ID A0A2C9VV53_MANES Unreviewed; 1119 AA.
AC A0A2C9VV53;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=MANES_05G110200 {ECO:0000313|EMBL:OAY50124.1};
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:OAY50124.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY50124.1, 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:OAY50124.1};
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}.
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; CM004391; OAY50124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9VV53; -.
DR EnsemblPlants; OAY50124; OAY50124; MANES_05G110200.
DR Gramene; OAY50124; OAY50124; MANES_05G110200.
DR OMA; SRIGVIC; -.
DR OrthoDB; 449350at2759; -.
DR Proteomes; UP000091857; Chromosome lg5.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099402; P:plant organ development; IEA:UniProt.
DR CDD; cd14066; STKc_IRAK; 1.
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; PTHR48054:SF85; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE FLS2; 1.
DR PANTHER; PTHR48054; RECEPTOR KINASE-LIKE PROTEIN XA21; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
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 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1119
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012338597"
FT TRANSMEM 780..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 842..1119
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 741..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 871
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1119 AA; 122389 MW; 8BBA52CF881A3C90 CRC64;
MNTNSFPEIL IFFLLCFCSS VYGGVLPDDS LLLEFKSFVS DPHGILSSWN SSGADHCSWV
GVACNSKSRV LSISIIGGDN GFEGSSQTLS CSESLKFPFT RFGIRRKCSN RVGKLAGNLS
PLIGKLSQLR VLSLPYNELS GEIPLEIWGL KNLEVLDLEG NVFTGKLPSA FVGLRKLRVL
NLGFNVLHGE IPISLSKCAG LELLNLAGNK FKGSISSFFG SFFKLRGLYL ANNKLNGTIP
AVLGSKCQHL QHLDLSGNSL FGGIPDALGN CRQLKTLLLF SNKLNGVVPP ELGQLGRLAV
LDISRNFING AIPAELGNCA ELSVLILSNL FETWPNDRNR SRKISANLPT FANHEYNHFQ
GSIPTEITTL PKLRVLWAPR ITSGGRLPST WGRCESLEMV NLAQNGFVGE INGVFGRCKK
LYYLDLSSNM LSGELDKKLP VPCMTFFDVS QNEISGTIHK FNDNICSRVR SLNSGLGEAC
DPTHGYTSFL RYKTCLASHL PFSVANTAMI HNFSGNKFTG PIRWLPVAPE RLGKQTDYAF
LASGNKVTGL FLGRLFRNCN KLHGVIINIS KNQISGPIPL NIGSVCRSLK FLDVSENQIL
GSIPQSIGDL KFLVALNLSG NKLQGQIPAS LYRLKYLKRI SLAGNNLTGI IPSSFRQLHS
PQSLEITPNS LSGKISENTV KLGNFTSFVL ENNKLLRQLS SGFSNIRSLS SNYPAEPSRL
TSELMNCTDA PGNPFPRSCK TYSFSASSPH PTEGNGDQQS NATSNPETKT GSTGFKHIEI
LSMASAAAVV SVLLVLIFLF FCTRKWRTDA RAQVSEQREI TVFVNIGVPL LYENIVEASG
NFNVSNCIGN GGFGATYKVE ISPGTLVAIK KLAVGRFQGV QQFHAEIKAL SRARHPNLVT
LVGYHASETE MFLIYNYLPG GNLEDFIKER SARAVTWKVL HKIALDIASA LAYLHHQCVP
RILHRDVKPN NILLDNELNA YLSDFGLSRL LGISQTHVTT SVAGTFGYVA PEYAMTSRVS
EKADVYSYGV VLLELISDKK ALDPSFSSHE NGFNIVSWAC TLLRHGQGND VFNAGLWDSA
PRDDLVEMLH LAARCTVASL SMRPNMKQVV QQLKQIQPA
//
