ID A0A2G9HPN1_9LAMI Unreviewed; 1169 AA.
AC A0A2G9HPN1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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_07832 {ECO:0000313|EMBL:PIN19484.1};
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:PIN19484.1, 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:PIN19484.1}.
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DR EMBL; NKXS01001269; PIN19484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9HPN1; -.
DR STRING; 429701.A0A2G9HPN1; -.
DR OrthoDB; 1067631at2759; -.
DR Proteomes; UP000231279; 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:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099402; P:plant organ development; IEA:UniProt.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF585; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-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:PIN19484.1};
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:UP000231279};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:PIN19484.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIN19484.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 843..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 886..1166
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 914
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1169 AA; 129511 MW; DEE7326D2ACFA83E CRC64;
MEELLKGKEN ARTSSPVIHN LGPKNGNDSS NVLNITTDQS ALIVFKSQFE HNHSNILARN
WSSDTPICSW IGVTCSSRHQ RVVAISFSNM DLSGIIPPQL GNLSFLVSLD MSGNKLHGNL
PKELAQLKRL KFISFSFNRF SGKIPSFFEA MPNLQHLRLR NCSFTGAIPP SLSNISKLET
LDLTYNTLEG MIPVEIGNLG NLKTLLLSRN WLSGPIPASI FNCSTLKKAD FSYNNLSGIL
PANMCRNLPS LKYFSVHSNQ LYGHIPSTID ECSQLQDLEL QLNQFNGRVP KQIGNLSMLL
YLDLGDNNFK GEIPEEIGNP GNLESLALDN VGLNGPIPSF IYNISTLQWL HLGRNNLTGN
LPMEICLQLP AIHGLYLNEN QLTGSIPREL GNCSSLVELY LGENMFTGEI PSEIGNLLNL
ETLNLQTNYL TYIPAAIFNI STLKILRVPE NHFTGSLPST MGQNLPSLRN LVLMKNQFTG
PIPDSISNAS SLVCVTFFAN KLTGRVPNSL GKLKFLDFLN LGGNEFTSES LEMSFLTSLT
NCRHLRIAWM YSNSFSGYLP NSIGNFSSTL EQLDLKNSRI KGGIPKEIGN ITNLAFLYMD
DNEFTGFVPF TIQNLKNLQL LRLRGNKLSG TIPDGLCHLP NLGELTLSNN KLYGPLPACL
GNLTSLRYLK LDSNELNSSI SPTIGGLKDL LEFNLFSNFL SGPLPPEIGN FKAVTLMDLS
MNELSGSIPS TIGGMSSLIH LSLAQNRLQG PIPDSINKML SLERLDLSHN NFTGLIPKSM
EALRYLHYLN LSFNKLTGEI PNGGPFAYFN HESFILNDAL CGPPRLQVPT CPSHHHHRSK
QKAVLRASLI SFASVSTIVI LIISFFLIKR LRKNEDPNLQ RATNGFSVAN LLGVGSFGSV
YKGIFSDRTT VAVKVFNLQI EGAFKSFDTE CEILRNLRHR NLAKVISSCS NIDFRALLLE
YMPNGSLENW LYCRERPLNL SQRLSIMIDV ATAVEYLHHG YAMPVVHCDL KPNNVLLDDA
MVAHVSDFGI AKLVNAGDNA ILTKTLATFG YIAPEYGSEG LVSTKCDVYS FGIMLMETFA
RKRPTDDLFT AGLSLRDWIY DSYPQSLGHV IDDTLLNPDE ESFDKNVECI SLIMKLALSC
SSELPGERTN MKDTLAILQK IRKQFFPHL
//
