ID A0A1R3KBZ0_9ROSI Unreviewed; 1585 AA.
AC A0A1R3KBZ0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_09510 {ECO:0000313|EMBL:OMP04564.1};
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:OMP04564.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:OMP04564.1}.
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DR EMBL; AWUE01014242; OMP04564.1; -; Genomic_DNA.
DR STRING; 93759.A0A1R3KBZ0; -.
DR OrthoDB; 1127948at2759; -.
DR Proteomes; UP000187203; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 3.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd01098; PAN_AP_plant; 2.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 3.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR021820; S-locus_recpt_kinase_C.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32444:SF183; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 3.
DR Pfam; PF11883; DUF3403; 1.
DR Pfam; PF08276; PAN_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 3.
DR Pfam; PF00954; S_locus_glycop; 2.
DR SMART; SM00108; B_lectin; 3.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00473; PAN_AP; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 3.
DR PROSITE; PS50927; BULB_LECTIN; 3.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50948; PAN; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000187203};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..140
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 221..303
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 406..527
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 601..892
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 954..1075
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 1214..1250
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1270..1351
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
SQ SEQUENCE 1585 AA; 177903 MW; C9A2CE3915BB5CC2 CRC64;
MPNSNFVKLV QELVLFSGSV DFIDTTGSIR DGETIVSASE IFELGFFSPG DTDKRYLGIW
YKKSVKTVVW IANREIPLND SSGIVKVTNH GILVLLSGKG ITIWSSHSSR PTRNPVAQLL
DSGNLVVKDE IDKSIIWQNF DYHNGDLKHF RWIDQKQDWR HSRLLQEDTC DGYGLCGAYG
FCNSDDSPIC TCLNGFVPRN KDEWGKEQWT SGCMRETPIS CSGDGYYREI SGVKFPDSRQ
PPQSYSSMNI DQCKIQCTKN CSCSAYAILD IRDGGSGCQL WFGDLIDLKH SAGRGQSIYL
RIAASELGSM QGFSERSYKY DEQKEDLELP LFDFATIARA TSNFSPNNKL GEGGFGSVYR
GILEDEQEIA VKRLSKGSTQ GDNEFRNEVE QIAKVQHRNL VKLLVVDTLN TTQVIRDGES
IVSANGRYEL GFFSPGASNK KYLGIWYKPI PVKTAVWVAN RDISLNNSSG VLKLTKQGIL
VLLNHNGSTI WSSNSSRPAR NPVAQLLDSG NLVVKEENDS NPGNFLWQSF DYPTDTMLQG
MKLGRNLITG LDRYLTSWKS LDDPSPGNFT YRFEIGGFPE LILREGSIIR FRPGPWNGLR
FSGTPELRPN PFFTVNVVIN EKEGIMKDGQ EIAVKRLSKT SGQGLTEFKN EVIHISKLQH
RNLVKLLGCC IQAEEKMLIY EFMPNKSLDF FIFDETQSNR LDWPMRYNII NGIARGLLYL
HQDSRQRIIH RDMKAGNVLL DYEMNPKISD FGLARSFGEK DFEASTKKVV GTFGYMAPEY
AIDGLYSIKS DVFSFGVLVL EIVSGKRNRG FCHPDHQLNL LGHAWRLFTE EKPMELIEPA
IQETCNPSQV LRSIHVGLLC VQHSPEDRPN MSNVVLMLGS QGSLSQPKQP GFFTERDLVD
QSSTSSTTQK LLSSNDFPIM MFVRERISSM ETFAKISLSF FLVSNLTLAI AVDTLTLNAT
QSIRDGETLV SEGGNFELGF FSPGSSTNRY LGIWYSNISV QTVVWVANRE SPLKDFSGIL
KLTNKGILVL QTQKGNTVWS SNSSRSAHNP VAKLLNSGNL IVKEENENDP ENFLWQSFDY
PSDTLLQGMK LGRNLITGLD RYLTSWKSPD DPSPGNFTYR YEIGGFPECV LREGSIVRFR
PGPWNGVRFS GTPELKPNSL FTFGVVINEK EVYYSYKLRN SSILSMMVLT QKGYWQRHKW
IEETKAWDVY VTVQMDECDN YGLCGSYGSC NSLDSPRCSC LKGFVPKFPE KWDSNKDWSS
GCVRKTPLNC STDGYLKYSG VKLPDSRKSW FDFRLNLEEC RNLCMRNCSC TAYSNLDVRN
GGSGCLLWFV DLVDIQQFTE NGQEIYVRMA ASELVSILGI ALVVYFWRKT GNKKPEVSES
ESHPEGNSSV KKHKEDLELP LFDLAAIVCA TNSFSTTNKL GEGGFGSVYK VTICGYMAPE
YAIDGLYSIK SDVFSFGVMV LEIVSGKRNR GFCHPEHQLN LLGHAWRLFG VGDSLDLIES
AIKETCNHSE VLRSIHVGLL CVQHSPEDRP NMSNVVLMLG SQGPLLQPKQ PGFFTQRDLI
ESSSSSTGNK LLSSNDFTIT MMEAR
//
