ID A0A0L9UU23_PHAAN Unreviewed; 929 AA.
AC A0A0L9UU23;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=LR48_Vigan06g138300 {ECO:0000313|EMBL:KOM46077.1};
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:KOM46077.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003376; KOM46077.1; -; Genomic_DNA.
DR RefSeq; XP_017427692.1; XM_017572203.1.
DR AlphaFoldDB; A0A0L9UU23; -.
DR STRING; 3914.A0A0L9UU23; -.
DR EnsemblPlants; KOM46077; KOM46077; LR48_Vigan06g138300.
DR GeneID; 108335962; -.
DR Gramene; KOM46077; KOM46077; LR48_Vigan06g138300.
DR KEGG; var:108335962; -.
DR OMA; MHLVPWF; -.
DR OrthoDB; 1210136at2759; -.
DR Proteomes; UP000053144; Chromosome 6.
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 CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
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; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR PANTHER; PTHR47986:SF6; TRANSFERASE, PROTEIN KINASE RLK-PELLE-LRR-IX FAMILY-RELATED; 1.
DR Pfam; PF08263; LRRNT_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..929
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005595940"
FT TRANSMEM 474..496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 577..857
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 433..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 929 AA; 100676 MW; ABB5324FFD7219BC CRC64;
MGFVSWLAVL LLFCVGFECA WCQDDTVMNK LKKAINEPSG LQWNDPDVCK WKHVKCSAMK
RVTAIQIGGQ SLQGSLPKEL AQLSELTRFE CMSNDFTGPF PNMPKSLEVL LIHKNNFQSL
PGDFFTGMTN LQNVSIGYNP FSQWGIPDGL KDCVALRSFS ATSAGLVGKI PDFFGKDGPF
PGLVSLILSF NSLEGGLPAT FSGSSLETLW VNGQKSDGKL NGTLDVLKSM TYLKQIWVHG
NSFTGPIPDF SNHDQLYDVS LRDNQLTGVV PLSLTALPAL KVVNLTNNLL QGSPPLFKDG
VKVDNDLDKG INSFCTVEAG KPCSPVVDAL LSVVEPFGYP LRLAESWKGN VPCGQNWLGI
VCSNGNVSVI NLQSMNLSGN ISPSFASLTS VTKLLLPNNG LTGTIPSELT SMPGLVELDV
SNNQLHGKVP SFREGVVVKT GGNPDIGKDK PQGPPGSNPQ GKSGGQVKKN NTGAIIGTVL
GGISLIGLGA LIFLMYGRKR KQAGKVQGPS AIVVHPRYSG DGNNLKISVA DASAGVSVGG
SGVGGIGVLS PASTAQHVEA GNMVISIQVL RQVTNNFSEA NILGKGGFGT VYKGELYDGT
KIAVKRMECG MMVEKGLTEF ESEIAVLTKV RHRHLVALEG HCLDGNEKLL VYEYMPQGPL
SKHLFDWKEQ GIQPLEWKRR LSIALDVARG VEYLHGLAQQ IFIHRDLKPS NILLGDDMRA
KVSDFGLVRL APEGQTSFET RLAGTFGYLA PEYAVTGRVT TKVDVYSYGV ILMEMITGRK
AIDNSQPEEN VHLVTWFRRM LLNKDSFEKI IDPIMCIDEE ALPSCRTVAE LAGHCCAREP
YQRPDMSHVV NVLAPLVEIW KPSETDDEDI YGIDLDMTLP QALRKWQAVE GRNTFDTSSS
MLTSEENTQS SIPTRPFGFA NSFNSSDGR
//
