ID A0A0A0K5D9_CUCSA Unreviewed; 557 AA.
AC A0A0A0K5D9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Non-specific serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Csa_7G373510 {ECO:0000313|EMBL:KGN44708.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN44708.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN44708.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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DR EMBL; CM002928; KGN44708.1; -; Genomic_DNA.
DR RefSeq; XP_004148960.1; XM_004148912.2.
DR AlphaFoldDB; A0A0A0K5D9; -.
DR STRING; 3659.A0A0A0K5D9; -.
DR EnsemblPlants; KGN44708; KGN44708; Csa_7G373510.
DR GeneID; 101221720; -.
DR Gramene; KGN44708; KGN44708; Csa_7G373510.
DR KEGG; csv:101221720; -.
DR eggNOG; KOG0605; Eukaryota.
DR OMA; IRSHEWY; -.
DR OrthoDB; 988261at2759; -.
DR Proteomes; UP000029981; Chromosome 7.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21742; MobB_NDR_LATS-like; 1.
DR CDD; cd05599; STKc_NDR_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF346; PROTEIN KINASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 120..418
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 419..491
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 557 AA; 64495 MW; 3A00D80B51E7F54E CRC64;
MDSARSWFNQ RRDRLRGSTK KKDNSMGENE DSTATDQMDE EALSNITKQK VAAAKQYIEN
HYKEQMKNLQ ERKERRNVLE KKLADADVSE EDQNNLLKFL EKKETEYMRL QRHKMGVDDF
DLLTIIGKGA FGEVRVCREK TTGQVYAMKK LKKSEMLRRG QVEHVRAERN LLAEVDSNCI
VKLYCSFQDD EFLYLIMEYL PGGDMMTLLM RKDTLTEDEA RFYVGEIVLA IESIHKHNYI
HRDIKPDNLL LDKFGHLRLS DFGLCKPLDC SILREQDFDI GSTRNGAGQN DERNATPRTQ
QEQLQHWQKN RRMLAYSTVG TPDYIAPEVL LKKGYGMECD WWSLGAIMYE MLVGYPPFYS
DDPMSTCRKI VNWRTHLKFP DEAKLSLLAK DLISKLLCNV NQRLGTNGAD EIKVHSWFEG
TEWDRLYQME AAFVPEVKDE LDTQNFEKFE ESDSQSSTSS KTGPWRKMLS SKDINFVGYT
YKNFEIVNDY QLPGMAELKK KCSKPKRPSI KSLFDGELEE GDASDTPSHS HQHTGGSFSN
SMTSPKMDDV DIRKESM
//
