ID A0A0L9TP40_PHAAN Unreviewed; 527 AA.
AC A0A0L9TP40;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=LR48_Vigan01g177800 {ECO:0000313|EMBL:KOM32222.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM32222.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; CM003371; KOM32222.1; -; Genomic_DNA.
DR RefSeq; XP_017440311.1; XM_017584822.1.
DR AlphaFoldDB; A0A0L9TP40; -.
DR STRING; 3914.A0A0L9TP40; -.
DR EnsemblPlants; KOM32222; KOM32222; LR48_Vigan01g177800.
DR GeneID; 108345952; -.
DR Gramene; KOM32222; KOM32222; LR48_Vigan01g177800.
DR KEGG; var:108345952; -.
DR OMA; GCKKPPE; -.
DR OrthoDB; 655312at2759; -.
DR Proteomes; UP000053144; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR CDD; cd05117; STKc_CAMK; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24349:SF569; MAP KINASE-ACTIVATED PROTEIN KINASE 2; 1.
DR PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
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}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 67..327
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 370..405
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 407..442
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 448..483
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 486..513
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 527 AA; 59452 MW; 28B10184B8CEB7D6 CRC64;
MGICYSATKV SGSNGNAVTD KKNRKRTAKP ESPTAAANPE RRKASARQVP CGKRTDFGYD
KNFDTRYTLG KLLGHGQFGY TYEGIDKANA DRVAVKRIDK SKMVQPIAVE DVKREVKILK
ALTGHENVVQ FYDAFEDDSY VYIVMELCEG GELLDRILAK KDSRYTEKDA AVVVRQMLKV
AAECHLHGLV HRDMKPENFL LKSTKEDSPL KATDFGLSDF IKPGKKFHDI VGSAYYVAPE
VLKRKSGPQS DVWSIGVITY ILLSGRRPFW DKTEDGIFKE VLRKKPDFQR KPWQTISNAA
KDFVKKLLVK DPRARLTAAQ ALSHPWVREG GEASEIPIDI SVLSNMRQFV KYSRLKQFAL
RALASTLNEE ELADLKDQFD AIDVDKNGSI SLEEMRQALA KDLPWKLKEP RVLEILQAID
SNTDGLVDFS EFVAATLHVH QLEDDSGKWQ QRSQAAFEKF DLDKDGYITP DELKMHTGLR
GSIDPLLEEA DIDKDGKISL SEFRRLLRTA SMGSQKVSSP AVYKRRV
//
