ID A0A1R3IXB2_COCAP Unreviewed; 765 AA.
AC A0A1R3IXB2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 08-NOV-2023, 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=CCACVL1_09183 {ECO:0000313|EMBL:OMO87227.1};
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:OMO87227.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO87227.1, 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:OMO87227.1};
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; 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PDPK1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010006}.
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:OMO87227.1}.
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DR EMBL; AWWV01009253; OMO87227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3IXB2; -.
DR STRING; 210143.A0A1R3IXB2; -.
DR EnsemblPlants; OMO87227; OMO87227; CCACVL1_09183.
DR Gramene; OMO87227; OMO87227; CCACVL1_09183.
DR OMA; WANISQH; -.
DR OrthoDB; 208777at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd05581; STKc_PDK1; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR033931; PDK1-typ_PH.
DR InterPro; IPR039046; PDPK1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF163; 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1-RELATED; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF14593; PH_3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000188268}.
FT DOMAIN 54..321
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 84733 MW; C99FCE099A700BCC CRC64;
MEKDFDSKLK IQGTNNNDNN NSSNSSNGGA SNNVQRSKSF AFRAPQENFT IQDFELGKIY
GVGSYSKVVR AKKKDTGMVY ALKIMDKKFI TKENKTAYVK LERIVLDQLD HPGVVRLYFT
FQDTFSLYMA LESCEGGELF DQITRKGRLP EDEARFYAAE VVDALEYIHS MGLIHRDIKP
ENLLLTTDGH IKIADFGSVK PMQDSRITVL PNAASDDKAC TFVGTAAYVP PEVLNSSPAT
FGNDLWALGC TLYQMLSGTS PFKDASEWLI FQRIIARDIR FPNYFSEEAR DLIDRLLDID
PSRRPGAGPE GYAAVKMHPF FRGVDWSNLR SQTPPRLALE TGAQSGDGDD HNDSSWNPTH
IGDGSVRQND GNGGASSSES SGHITRLASI DSFDSKWQQF LDQGESVLMI SMVKKLQKLS
SKKVQLILTN KPKLIYVDPS KLVVKGNIIW SDNSNDLSVQ VTSPSHFKIC TPKKVLSFED
AKQRAWQWKK AIEGLQNRFM MKTTAKLCIY RAVSPLKDFK KTSLNIIKEV NRRGPYIGLI
TVIPTEENSF FATRSFKPDP KHPFVDLSGR RFRVGKVQGK KVIYVRCGVG MVNAAAVTQQ
MLDLFDVEGI IHFGIAGNVN NSMSIGDVSI PGQVAHTGIW DWVNPQGKVD QDDVAQLDIG
SYNVPKGNGT NLLGHIGYSK EQFFSESGNP NTAQPLLWAN ISQHWLQLAF NFGTSLSNGF
PVIVVRGMSD LAGRQQGENA IGEFGSLAAI NTAKAVLEFI GKLPS
//
