ID W9S155_9ROSA Unreviewed; 1021 AA.
AC W9S155;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=L484_016090 {ECO:0000313|EMBL:EXC03886.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC03886.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-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. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; KE345419; EXC03886.1; -; Genomic_DNA.
DR RefSeq; XP_010105101.1; XM_010106799.1.
DR AlphaFoldDB; W9S155; -.
DR GeneID; 21399160; -.
DR KEGG; mnt:21399160; -.
DR eggNOG; ENOG502QQRQ; Eukaryota.
DR OrthoDB; 1203965at2759; -.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 4.
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; IPR025875; Leu-rich_rpt_4.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47988:SF76; MDIS1-INTERACTING RECEPTOR LIKE KINASE 2-LIKE; 1.
DR PANTHER; PTHR47988; SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1; 1.
DR Pfam; PF00560; LRR_1; 8.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 5.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EXC03886.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|EMBL:EXC03886.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EXC03886.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1021
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004931752"
FT TRANSMEM 641..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 693..967
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 965..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 110963 MW; 297A7E63FFDCA06C CRC64;
MRLLLLLLLL LHLRLSPATV AAARAVPEYK ALLSFKAALT DDPQSSLATW NASTLHCTWF
GITCDSRRHV TSLDLSGLNL SGSLSPELAY LRFLSNVSLA DNQFSGPIPA EISAISGLRL
LNLSNNVFNG TFPPELSQLK NLQILDLYNN NMTGDLPLDV VDLPNLRHLH LGGNYFSGAI
PKEYGRWEFL EYLAVSGNEL SGKIPPEIGS LTNLRELYIG YYNTYEGGLP AEIGNLSELV
RFDGANCALS GEIPPEIGKL QKLDTLFLQV NALSGSLTPE LGSLNSLKSM DLSNNMLSGE
IPPSFAELKN LTLLNLFRNK LHGAIPEFIG ELPELEVLQL WENNFTGSIP QGLGRNGKLQ
LLDLSSNKLT GTLPPDMCSG HRLHTLITLG NFLFGPIPES LGKCQSLSRI RMGENFLNGS
IPKGLFGLPK LTQVELQDNL LSGDFPESDG TFAANLGQIS LSNNQLSGSL PPSIGNFSGV
QKLLLDGNKF SGRIPPEIGR LQQVSKIDFS HNKFSGLITP EISQCKVLTF VDLSRNELSG
EIPNEITGMR ILNYLNLSRN HLVGNIPSSI ASMQSLTSVD FSYNNLSGLV PGTGQFSYFN
YTSFVGNPGL CGPYLGACKD GVSDGSHQSH VKGSLSSSLK LLLVIGLLVC SIAFAVAAII
KARSLKKASE SRAWKLTAFQ RLDFTVDEIL DCLKEDNIIG KGGAGIVYKG AMPNGENVAV
KRLPAMSRGS SHDHGFNAEI QTLGRIRHRH IVRLLGFCSN HETNLLVYEY MPNGSLGEVL
HGKKGGHLHW DTRYKIAIEA AKGLCYLHHD CSPLIVHRDV KSNNILLDSS FEAHVADFGL
AKFLQDSGTS ECMSAIAGSY GYIAPEYAYT LKVDEKSDVY SFGVVLLELV SGRKPVGEFG
DGVDIVQWVR KMTDSNKEGV LKILDPRLPS VPIHEVMHVF YVAMLCVEEQ AVERPTMREV
VQILTELPKP PGSKQGDSTT ITESSPPPVG GYDSSPTTVT KDNQQSTPQP PQSSPPDLLS
I
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