ID A0A2G9G1I7_9LAMI Unreviewed; 786 AA.
AC A0A2G9G1I7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Tyrosine kinase {ECO:0000313|EMBL:PIM99147.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:PIM99147.1};
GN ORFNames=CDL12_28362 {ECO:0000313|EMBL:PIM99147.1};
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:PIM99147.1, 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:PIM99147.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NKXS01007773; PIM99147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9G1I7; -.
DR STRING; 429701.A0A2G9G1I7; -.
DR OrthoDB; 722200at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR23257:SF878; PAS DOMAIN-CONTAINING PROTEIN TYROSINE KINASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50112; PAS; 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}; Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PIM99147.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIM99147.1}.
FT DOMAIN 109..159
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 516..776
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 273..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 786 AA; 87969 MW; 7A1380099C0B8B8A CRC64;
MCTFRTTMST AMDGGEESQA NLYRVLLDRF QSLEASHQKI KEQFKVLSEE KTRNTACKAS
LEKDVASDSE DMTSFPGWGC LQGAYFFRSP YRSVLEYMGH AVHVCRTGSG EIVYWNSAAK
KLFGYKDYEA VGRRVVELIF DEQHLPSALT VMRTVSTGKS WTGQLPLKKR SGQNFMAMVT
KTPLYEDGEL VGIITVSSDA NVFNGTNSGT MRTHQDHTNE QSKVRRINFK KIQWHPDPQI
VAVPQLASSV SNLASKVLLW KRGDVTCNAC RPTRETEEAE VESQDAKADR PPRAPILNSG
FSMFIGRSRT DVMSSEKEGS TSEFVQPSKI AEKLFSKLQI GPISNLAKDK DENIQQNGLE
DNPRKDGTSE RWYQRDSVES TSHLYDRDAN YHPEDAVIGI VDVAEREHLD MHMNTSVTNE
SSSTGAFSGA YQGCFEVHRP ADQMPGSGFQ SDRRKSIANL PNITLADSED VSPRQSGPRE
TQSTGGSCGN GPGSSPNKGD SDTHLVVDSE IRWEDLHLKE EIGQGSFAVV YRGVWNGSDV
AVKVYCGNQY NEDTLLDYKK EIDIMRKLRH PNVLLFMGAV CTEEKLAIVT EYMTRGSLFK
TLHRNGQSLD IRRRLRMAID VARGMNYLHH RNPPIVHRDL KSSNLLVDKS WTVKVGDFGL
SKLKDATFLT ARSGRGTPQW MAPEVLRNEP STEKSDVFSF GVILWELMTE RIPWSNLNFL
EVVGVVGFMD GRLDLPENID PQVSSLISQC WRSNPEDRPS FEEIIRKMTD IVHAGAGVTV
KTPSTP
//
