ID A0A2C9UWW0_MANES Unreviewed; 986 AA.
AC A0A2C9UWW0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=MANES_12G090400 {ECO:0000313|EMBL:OAY35312.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY35312.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY35312.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY35312.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CM004398; OAY35312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9UWW0; -.
DR STRING; 3983.A0A2C9UWW0; -.
DR EnsemblPlants; OAY35312; OAY35312; MANES_12G090400.
DR Gramene; OAY35312; OAY35312; MANES_12G090400.
DR OMA; EYEIADC; -.
DR OrthoDB; 391466at2759; -.
DR Proteomes; UP000091857; Chromosome lg12.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF70; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 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 Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
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:UP000091857};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..986
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012180693"
FT TRANSMEM 620..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 678..972
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 986 AA; 108826 MW; 75A10D1D84F6AE73 CRC64;
MLLFLSLLFL SFPFPTLSLN QEGLFLQRVK LGLSDPTHAL SNWNERDQTP CNWYGITCDS
VTQRVHSVDL SESFLSGPFP TFLCHLPSLT FISLNNNSIN SSLPVDFSLC QNLESLDVGQ
NLLVGTIPES LAHLPNLRYL NLAGNNLTGE IPVKFGEFRR LETLLLAGNF LNGTIPGQLG
NISTLEALFI AYNPFTPSPL PTQLANLTNL KELWLSDCKL IGPIPTSLSR LSRLENLDLS
QNRLTGSIPI SLNELKSIVQ IELFNNSLSG TLPVRFANLT NLRRFDASMN ELTGTIPIEL
CQLELESLNL YENRLEGTLP ESIANSPNLF ELKLFNNKLT GQLPSKLGQK SPLKSLDVSY
NGFSGEIPEN LCAKGVLEDL ILIYNSFSGK IPESLGKCHS LGRARLRNNQ LSGTVPEDFW
GLPRVYLVEL VGNSLSGQVS KRISSAYNLS ILLISDNKFS GHMPMEIGFL GNLIEISASN
NMFTGPIPGS LVNLSMLNRL VLNGNELSGE FPAGIQGWKS LNELNLADNK LSGPIPDEIG
NLPVLNYLDL SGNHFSGKIP LELQKLKLNV LNLSNNMLSG ELPPLFAKEF YKNSFVGNPG
LCGDLEGLCP QIRGSKKLSY LWILRSIFIL AGLVFVVGVV WFYFKYMNFK KGKKVITISK
WRSFHKLGFS EFEIADSLKE DNVIGSGASG KVYKVILSNG ETVAVKKLSG GSKKSANYDG
FEAEVETLGR IRHKNIVRLW CCCSNGDCKL LVYEYMPNGS LGDLLHSSKS GLLEWPTRYK
IALDAAEGLS YLHHDCVPPI VHRDVKSNNI LLDGEFAARV ADFGVAKVVE GVNKGTESMS
VIAGSYGYIA PEYAYTLRVN EKSDIYSFGV VILELVTGRL PMDPEFGEKD LVKWVHSTLD
QKGVDHVIDP KLDSNLKEDI CRVLEVGLRC TSSLPISRPS MRRVVNLLQE AGAKSKSMPK
SSNKDGKLSP YYHEEVCDEV QLRVES
//