ID A0A2P5B0Y0_TREOI Unreviewed; 919 AA.
AC A0A2P5B0Y0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=TorRG33x02_335750 {ECO:0000313|EMBL:PON42470.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON42470.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) 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:PON42470.1}.
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DR EMBL; JXTC01000636; PON42470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5B0Y0; -.
DR STRING; 63057.A0A2P5B0Y0; -.
DR InParanoid; A0A2P5B0Y0; -.
DR OrthoDB; 376508at2759; -.
DR Proteomes; UP000237000; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; PTHR27008; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF597; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PON42470.1};
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:UP000237000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:PON42470.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 719..919
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 919 AA; 100397 MW; 5FFFF32F664678B2 CRC64;
MILQNHANYS AFWPMFLSFI LIFSMNLLLM NPTSIIASAM GNETDRFALL KFKDSISNDP
YGVLRSWNDS SINFCNWPGI ACSRRHQRVT SLNLEDCTLR GTISPYIGNL SFLRVVNLGN
NKFYGEIPPQ VGHLFRLQRL NLSINMLEGE IPANLSYCSN LTVLILALNN LSGVIPLELG
STEKLSVLYL GGNNLTGGIP PSLGNISSLT RVDLARNNLV GSIPHELGRL KSLIRFLLWS
NFLYGTIPPS LYNISSLSEF IITENQFRGT LPPNIGLTLP NIKVFAIGGN NFSGMIPESF
SNASKLQSFD IGQNSFVGKV PSNLGNLPDL SIFSLKDNML GSHLANSLDF IASLTNCSKL
KILSLTENNF GGVIPKHVAN LSTQLTRFYL GGNQVSGNIP ATLENLVNLT ALGLDYNLFT
GVIPSSLGKL PNLQLLALNW NALSGKIPSS IGNLTKIFGL TLPGNKLEGS IPSDIANCKK
LQTFDISDNS LSGTIPKELF GPSSSFILVN LSRNSLIGSI PVEVSNLKNI YALDLSENNL
TSEIPETIGD CESLEFLYLQ GNFFQSTLPS SLASLKGLRY LDLSQNKLFG KIPNDLQNLH
VLLYLNLSFN DLEGEVPNKG VFQNTSAISI VGNTKLCGGV PKLQLPPCPI KASKKQQNTS
RLKLTIIVVC AAAFSLSFLS FLIFYWRRKS TSTSSSAPST ISFLSKVSYK SLYQATNGFS
QSMLIGTGSF GSVYKGIIDE EESPIAVKVF NLQQKGASKS FIAECNALRN VRHRNLVKIL
TCCSSMDFNN NDFKALVFEY MSNGSLEKWL HPVTSYENQS MSLNLIQRLN VVADVATAIH
YLHDHCDQPI IHCDLKPSNV LLDNDMIAHV GDFGLARLML NTNGLSESQS STIGIKGTIG
YAPPGTHLAL ISHKFCAYI
//
