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Database: UniProt
Entry: A0A2G9G9A4_9LAMI
LinkDB: A0A2G9G9A4_9LAMI
Original site: A0A2G9G9A4_9LAMI 
ID   A0A2G9G9A4_9LAMI        Unreviewed;      1104 AA.
AC   A0A2G9G9A4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=CDL12_25615 {ECO:0000313|EMBL:PIN01874.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN01874.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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:PIN01874.1}.
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DR   EMBL; NKXS01006192; PIN01874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9G9A4; -.
DR   STRING; 429701.A0A2G9G9A4; -.
DR   OrthoDB; 455055at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051707; P:response to other organism; IEA:UniProt.
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; 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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR   PANTHER; PTHR27008:SF609; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 9.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00365; LRR_SD22; 8.
DR   SMART; SM00369; LRR_TYP; 13.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-like; 2.
DR   PROSITE; PS51450; LRR; 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:PIN01874.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:PIN01874.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:PIN01874.1};
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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1104
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013674836"
FT   TRANSMEM        773..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          829..1099
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   1104 AA;  122875 MW;  71BC69B8169F83B6 CRC64;
     MGFIRAHLFP HALFLAQCLL ACSATALTNI NTDKSALLAL KSRLSIDPSY VLYKNWSDSA
     SVCSWVGVTC GSRHQRVTAL DISAMGLAGD LPHEMGNLTF LGYLNLSSNN FHGILPEELA
     QLRRLKVIDF KFNNFTGEIP SWFRFLRELH FLNLRNNSFT GLLPNSISNV SKLEMLDLSF
     NSLWGKVPEE VGHLYNLKTL SMQFNKFNGA IPRAIFNISS LEILSLTGNN LSGELPADMC
     HGLPGLKRLY LSSNELEGQI PSNISQCSQL RLISMSYNKF SGTIPREIGN LRALEMLYLG
     ANYLTGEIPE ELGKLQKLKE LDIGTNFFIG SMPSAIFNIS SLERINIASC SLSGPLPLDM
     IGECLALENV ELSFNNITGT IPGSVGNLTK LHTFYVADNN LIGTIPKEIG NLHNLEVLDL
     AVNNLRGSIP KEIFNISTLR GIRVSGCLPS NFGYGLPNLQ ELRFDNNNLC GEIPHSISNS
     SKLTFIYFSE NQFSGLLPNS LGELTFLKHL FLNGNNFVAE SLELKFITSL TNCRYLRKLG
     LSNNNFNSIL PASIGNLSNS LWDFYCDNCG LHGNIPDEVG NLTNLIRLSL YSNQMTGSIP
     KTLGNLKHIQ GLGIFDNRIS GSIPDSLCGL EHLDSLSLFQ NQITGAIPDC IGKLTALRDL
     QNLVNLSLAH NRFAGSIPES TGKLVNLETL DLSHNNLSDN IPKSLEALRY LTYFDVSFND
     LSGEIPSGGP FKNFGSQFFM SNGGLCGDPR YGVPQCPISK VHKPKRRKLI LRVLYALLGV
     LALVFFLVLA YLLLRYRRKE VVKDKKDISY GTTRLRVSYY DLQQATEGFS ESHLLGICGF
     SSVYNGTFKN GEEVAVKVFN LELEGAFKSF DIECEVLRTL RYRNLCKVIK YMPNGSLEKR
     LYSDDYSLDF MQRINKMIDV ADALEYLHHG YSISIAHCDL KPSNVLLDQD MVSHLSDFGI
     AKLLCNGDSF AQTTTFATLG YIAPEYGTEG LVSIKCDVYS YGIMLMEVFT RMKPRSEAFT
     GDLRLRRWVK NVLPDGITKV MDPKLLNPEE DNSKEKLECL SSIMEVALNC STEIPGERIS
     MKDVAPHLNK IRVKLLEYFC RSNS
//
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