ID A0A3Q0EQH3_VIGRR Unreviewed; 1016 AA.
AC A0A3Q0EQH3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC106756291 {ECO:0000313|RefSeq:XP_022634098.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022634098.1};
RN [1] {ECO:0000313|RefSeq:XP_022634098.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022634098.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_022634098.1; XM_022778377.1.
DR AlphaFoldDB; A0A3Q0EQH3; -.
DR Proteomes; UP000087766; Chromosome 2.
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 GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042:SF136; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE 1; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_022634098.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777,
KW ECO:0000313|RefSeq:XP_022634098.1}.
FT DOMAIN 41..150
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 419..723
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1016 AA; 114550 MW; 74E701DD0A5C3183 CRC64;
MGHSSKKKKR GGGSGRRSKG RTQSKDHASQ SGADDYDQLS EEITAVCAIF QEDCKVLPGS
PPRIVIKLRP YSKDMGYEDL DVSAALVVRC LPGYPFKCPK LQITPEKGLS EADADKLLSL
LHDQATLNAR EGRVMIFNLV EAAQEFLSGI EPIAISNDSK LLHSTVESNE ELFTKDKTSL
SKKGSFVYGF IDLFSAYGET WSWGFGMDET AGKSSSPLSN LDGSKQSFEA HEKKFNSKEM
PLVMQEHPAE LGTVIEVIED SKSSLSLTSS STSSEEDFVG NDNEGEKEYF IVDKYTTEDN
DGINESESPK ALPSDFLPHH QPSQTIEKDI LMVHMLRLVC ASNRSLADSL PQVVTELYNI
GIISDLARDM ACKSPSIFNK TFDRVFHKHL ASSRISQFWN PNLGGSNTVS HTSRYLNDFE
ELRPLGHGGF GHVVLCKNKL DGRQYAVKKI RLKDKSMPDR ILREVATLSR LQHQHVVRYY
QAWFETGVSD SSGDSAWGSK TTLSSTFSFT AATSNDVFGH ENQLESTYLY IQMEYCPRTL
RQKFESYNHF DKELAWHLFR QIVEGLAHIH GQGIIHRDLT PNNIFFDARN DIKIGDFGLA
KFLKLEQLDQ DVGHTADATG VSIDGTGQVG TYFYTAPEIE QGWPKIDEKA DMYSLGVVFF
ELWHPFGTAM ERHVVLSDLK QKGEVPSIWV AEFPEQESLL RQLMSPAPSD RPSATELLQN
AFPQRMESQL LDDILRTMQK SEDTSIYDKI LNAIFDEEML STKHIRQVGR LGSVGDSSSS
IQYTEFETEV RDYVVDMNRE IFRQHCAKHL EISTMRLLED CPQFNRNAVK LLTHGGDMLE
LCHELRFPFV NWIIFNQKSS FKRYEISCVF RRAVGHSSPN RYLQGDFDII GGTSALTEAE
VIKVTRDVVT CFFHADSCDI HLNHADLLDA IWSWTGVKVE HRLKVAELLS MMGSLRPQSS
ERKSKWVVIR RQLLQELNLA EAKVNRLQTV GLRFCGSADH ALPRLRGALP SVNCCR
//
