ID A0A2P5BD11_PARAD Unreviewed; 999 AA.
AC A0A2P5BD11;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=PanWU01x14_249660 {ECO:0000313|EMBL:PON46670.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON46670.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
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:PON46670.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXTB01000307; PON46670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5BD11; -.
DR STRING; 3476.A0A2P5BD11; -.
DR OrthoDB; 391466at2759; -.
DR Proteomes; UP000237105; 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 GO; GO:0099402; P:plant organ development; IEA:UniProt.
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; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF15; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 5.
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:PON46670.1};
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:UP000237105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:PON46670.1};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..999
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015200044"
FT TRANSMEM 625..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 686..969
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 999 AA; 110088 MW; B49465CB25742F7B CRC64;
MLLFLPNFFF FFFLLLISSP VTLCLNQEGL YLQRVKNSLD DPDSVLSSWN DRDDTPCSWY
GVSCDPTSRS VYSVNLSNAN VAGEFPSVVC RLQNLTFLSL FNNSINSTLP LDISTCQALR
HLDLSQNLLT GSLPNTLADL QELLYMDLTG NNFSGEIPVS FGRFQKLEVI SLVYNLFDGS
IPPFLGNVTT LKMLNLSYNP FLPGRIPPEF GNLTNLEVLW LTDCNLVGEI PDSLGHLKRL
KDLDLAINNL HGPIPSSLVE LTSVVQIELY NNSLSGELPP GMSNLRSLRL LDASMNELTG
TIPDELCKLQ LESLNLYENR FQGRLPEGIA YSPALYELRI FRNFLSGELP RNLGKNSPLR
WLDVSSNNFS GEIPATLCEK GELEELLMIY NSFSGQIPAS LGDCESLTRV RLGHNQLSGE
VPAGVWGLPH VYLLELAENS FSGSIAKTIA GAANLSLLII SKNNFTGPIP DEIGWVENLV
ELLGNDNGLN GPLPESIVNL GQLGTLDLHN NELSGHLPTK MEYWKKLNEL NLANNQLSGK
IPGGIGKLEV LNYLDLSENQ FSGEVPLGLQ NLKLNQLNLS SNRLSGELPP LLAKDTYKNS
FLDNPGLCGS LKGLCDSSTE VKSQGYIWVL RSMFILASLV FVVGVVLFYL KYRKFKNAKR
AIDKSKWTLM SFHKLGFSEY EILDCLDEDN VIGSGSSGKV YKVVLSNGEA VAVKKLWGAV
KKDCESEDLE KGRPQNDGFE AEVEILGKIR HKSIVKLWCC CTTRDCKLLV YEYMPNGSLG
DLLHGSKGGL LDWPTRFKIA VDAAEGLSYL HHDCVPPIVH RDVKSNNILL DGDFGARVAD
FGVAKVVDLS GKGPKSMSVI AGSCGYIAPE YAYTLRVNEK SDIYSFGVVI LELITGRLPI
DPEFGEKDLV KWVCTTLDQK GVDHVIDSKL DSCYKEEICT VLNIGLLCTS PLPINRPSMR
RVVKLLQEVG GAAEMKAAKK DGKLSPYYYE DASDQGSVA
//
