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Database: UniProt
Entry: A0A1S3BF04_CUCME
LinkDB: A0A1S3BF04_CUCME
Original site: A0A1S3BF04_CUCME 
ID   A0A1S3BF04_CUCME        Unreviewed;      1221 AA.
AC   A0A1S3BF04;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Cysteine-rich receptor-like protein kinase 10 {ECO:0000313|RefSeq:XP_008446411.2};
GN   Name=LOC103489161 {ECO:0000313|RefSeq:XP_008446411.2};
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_008446411.2};
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_008446411.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   RefSeq; XP_008446411.2; XM_008448189.2.
DR   AlphaFoldDB; A0A1S3BF04; -.
DR   eggNOG; ENOG502QWDY; Eukaryota.
DR   InParanoid; A0A1S3BF04; -.
DR   OrthoDB; 3900892at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   GO; GO:0016020; C: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; 2.
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; 2.
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   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27002:SF427; OS07G0628700 PROTEIN; 1.
DR   PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   Pfam; PF01657; Stress-antifung; 2.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51473; GNK2; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_008446411.2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000313|RefSeq:XP_008446411.2};
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|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        835..858
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          188..466
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          580..685
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          691..798
FT                   /note="Gnk2-homologous"
FT                   /evidence="ECO:0000259|PROSITE:PS51473"
FT   DOMAIN          898..1174
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1196..1221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..82
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..109
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..826
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         926
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1221 AA;  136755 MW;  A57CAD52ED9A1246 CRC64;
     MAMEAPTNIS LRRRSLTAPV SPSDQIFRYV VVNASAVDLP PPPPPSPPPP PPSSPPPPPS
     SPPPNVPPPP FPDAPPPAQS WTELNPSPST PSPLSSLSMP LPPATSPDLS PLPGESRYSS
     LPMIILVLIA TSLFIPLLVR GYKCFIRRGA KKKHTTLKKE DSTFVTEFTS IESLQYDFNT
     IDAATSNFSA DNKLGEGGFG AVYKGMLDNG QEIAVKRLSR RSLQGSEEFK NEVMVVSKLQ
     HRNLVRLLGF CLEGEEKILI YEYIPNKSLD YFLFDSKRRQ ELDWLSRYKI INGIAREILY
     LHEDSRLRII HRDLKASNVL LDDNMHPKIS DFGIARIIQV ADQNNQANIT NRIVGTYGYM
     SPEYAMYGNF STKSDVYSFG VLILEIISGK KNSTFYLSEL AEDILTYAWK LWKEEMALEL
     SDPSLETRYS KDEVLRCIHI GLLCVQDDPS RRPSMASIVL MLNTYSVPLP LPEEPTIFMH
     NTDNAIVINS DQLATNLFIS STNEISITEL HQVAVAKKIV YPINSAKSFF SVHIILTICS
     KTLSRPTFFK LQYNSFTMLN LLTFIFLLNL LTHGNAQNEA SYPYRRCLTG NFTQNSTYQA
     NLNLLFSTLS TNGPPTNRFF NTSVGRSPND TVYGLFQCRG DVTNATCRTF LATATRDAER
     LYCPLAKGAV IWYDEIIFRY SDQPFFSIIT STPNLRLLNL VNIDGDKARF NQLVMSTLRA
     TAALAASSMD ELFATQMANF TQDRNIYTLA QCTGDLSNTD CGECLRQATN EIPNCCTDKQ
     GGRVLLPSCI VRYEVYSFYE TSIPPPATPT PISTIPSRPL LPSSPPPGER RSSTVLIVAI
     VAPITVSILL FVMGCCFLRQ RAKKRDSAVK EDSVVDEMTT SDSLQFDFKT IEAATNKFSE
     ENRLGEGGFG AVFKGRLDNG QEIAVKRLSR GSLQGSEEFK NEVMLVAKLQ HRNLVRLLGF
     CLEGEEKILI YEFIPNKSLD FFLFDQEGQK QLDWLKRYKI INGIARGILY LHEDSRLRII
     HRDLKASNIL LDGDMNAKIS DFGMARIIQM DQSQGNYTSR IVGTYGYMSP EYAMHGNFSM
     KSDIYSFGVL VLEIISGRKN NTFYLSDLAE DILTYAWALW KDGIPLELLD PMLKDNYSRN
     EVLRCIHIAL LCVQEDPNSR PSMASIVLML NSYSVTLPIP KEPALFVRSK DNGNTIGSDH
     SSNKSTKCSV NETSLSELHP R
//
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