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Database: UniProt
Entry: A0A068VM87_COFCA
LinkDB: A0A068VM87_COFCA
Original site: A0A068VM87_COFCA 
ID   A0A068VM87_COFCA        Unreviewed;       726 AA.
AC   A0A068VM87;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=GSCOC_T00007330001 {ECO:0000313|EMBL:CDP20793.1};
OS   Coffea canephora (Robusta coffee).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX   NCBI_TaxID=49390 {ECO:0000313|EMBL:CDP20793.1, ECO:0000313|Proteomes:UP000295252};
RN   [1] {ECO:0000313|Proteomes:UP000295252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH200-94 {ECO:0000313|Proteomes:UP000295252};
RX   PubMed=25190796; DOI=10.1126/science.1255274;
RA   Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA   Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA   Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA   Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA   Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA   Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA   Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA   Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA   Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA   Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA   Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA   Lashermes P.;
RT   "The coffee genome provides insight into the convergent evolution of
RT   caffeine biosynthesis.";
RL   Science 345:1181-1184(2014).
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; HG740846; CDP20793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068VM87; -.
DR   STRING; 49390.A0A068VM87; -.
DR   EnsemblPlants; CDP20793; CDP20793; GSCOC_T00007330001.
DR   Gramene; CDP20793; CDP20793; GSCOC_T00007330001.
DR   InParanoid; A0A068VM87; -.
DR   PhylomeDB; A0A068VM87; -.
DR   Proteomes; UP000295252; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProt.
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; IPR001611; Leu-rich_rpt.
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; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR   PANTHER; PTHR48005:SF16; OS02G0553000 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00365; LRR_SD22; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51450; LRR; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295252};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..726
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001655963"
FT   TRANSMEM        396..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          450..721
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   726 AA;  79289 MW;  EE8201E93BA5A277 CRC64;
     MDYLSIRKSF FAFLLVLFVS SFSAKANAST SDEEAAALLK WKASSGNENN SFLTSWNLQP
     TNAKNSSNPC TWAGVSCIDG SLIHLNLSSN LLSKKIPPEI GLLSKLETLL LSLNNFCGSI
     PMEVGQLRSL MQLSLHANNI HGPVPSSLGN MKNLTFLSLG YNMLSGPIPT EIGNLSNLAY
     INMQSNYLTG PIPPEIGNLK ALESLSLSEN NLTGSIPKSL GSTTNLALLS LDRNQFSGSI
     PASLGNLSKL EILELQDNKI SGAILEELGQ IPELVMLEMG ENQLSGQLPK QLCQNSKLMY
     FSVSNNLLTG PIPRCLRNCL SLIRATFSGN QLTGNLTEII LRMANNNISE GPVPNGTAFR
     NATIEELKGN KGLCGNNAGL KPCENPQRKE KGHKHVLIIV LPLVGSLILV CASLGVLICC
     ERRKSKRTTN GHGMDVKDDN LEILKATQEF NDLFYIGGGG YGSVYKAQLL SGATLAVKRL
     HDLSEMADHG GFLNEIRALT RIKHQNIVNL YGFCSNATHS LLVYEYLGQG SLAKILRMDK
     EATELDWEKR VNIIRGVADA LSYMHHDCSH PIFHRDISSY NVLLDSEYQA RISDFGTAKL
     LKKGSSNWSA LPGRCGSIAP ELAYTMKATE KCDVYSFGIL TLEIIRGRHP GDLIDVLMSQ
     KPGNIELKEL LDQRLAYPSP ENEKILVSIL KIARSCLEVD PKSRPTMLVI YRLLSIGAPV
     VQHPGE
//
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