ID A0A2I0A0Z4_9ASPA Unreviewed; 992 AA.
AC A0A2I0A0Z4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, 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=AXF42_Ash010894 {ECO:0000313|EMBL:PKA49209.1};
OS Apostasia shenzhenica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Apostasioideae; Apostasia.
OX NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA49209.1, ECO:0000313|Proteomes:UP000236161};
RN [1] {ECO:0000313|EMBL:PKA49209.1, ECO:0000313|Proteomes:UP000236161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC TISSUE=Stem {ECO:0000313|EMBL:PKA49209.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; KZ452040; PKA49209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0A0Z4; -.
DR STRING; 1088818.A0A2I0A0Z4; -.
DR OrthoDB; 1210969at2759; -.
DR Proteomes; UP000236161; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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:SF281; OS06G0186100 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 2.
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:PKA49209.1};
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}; Receptor {ECO:0000313|EMBL:PKA49209.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PKA49209.1};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..992
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014130557"
FT TRANSMEM 588..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 662..975
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 690
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 992 AA; 106918 MW; 275F09FB1738DDCD CRC64;
MAAVHLLSIL LLLSIGLPAS AADGDRPALL SFLLGIRSLS QRSLLHWTSP DICNWTGVSC
HRTLPQRVLQ LDLSCRGLIG SISPAIVGLS FLQVLDLSNN LFSGEIPPEL GFLTGLKELT
LSSNLLSGTI PPQLSFLAEL VYLDLSGNQL AGHIPDALFC NSSNLQYVDL SNNSLAGEIP
IHPDSRLNEL RFLFLWSNVL EGPIPPSISN SSKLEGIDLK SNYLSGRLPV NLFGKLPSLQ
FLYLSYNYLS AAGNLDAFLR SLSNCSRMRE LELAGNDLVG EIPPSVGLLS VNFLQIHFEE
NRLTGQIPAN ISNLVNLTYL NLSNNALNGS IPPDISRLQR LERLYLSNNK LAGDIPQSFG
EMPHLGLLDI SGNILSGTIP NSFAELRQLR QLLLHGNRLS GNIPHSLGFC NKLEVLDLSH
NQLSGSIPAE VASLRSLKFY LNLSSNHLSG PLPPELSKMD MILAMDLSSN HLSGDIPPQL
GSCAALEYLN LSSNSLHGQL PGAIGALSSL KVLDLSSNQL AGSLPVSLQA SSTLQQLNLS
VNNLSGVIPD NGVFASLSGS SFAGNPLLCG HIAGVPSCSK PKRDRRRAVV PILLFAVIGT
PCLVFFAVGY PIIRRKRSGR LKFQLPIFHR VVIEHSDEAG NLCSSDYPRI SYRQLVEATG
GFSDEAVIGS GRFGRVYRGD LRNGTQIAVK ILDLNAGGAG EASGSFKREC EVLRRTRHRN
LIKIITACSR PDFKALVLPL MPNGNLEQWL YRAKQSPELQ LRGMSLETMV RVGSDVAEGM
AYLHHYSPVR VVHCDLKPSN VLLDGDMTAV VSDFGIARLV KRGGNDGGCG GGGAGDVGSL
ASCISTAGLL HGSVGYIAPE YGLGGHPSIH GDVYSFGVLL LEMITGKRPT DVVFHEGLTL
QEWVRSHYPD SLHAVVPQDL TLSTLKTLAD SDPFSFRKMN VFVITELVEL GLSCSQHSPS
LRPSMADVAH EMAVLKQELS RLSAQEASSF KA
//
