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Database: UniProt
Entry: A0A1S3CIV1_CUCME
LinkDB: A0A1S3CIV1_CUCME
Original site: A0A1S3CIV1_CUCME 
ID   A0A1S3CIV1_CUCME        Unreviewed;       400 AA.
AC   A0A1S3CIV1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Serine/threonine-protein kinase CDL1 {ECO:0000313|RefSeq:XP_008463258.1};
GN   Name=LOC103501458 {ECO:0000313|RefSeq:XP_008463258.1};
GN   Synonyms=103501458 {ECO:0000313|EnsemblPlants:MELO3C004977.2.1};
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_008463258.1};
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:MELO3C004977.2.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_008463258.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   RefSeq; XP_008463258.1; XM_008465036.2.
DR   EnsemblPlants; MELO3C004977.2.1; MELO3C004977.2.1; MELO3C004977.2.
DR   GeneID; 103501458; -.
DR   Gramene; MELO3C004977.2.1; MELO3C004977.2.1; MELO3C004977.2.
DR   KEGG; cmo:103501458; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   InParanoid; A0A1S3CIV1; -.
DR   OrthoDB; 1217203at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   Proteomes; UP000596662; Unplaced.
DR   GO; GO:0005886; C:plasma 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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR47989; OS01G0750732 PROTEIN; 1.
DR   PANTHER; PTHR47989:SF15; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 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   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_008463258.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..368
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          378..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   400 AA;  44072 MW;  E85F71FED83B9EE3 CRC64;
     MEVEDDYRRK QQLVLLAIVV LASLALVSLL VAFSYYCYIS NKVSKRLKIR KRADLEDGGS
     FENVKEFSTE KGLQLFTFKQ LHSATGGFSK SNVVGHGSFG HVYRGVLNDG RKVAIKLMDQ
     AGKQGEDEFK VEVELLRRLH SPYLLALLGY CSDNNHKLLV YEFMANGGLQ EHLYPVGSSN
     SISVKLDWET RLRVALEAAK GLEYLHEHVC PPVIHRDFKS SNVLLDKNLH AKVSDFGLAK
     IGSDKAGGHV STRVLGTQGY VAPEYALTGH LTTKSDVYSY GVVLLELLTG RVPVDMKRTP
     GEASLVSWAL PRLTDRERVM HIMDPALEGQ YSMKDVVQVA AIAAMCVQPE ADYRPLMADV
     VQSLVPLVRN YRTTSKIIGS SSSSSATKSP APHDNASSGD
//
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