ID A0A1S3BU82_CUCME Unreviewed; 999 AA.
AC A0A1S3BU82;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC103493324 {ECO:0000313|RefSeq:XP_008452253.1};
GN Synonyms=103493324 {ECO:0000313|EnsemblPlants:MELO3C016502.2.1};
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_008452253.1};
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|EnsemblPlants:MELO3C016502.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_008452253.1}
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_008452253.1; XM_008454031.2.
DR EnsemblPlants; MELO3C016502.2.1; MELO3C016502.2.1; MELO3C016502.2.
DR GeneID; 103493324; -.
DR Gramene; MELO3C016502.2.1; MELO3C016502.2.1; MELO3C016502.2.
DR KEGG; cmo:103493324; -.
DR eggNOG; ENOG502QPVY; Eukaryota.
DR InParanoid; A0A1S3BU82; -.
DR OrthoDB; 1203965at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR Proteomes; UP000596662; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF38; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 13.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 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};
KW Kinase {ECO:0000313|RefSeq:XP_008452253.1};
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};
KW Receptor {ECO:0000313|RefSeq:XP_008452253.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|RefSeq:XP_008452253.1};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..999
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041161071"
FT TRANSMEM 630..652
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 684..960
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 963..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 109635 MW; CFF4EB8EC7A21058 CRC64;
MFFLVFTFFS LLGYSSSHSL VSDFHVLLAL KQGFEFSDSA TLSTWTATNF SSVCSWVGIQ
CSHGRVISVN LTDLNLGGFV SPLISNLDQL TELSFAGNNF SSGIEVVNLS YLRFLNISNN
QFTGTLDWNF SSLPNLEVLD AYNNNFSALL PTEILNLQNL KYLDLGGNFF HGKIPESYGN
LEGLQYLSLA GNDLVGKIPA ALGNLTNLRV IALGHYNVFE GGLPPELGKL ANLVVMDIAD
CNLDGQIPHE LGNLKALNSL YLHTNLFSGS IPKQLGNLTN LVNLDLSNNA LTGEIPSEFV
ELKQLNLYKL FMNKLHGSIP DYIADLPNLE TLELWMNNFT GTIPKNLGQN GRLQLLDLST
NKLTGTIPEG LCSSNQLRIL ILMNNFLFGP IPDGFGTCTS LTKVRLGQNY LNGSIPNGFI
YLPQLNLAEF QDNYLSGTLS ENWESSSTPI KLAQLNLSNN LLSGTLPSSL SNLSFLQILL
LNGNQFSGTI PPSIGELNQL LKLDLSRNSL SGEIPPEIGN CIHLTYLDLS RNNLSGPIPP
EISNAHILNY LNLSRNHLNQ SLPKSIGTMK SLTIADFSFN DFSGKLPESG LAFFNASSFA
GNPQLCGSLL NNPCNFATTT TSKSGKTPTY FKLIFALGLL ICSLVFAVAA VVKAKSFKRN
GASSWKMTSF QKLDFTVFDV LECVKDGNEI GRGGAGIVYH GKMPNGVEIA VKKLLGFGPN
SHDHGFRAEI QTLGNIRHRN IVRLLAFCSN KETNLLVYEY MRNGSLGEAL HGKKASFLGW
NLRYKIAIEA AKGLCYLHHD CSPLIVHRDV KSNNILLNSN FEAHVADFGL AKFMFDGGAS
ECMSVIAGSY GYIAPEYAYT LKVDEKSDVY SFGVVLLELL TGRRPVGDFG DGVVDIAQWC
RRAVTYGENE NDIICLVDKR VGMIPKEEAK HLFFIAKLCV EENSVERPTM REVVQMLAEF
PHQSPSCFQS SSSSSPCQKL KNGEKEREHQ SKSKPDHLV
//
