ID A0A1R3JV96_9ROSI Unreviewed; 1080 AA.
AC A0A1R3JV96;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=COLO4_13725 {ECO:0000313|EMBL:OMO98748.1};
OS Corchorus olitorius.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO98748.1, ECO:0000313|Proteomes:UP000187203};
RN [1] {ECO:0000313|Proteomes:UP000187203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA Shommy N.S.;
RT "Corchorus olitorius genome sequencing.";
RL Submitted (SEP-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO98748.1}.
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DR EMBL; AWUE01015262; OMO98748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JV96; -.
DR STRING; 93759.A0A1R3JV96; -.
DR OrthoDB; 457890at2759; -.
DR Proteomes; UP000187203; Unassembled WGS sequence.
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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 6.
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:SF69; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EXS; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 8.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 9.
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:UP000187203};
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 719..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 787..1073
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 816
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1080 AA; 118041 MW; B4979C6467C427C3 CRC64;
MARPSHFVRS YFFFFFFFFF FLFSPRTLFV TSISPDGEAL LSLLSGADPS AKASSSILSS
WNPKSQTPCS WQGITCSPQD TVISLSLPNT FLNLSSLPPQ LSSLSSLQLL NLSSTNISGT
IPPSFGQLTH LRLLDLSSNS LSGPIPQQLG QLSLLQFLFL NSNRLTGRIP QQLANLTSLQ
VLCLQDNLLN GSIPSQLGSL VSLQQFRVGG NPYLTGEIPS QLGLLTNLTT FGAAATGLSG
VIPPTFGNLI NLQTLALYDT EVFGSIPPEL GMCSELRNLY LHMNKLTGTI PPQLGKLQKL
TSLLLWGNAL SGSIPPELSN CSSLVVLDAS ANDLSGEIPG DIGKLVVLEQ LHLSDNALTG
LIPWQLSNCS SLTALQLDKN QLSGRIPWQV GNLKYLQSFF LWGNSVSGTI PSSFGNCTEL
YALDLSRNKL TGSIPEEIFS LKKLSKLLLL GNSLSGGLPK SVANCQSLVR LRLGENQLSG
QIPKEIGQLQ NLVFLDLYMN HFSGGLPHEI ANITVLELLD VHNNYITGEI PSQLGELVNL
EQLDLSRNSF TGEIPSSFGN FSYLNKLILN NNLLTGSIPK SFRNLQKLTL LDLSYNSLSG
EIPPEIGYVT SLTISLDLSS NSFTGEIPES MSSLTQLQSL DLSHNMLHGR IKVLGSLTSL
TSLNISFNNF SGPIPVTPFF RTLSSSSYLE NPSLCESLDG STCSSRLIRK NGLRSAKTVA
LISVILASVT IAVLALWFLV TRNHRYMVEK SAGASSSSPG AEDFSYPWTF IPFQKLNFTI
DNILDCLKDE NVIGKGCSGV VYKAEMPSGD LIAVKKLWKT KRDEEPAVDS FAAEIQILGH
IRHRNIVRLL GYCSNKSVKL LLYNYIPNGN LQQLLRGNRN LDWETRYKIA VGSAQGLAYL
HHDCVPAILH RDVKCNNILL DSKYEAYLAD FGLAKLMNSP NYHHAMSRVA GSYEYGYTMN
ITEKSDVYSY GVVLLEILSG RSAVESQVGD GMHIVEWVKK KMGSFEPAAS ILDTKLQGMP
DQMVQEMLQT LGIAMFCVNS SPAERPTMKE VVALLMEVKS PPEEWGKTSQ PLIKQSSNQS
//
