ID A0A2G9H3Z3_9LAMI Unreviewed; 1198 AA.
AC A0A2G9H3Z3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Tyrosine kinase {ECO:0000313|EMBL:PIN12226.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:PIN12226.1};
GN ORFNames=CDL12_15173 {ECO:0000313|EMBL:PIN12226.1};
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:PIN12226.1, 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 -!- 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:PIN12226.1}.
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DR EMBL; NKXS01002749; PIN12226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9H3Z3; -.
DR STRING; 429701.A0A2G9H3Z3; -.
DR OrthoDB; 47962at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
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 CDD; cd06410; PB1_UP2; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF957; KINASE SUPERFAMILY WITH OCTICOSAPEPTIDE_PHOX_BEM1P DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PIN12226.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIN12226.1}.
FT DOMAIN 922..1187
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 953
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1198 AA; 131837 MW; 654744FDD9EA033D CRC64;
MKPSKNHNYM QGNSLEQGNE DLDPEPLGHG ADTPGHANGS LKSPETNFAE PKPVLNYSIQ
TGEEFALEFM RDRVNPRHPL PPNITGDPSY ATGYLELKGI LGISHTGSES GSDVSVIATT
GKSSREFERT NLSIHGNWGN HGSSQSMRHA SSDCSHHTLM YASSGASDSS ALKLKILCSF
GGRILPRPSD AKLRYVGGET RIIRISKDIT WQELWEKTTA IYDETHTIKY QLPGEDLDAL
VSVSSDEDLL NMMEECNVLE VGEGSKKLRM FLFSLGDLED AHFSLTNTDG DSEIKYVVAV
NGMDAASRKG STLRGLASSS GNNLNELDTL NVERDTCRTT TEFVGINTSN MGGFAVPSTA
TDPSTSIFPN SFKFYEPDLH FYNGHPVHRH EDKQHPPQFG YNFHPPYETP SESAIPQSSY
ETVSQQKGFA GKSLSSLGTQ GTEMQEKELK LKIDGSIPPE SGTNQMLANE HFVAYNGNTK
VSFPDEEAPI AVPKLDREFS SKTSKSEVMP QEPLQVSKPL DAVNPSQLPI SSGNDFCTSG
IPGPESINSE SDPTDFGYFE SSFPPQRVFY SERIPREQAG RHSRISKSDD SHSSQLLANQ
SSTDITQQDL VPGSVERLQN GNVIPTEQSI AISPVESETF DNGHPRTQTV DKLDVKDSVH
VNQVPVAEAE AGLKLPAVGH EDSVKHYEDP ITHWVDGVGS QSNANNAHGH PQPSAWTGAE
EESRAADPRT EQGDILIDIN DRFPRDLLSD IFSKAILSDS SSDIGRLQKD GAGLSVNIEN
HEPKHWSFFQ RLAGDEFTRR DVSLIDQDHV VFSSGLAKGE EASLAYDFAP PNHREAQDNY
AEDNQKGIPG GDGAVGVALH SNNNASQVKV SESIQYDDLM DNMRIQDSDY EDGMGKIGLP
PVDPSLVDFD INSLQIIHNL DLEELKELGS GTFGTVYHGK WRGSDVAIKR IKKSCFTGRQ
SEQERLTVEF WREAEILSQL HHPNVVAFYG VVQDGPGGTL ATVTEYMVDG SLRHVLVRKD
RHLDRRKRLI IAMDAAFGME YLHSKNIVHF DLKCDNLLVN LKDPSRPICK VGDFGLSKIK
RNTLVSGGVR GTLPWMAPEL LNGSSNKVSE KVDVFSFGIV LWEILTGEEP YANMHYGAII
GGIVNNTLRP TIPSYCDQEW RRLMEQCWAP NPAVRPSFTE IASRLRVMSA SAQPRKAS
//
