ID A0A2C9WB93_MANES Unreviewed; 1143 AA.
AC A0A2C9WB93;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=MANES_02G055300 {ECO:0000313|EMBL:OAY56915.1};
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:OAY56915.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY56915.1, 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:OAY56915.1};
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; CM004388; OAY56915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9WB93; -.
DR STRING; 3983.A0A2C9WB93; -.
DR EnsemblPlants; OAY56915; OAY56915; MANES_02G055300.
DR Gramene; OAY56915; OAY56915; MANES_02G055300.
DR OMA; NCANLEH; -.
DR OrthoDB; 449350at2759; -.
DR Proteomes; UP000091857; Chromosome lg2.
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; 4.
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:SF81; LEUCINE-RICH REPEAT CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 4.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 6.
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; 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};
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 TRANSMEM 21..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 864..1138
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 892
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1143 AA; 123902 MW; E260065921713114 CRC64;
MGSICFSSSV FKWYSFNKLK LFYVFLVINL SLNGVVLCDS DKSVLLEFKN SVSDPSGLLS
SWNLTSPNHC FWPGVSCDND SYVVSLNITG HRNNNRGKNS ENGSPFFCSG SVQNPLYGFG
IRRDCQVGNG FIWGKLIPAI AKLTELRVLS LPFNGFRGEI PLEIWRMQKL EVLDLEGNMV
TGSLPISFAG LRNLRVLNLG FNNIGGEIPS SLSYCTNLEI LNLAGNGING TLPAFIGGFR
GVYLSLNQLG GAVPTEFGDN CETLEHLDLS GNFFVGGIPG SLGNCGNLRT LLLYSNLFEE
VIPSEFGMLR KLEVLDVSRN SLSGSIPREL GKCAGLSVLV LSNFFDPYHN VNSSRGGYLL
DQSGSANEDF NFFQGGIPGE IVTLPNLKML WAPGATLEGN LPSNWGACEK LEMINLAFNF
FTSEIPHEFS HCSKLWYLDL SYNRLKGELV KELQVPCMAV FDVSGNSLSG TIPVFYSGSC
ESGPSTYGYS SSIYDPSSAY LSFFANKAKS GSPVKSLEGD GEISIVHNFG GNNFTGTLQS
MPIAPLRLEK KTTYAFLAGG NKLTGPFPGI LFEKCNELDK LILNVSNNRM SGQIPADVGT
MCRSLTLLDA SNNQITGFIP PGVGKMVSLV SLNLSWNLLQ GLIPTSLSQI KGLKYLSLAG
NKMNGSIPSS LGELRSLEVL DLSSNMLSGE IPNSLVNLRN LTALLLNDNK LSGQIPSGLA
NVTMLSSFNV SFNNLSGSLP LSNNLIKCSS VLGNPYLRPC HVFSLTVPTP DPGSATVAQG
YTVSPPSQSQ KSGNNGFNSI EIASIASASA IVSVLLALIV LFFYTRKWSP KSKIMGSTRK
EVTIFTDIGV PLTFENVVRA TGNFNASNCI GNGGFGATYK AEISPGVLVA IKRLAVGRFQ
GIQQFHAEIK TLGRLHHPNL VTLIGYHASE TEMFLIYNYL PGGNLEKFIQ ERSTRAADWR
ILHKIALDIA RALAYLHDQC VPRVLHRDVK PSNILLDDDF NAYLSDFGLA RLLGTSETHA
TTGVAGTFGY VAPEYAMTCR VSDKADVYSY GVVLLELLSD KKALDPSFSS FGNGFNIVAW
ACMLLKQGRA KEFFTAGLWD AGPHDDLVEV LHLAVVCTVD SLSTRPTMKQ VVRRLKQLQP
PSC
//
