ID A0A1R3H7U9_COCAP Unreviewed; 1249 AA.
AC A0A1R3H7U9;
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=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=CCACVL1_21173 {ECO:0000313|EMBL:OMO66414.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO66414.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO66414.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO66414.1};
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.;
RT "Corchorus capsularis 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000327};
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 Evidence={ECO:0000256|ARBA:ARBA00000671};
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:OMO66414.1}.
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DR EMBL; AWWV01012528; OMO66414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3H7U9; -.
DR STRING; 210143.A0A1R3H7U9; -.
DR EnsemblPlants; OMO66414; OMO66414; CCACVL1_21173.
DR Gramene; OMO66414; OMO66414; CCACVL1_21173.
DR OMA; VKHVNDF; -.
DR OrthoDB; 460418at2759; -.
DR Proteomes; UP000188268; 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:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045274; WAK-like.
DR InterPro; IPR025287; WAK_GUB.
DR PANTHER; PTHR27005:SF187; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 15; 1.
DR PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR Pfam; PF13947; GUB_WAK_bind; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1249
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013113995"
FT TRANSMEM 282..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..635
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 956..1237
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 984
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1249 AA; 138290 MW; 79E1BB424059E8BA CRC64;
MAMPPLLILT MAMLFMLFYA DCVVSLKICP NCGRIPVPYP LSTGPDCGDP WYKVRCNAGT
LWLDAMNKSS YMITSINPMS QTLIIRPPGF AKNKCMAADF GSGGVFLDSN LPFNITDTNT
VMIMNCSALV LTEYAALNCS STSICHDYVK GNSEAKANCG TLPYCCWFLT GGTMHAYRIH
VRPERCSAYQ SFVNLDMDLP VNKWPQPGLE LEWVPPVEPK CKLPADCGGL LNSMCLPDPV
NVGQKRCLCK SGFQWDPIHG ICQDLKCKHG KSCKHKKNKT SMLGGAAMAA GAIVIGLIVT
IIIVYKQRKH CEREAEVSLT KAHKDLLSSN SGKLAKFFTS KEIAKATNNF SEDNLLGSGG
FGEVFKGILD DGTNIAVKRA KLGNTKGIDQ IINEVRILCQ VNHRNLVKLL GCCVELEQPI
LIYEFIPNGT LFDHLHRTTS GNVIQLHPLS WQRRLCIAYQ TAQGLAYLHS SVVPPIYHRD
IKSSNILLDE NLDAKVADFG LSRLGLSSAS HVTTCVQGTL GYLDPEYYLN FQLTDKSDVY
SFGVVLMELL TCKKAIDFNR DEEDVNLVVL SRRFLKEEKF MDVIDPFLLQ EAGKAELETM
KALAILAGSC LNEKRQNRPS MRTVVKEIEN CAAAIVHCSN CGKFPVPYPL STDPSCGDQA
YKIRCTAGVL WFDALRGSYM IVSINPLTQR MSLRPPGLTV NTCISSDITT QGIQLDEKRP
FNITSSNTIF LLNCIDAMLH LQPPIDCAPT SLCHNYIKDN AAVCIKAPPL CCMFKPGGLQ
SAYMVRVHDK GCLAYQSFVN LDSVHPPKKW PEPGLELAWA LPKEPVCNMP VDCKSLLHSK
CLADPMRIKR CLCHKGFKWD PINGLCQSAK CPPGKRCKKP KKKAVLICGV AAALGGVSLA
IMAGILVYKQ RIRQSVKKEV HKNIIKERHE ILNAKNHGKS ARIFTGKEII KATDNFSTAN
LIGSGGFGEV FKGVFDDGTI TAIKRAKLGN TKGTDQVLNE VRILCQVNHR SLVRLLGCCV
ELDQPLMIYE FIPNGTLFEH LHCNLSGKFA PLTWKLRLRI AHQTAEGLAY LHSAAVPPIY
HRDVKSSNIL LDEKLNAKVS DFGLSRLVET TETGDHHMYT SAQGTLGYLD PEYYRSFQLT
DKSDVYSFGV VLLEILTAKK AIDFNREEEN VNLVVYMKTM MDEDRLMDAV DPVIKEGASN
LQLETIKAFG LLAGSCLDEK RQNRPSMKEV ADEIEYIINI AKGEVVSEV
//
