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Database: UniProt
Entry: K3XUU0_SETIT
LinkDB: K3XUU0_SETIT
Original site: K3XUU0_SETIT 
ID   K3XUU0_SETIT            Unreviewed;      1350 AA.
AC   K3XUU0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL09879, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EnsemblPlants:KQL09879, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL09879,
RC   ECO:0000313|Proteomes:UP000004995};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EnsemblPlants:KQL09879}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL09879};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) 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   EMBL; AGNK02002288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 4555.K3XUU0; -.
DR   EnsemblPlants; KQL09879; KQL09879; SETIT_005697mg.
DR   Gramene; KQL09879; KQL09879; SETIT_005697mg.
DR   eggNOG; KOG0597; Eukaryota.
DR   HOGENOM; CLU_002453_1_1_1; -.
DR   InParanoid; K3XUU0; -.
DR   OMA; HAVEIMS; -.
DR   Proteomes; UP000004995; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14002; STKc_STK36; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
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; PTHR22983; PROTEIN KINASE RELATED; 1.
DR   PANTHER; PTHR22983:SF6; SERINE_THREONINE-PROTEIN KINASE 36; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00185; ARM; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..256
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          260..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1350 AA;  148672 MW;  DF6D33EC5A56C620 CRC64;
     MGIEDYHVID LVGEGSFGKV YKGRRKYTRQ TVAMKFILKH GKTDKDIHNL RQEIEILRKL
     KHENIIEMID AFETPQEFCV VTEFAQGELF EVLEDDKCLP EEQVQAIAKQ LVKALYYLHS
     NRIIHRDMKP QNILIGKGSI VKLCDFGFAR AMSANTVVLR SIKGTPLYMA PELVREQPYN
     HTADLWSLGV ILYELFVGQP PFYTNSVYAL IRHIVKDPVK YPDNMSSNFK SFLKGLLNKV
     PQSRLTWPAL LEHPFVKDDS MESSIDTRTA PFEVKGSEDT RKKEEIQTPT NQSSQADPES
     RITVTNRENA SDKPKGNRKL DVPMQATEDH YGSSTGADPE NCSPSPSGNM FLFWMYAISK
     YFIAECTTLD KLEKASQTVK GANSILEDSE ALSTIVSPIK IWLTNPPSSP RELNIDGANQ
     SLRIIKNLID ASSCQSYAAI DICMLLEFTN LIIRTKLSDA YGLVMKCLAI ARKLLDTNDE
     LILSSYDRYW SSLYELYSQI LVSTVDPSGR IPRESTACLA LMLSRVISGL KASMSSEGPK
     PVDKTLLKII DQSRRSQLLE LLCECLIASG SDIISGSTNM VPAACEACKA IWYLAHAVEI
     MSISAQNFSF PFSNSWRHIH SIQEQGSMAD SNSTNLINIF VKSFLGSRPM QVAVYHCLHN
     GLESAIHACL QLISRACLQN MSFCAIICRP WNLPSDVDAV EYGGDGTIVS DMFSLLSLCG
     SILNKESKQN NNQKCKLSNP HALVVHCCLA LATIAACLKS GGESSASVIL TSSQKKQRSR
     LSVLAHLSSV DDTVKSCLQP HCASAMLALS ALVSLENGGQ TRSSLCETAL ALFPRMATLH
     TLLKLWLSDG SEALCRYNAG LLNLFGLRDG SIGLLETRLK WGGPLAIEQA CSVGIPQLLI
     RLLTDGFSKE TSDGKDGSAS RSGLSPLGVV WTLSTLSQCL PGGIFREVLY RREQLKLLTD
     LLSDVHLKAL AAWTGLGGGK RGVRELINSV VDILAFPFVA VQSSPNMPSA SASINSGFLL
     NVASPGVRIG TENKEMLKTI EQNMPQYIQV LLEVGIPGCM LRCLDYVDME DLARPLAIVA
     KMAGYRPLAL QLLKEGLLDP RRVAGLLEGP IAKETLLDFL MIVSDLARMS KDFYVPIDKA
     GLVGFLKNFL SNEDPDIRAK ACSAIGNMCR HSSYFYSPLA ANKVIQLVVD RCSDPDKRTR
     KFACFAVGNA AYHNDMLYEE LRRSIPQLTT LLLGPEEDKT KGNAAGALSN LVRNSDILCE
     DIVSQGAIQA LLKMVGSYST VALSPSRRDA LTESPLRIVL FALRKMCDHA ICRNFLRSSE
     LLPVIVHLRQ SPDPTISEYA SAIASRACQA
//
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