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Database: UniProt
Entry: A0A2C9V7D9_MANES
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ID   A0A2C9V7D9_MANES        Unreviewed;      1223 AA.
AC   A0A2C9V7D9;
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_10G113600 {ECO:0000313|EMBL:OAY39669.1};
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:OAY39669.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY39669.1, 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:OAY39669.1};
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. ROCO subfamily. {ECO:0000256|ARBA:ARBA00008171}.
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DR   EMBL; CM004396; OAY39669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9V7D9; -.
DR   EnsemblPlants; OAY39669; OAY39669; MANES_10G113600.
DR   Gramene; OAY39669; OAY39669; MANES_10G113600.
DR   Proteomes; UP000091857; Chromosome lg10.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047117; PERK1-13-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR47982; PROLINE-RICH RECEPTOR-LIKE PROTEIN KINASE PERK4; 1.
DR   PANTHER; PTHR47982:SF40; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          62..332
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1223 AA;  139082 MW;  DD4D4B2B8821AD2C CRC64;
     MNIAEDKMAS TESNSPSAPG EKQSVSPSQH TDLTESTSSE NFQADTLRKF SYSELAEATN
     SFSNSVCLGG GTFGIVYRGC LPIGDFAVKK LYYTGDGQHI EEFENRINVI GMARHRHLVS
     LIGYCCEEYD RLLVLEFVPN RSLRFHLRDA ERRSKLKWSK RMKIAIGSAK GLKYLHEYCE
     PKIIHGGIKS DNILLDRNFE PKVADFGLAI LLEGYDAARI YVDSNISDLE KISELDIYSF
     GVTLLELITG RKIYEDEYIV KWARPLMIKG DSINVDYDGL VDSTLKGQYD QSEVERIIYC
     IAASIYTPSS KLRPKMGQIL EALEGLIPHQ QLWAVEEHKE ITEVSNQLWS KATPSQGTGP
     KIMQIQEMPA ESNYSALEPA AMLSETSLEA TAQSAIPPSR LMKIYHILNK IVSRIKNSNV
     STIGVYGGEG IGKTTLSEAL KIQPAIRDMF HFVIWVSVPK VWNLREVQLQ IGRQLPLSGK
     KRINKYTLMS FLESVKFILI LDGVNGFISL NIVGIPEPTP ENGSKIVLTA RSAEVCDRMS
     ADLKINLEDL FRELFCENVG EIVYSFKLQP LAPKVVDLCC NHSHAIFLMS KALKDESDVR
     VWKNAVDMLS RQPASPEQEI ENIMVNILKF SYDRLPDDTT RRCLKNCALF FEKQEIARES
     LIDNWISDDL MDMYQKGQKV IETLVTAGLL ESSEDGQVFK LHEIDSSLLL EHVFPSRLFL
     RRKGSTLTEL LMDENWENSD EIYLMDNELT ELSEKLSSQA QALFLQRNLK LRKISDTFFQ
     DMLALQILNL SVTSIKFLPD SLFGLVNLKR LSLNRCVLLK LLPSRVGDLS CLEVLHLEGT
     AIVALPREVE HLKNLTSLKV SFREPVIFDH PKKMIPDGVI KKLSKLKKLR IDVSPEDGRW
     KASVVSIVLE VCTLTTLDTL QFYFPNVKLL SQINWDTTPT SPPLSHFKFI VGDHTNRIIC
     RLPHDVDVEL GRYDKCLKYV NGEGAPEEIK KVLRHTSAFF LDRNMSVEKL SEFEISNMMQ
     LKCCVAGECD KLQTIIEGDQ MVTSASGEVE LGLESLEYLY IYYAKSLRSI CEGRLDNSSF
     KKLKYLTLHM CPELTIIFMP ELLVNLSSLE ELIVDDCSEV KSLVHCKDNE HEIKHILPAL
     KKISFHFLPE LDSISDVVSI APRIEWMDFY YCPNLKSLPI SKAIHTKLRQ IKGEESWWQS
     LEWQNNEQDS NWEDIFTPVD EWD
//
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