLME FSAANNQLEG HLPPETGYAA SLERLVLSNN
RLTGIIPDEI GNLTALSVLN LNSNLLEGTI PAMLGDCSAL TTLDLGNNSL SGSIPEKLAD
LSELQCLVLS HNNLSGAIPS KPSAYFRQLT IPDLSFVQHH GVFDLSHNRL SGTIPDELGN
CVVVVDLLLN NNLLSGAIPS SLSQLTNLTT LDLSSNTLTG PIPAEIGNAL KLQGLYLGNN
HLMGMIPESF SHLNSLVKLN LTGNKLSGSV PKTFGGLKAL THLDLSCNEL DGDLPSSLSS
MLNLVGLYVQ ENRLSGQVVE LFPSSMSWKI ETLNLSDNYL EGVLPRTLGN LSYLTTLDLH
GNKFAGTIPS DLGDLMQLEY LDVSNNSLSG EIPEKICSLV NMFYLNLAEN SLEGPIPRSG
ICQNLSKSSL VGNKDLCGRI LGFNCRIKSL ERSAVLNSWS VAGIIIVSVL IVLTVAFAMR
RRIIRSQRDS DPEEMEESKL NSFIDPNLYF LSSSRSKEPL SINVAMFEQP LLKLTLVDIL
EATNNFCKTN IIGDGGFGTV YKATLPDGKV VAVKKLSEAK TQGHREFIAE METIGKVKHH
NLVPLLGYCS LGEEKLLVYE YMVNGSLDLW LRNRTGTLEI LNWETRFKVA SGAARGLAFL
HHGFIPHIIH RDVKASNILL NQDFEPKVAD FGLARLISAC ETHVTTEIAG TFGYIPPEYG
QSGRSTTKGD VYSFGVILLE LVTGKEPTGP DFKEIEGGNL VGWVFQKINK GQAADVLDAT
VLNADSKHMM LQTLQIACVC LSENPANRPS MLQVLKFLKG IKDE
//
