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Database: UniProt
Entry: A0A1S4DS67_CUCME
LinkDB: A0A1S4DS67_CUCME
Original site: A0A1S4DS67_CUCME 
ID   A0A1S4DS67_CUCME        Unreviewed;       679 AA.
AC   A0A1S4DS67;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Cysteine-rich receptor-like protein kinase 26 isoform X1 {ECO:0000313|RefSeq:XP_016898831.1};
GN   Name=LOC103489186 {ECO:0000313|RefSeq:XP_016898831.1};
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_016898831.1};
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_016898831.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_016898831.1; XM_017043342.1.
DR   AlphaFoldDB; A0A1S4DS67; -.
DR   GeneID; 103489186; -.
DR   InParanoid; A0A1S4DS67; -.
DR   OrthoDB; 1053684at2759; -.
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; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR27002:SF844; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 27-RELATED; 1.
DR   PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01657; Stress-antifung; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51473; GNK2; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|RefSeq:XP_016898831.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000313|RefSeq:XP_016898831.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|RefSeq:XP_016898831.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..679
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010295758"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..138
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          144..251
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          381..673
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         409
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   679 AA;  76334 MW;  5961FAC223FC3EFB CRC64;
     MAASTFVFSI TTLSLLVLAL INHPPLAFAQ PRFSRYVCVE YTINNHTTDG AAYKANLNHL
     LTTLTTDHHI DYGFYNSSYG AGENRANVIG LCRGNISPET CRKCLNDSRD LLPVRCPTHK
     EAIGWYQDCM LRYSDRPILG SMELSPSIPM GYPFNASDPE RFTQAARKLI ESLIAKASAG
     DSHVKFSTGN TTLADFPTIY AFAQCTPDLS RRQCNECLTE ALAIIQDCCV GNLFGRVATP
     SCLFRYGDDS LIQWPTSPWL SSSPSPVSSL LNRTTHHGNK SSLSRTFIPV IVPMAVVVLL
     LTITIYMGQR KYSPTTRGEE CMLIKLVFLF FKLNQPLEMD LKFPSTIIPC FEATGQTEEE
     MARMGFMQYD FDTIRIGTDK FSDENKVGEG GFGAVYKGKL PNGRIVAVKR LSQASRQGDV
     EFKNEVVLLS KLRHRNLVKL LGFSFKENEE LLIYEFLQNA SLQKFIFDPL KPGGLDWTTR
     YKIIEGITRG LVYLHEDSRI KIVHQNLKAH NILLDAEMNA KISDSGIARL FALEQTQDDT
     CTIIDNVGCM APEYIRYGHL SSKSNVFSYG VLVLEIVTGH KENYQTVSNI ENTKYPLISY
     ARRNWREGRT LLNIVDPTIE IQSETTMNEV TKCIHIGLLC TQEDVDERPK MTDVLLMLKS
     DLADFPKPSQ PSFFMNTIS
//
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