ID A0A2G9HVY1_9LAMI Unreviewed; 1130 AA.
AC A0A2G9HVY1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:PIN21677.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:PIN21677.1};
GN ORFNames=CDL12_05593 {ECO:0000313|EMBL:PIN21677.1};
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:PIN21677.1, 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:PIN21677.1}.
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DR EMBL; NKXS01000904; PIN21677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9HVY1; -.
DR STRING; 429701.A0A2G9HVY1; -.
DR OrthoDB; 1211453at2759; -.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
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; PTHR45974:SF61; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00560; LRR_1; 10.
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; 6.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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:PIN21677.1};
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:PIN21677.1};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:PIN21677.1};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1130
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013842971"
FT TRANSMEM 754..777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 835..1117
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 791..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 121534 MW; 310856C850F02838 CRC64;
MPTASILFAV VLCATLTATL PCAGAVESEI LALLSFKQNL YDPLGAMDGW DASTPAAPCD
WRGILCYAGR VRELRMPRLK LGGQLSEQLG NLRQLRALSL HSNNLNGSIP RALSECTLLR
AVYLQYNSIA GEISPAFFSN ITNLQVLNLA HNLFSGEIPA ELPVRLRILD LSSNSFSGGI
PVKFSSSHKL QLFNLSFNRF SGAIPASIGM LQRLEHLWLD DNELQGTIPS AISNCSSLIH
FSAGGNMLSG IVPATMGSLK SLQVISLPRN QLSGVISSSL FCKMSALNAT VRVLDLSFNA
LTGIENNTGP ACASVLEVLS LHENQINSVF PDFLMTFLTL RVLDISGNLI SGILPGSVGN
LGILEEFRAG NNSLNGGIPE SITKCGLLRV LDLGKNRFSG SIPEFLGGMK NLTMLFLGGN
LFTGSIPASL GNLSLLELLD LSDNKLSGAV PQELMELSNL STLNLSNNRF SNDVLVNIGG
LEGLEVLNMS ACGFSGAIPS SIGNLFRLTT LDLSKQNLSG ELPIELFGLP SLQVVALEEN
SLSGNVPEGF SSLSSLQYLN LSSNAFSSQI PATYGFLRSL NVLSLAHNHI NGSIPVGLGS
CSGLQNLELR ENDLTGEIPA GFSHLSHLQR LDLGQNSLTC EIPESISNCS SLVVLLLDLN
HISGHIPDTL SQLSNLTELD VSSNNLTGVI PANLSLISTL QHLNLSANNL EGEIPGALAA
RFSDPSVYAM NKNLCGQPLN KNCQNVRRHG RKRLILFIVV AVAGSLLLLL CCCGYIYSLL
RWGKKLKEAA AGEKKRSPSP GSQGGRGSGE NGPPKLIMFN NKITYAETLE ATSQFDEENV
LSRGKYGLLF KATYADGMVL AIRRLPNTSI PENTFRKEAE SLGKIKHRNL TVLRGYYAGP
PPDMRLLVYD YMPNGNLATL LQEASHQEGH MLNWPMRHLI ALGIARGLAF LHSVPIIHGD
IKPQNVLFDA DFEAHLSEFG LDKLTIAAPA EASTSATPVG TLGYVAPEAT LTGEVTKEAD
VYSFGIVVLE ILTGKKPMMF TQDEDIVKWV NRQLQRGQVS ELLEPGLLEL DPESSEWEEF
LLGVKVGLLC TMPDPVERPS MADVVFMLEG CRLGPEMPSS ADPTTLPSPT
//
