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Database: UniProt
Entry: A0A2C9UWW0_MANES
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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
//
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