ID A0A0T6BGX6_9SCAR Unreviewed; 1309 AA.
AC A0A0T6BGX6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:KRT86135.1};
GN ORFNames=AMK59_2252 {ECO:0000313|EMBL:KRT86135.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT86135.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT86135.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT86135.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT86135.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
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:KRT86135.1}.
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DR EMBL; LJIG01000805; KRT86135.1; -; Genomic_DNA.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000051574; 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:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06366; PBP1_GABAb_receptor; 1.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF489; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR01176; GABABRECEPTR.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 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; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:KRT86135.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000051574};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:KRT86135.1};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1309
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006668675"
FT TRANSMEM 860..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 922..1195
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 955
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1309 AA; 150295 MW; 87A3593D77C2411E CRC64;
MLFHNFLRDH QILLAICLSL LINSPAVTGN RKCLKLPQEV PRRYIHYEGV SLNLTIESSN
RPTHQIISYI FKIFVQEMLG YPNVNVIDIV DDFDVDSIVT RLSGPVSENH RKSIPKSVIN
LEVWIPPHKD MVDLLRSTTV KEYGILRPPS TFGWFIPKSL TRHITEIDRM WHHEYGSIPW
TMFNNRDFIS AFVITNQTLR QDIERLSMVN SDKKIYYCND KEYCKNGYYT PETCLTQDCA
LLLAPYFNGT EYVIDQIDRE NLKVKVLWLG DNLKTAMNMI NATYLANSVN KSFVVLSWSP
SEIIYPEDNY INIDFRQCDP TDVNISHPLV DVNDMCPYEM WKIEKLMWNK LEDQAPVVYD
TMTKIHFNRT DYQNLLDIYY KFYGKSYEQM ACEWLRRNQN WATIYWTIPT ETVPTIHIGG
IFPIQSTSYK GTGIVHGARM AIKAANELIF TNYKLSMYVL DGQCKAEKVM KAFIDYIKDE
AALKTLVGVL GPACSETVEP IASVSRLFRT LVISYSAEGA SFADREKYPY FFRTIGSNTE
FMFVYLELMK QMKWNRVAAL TEDGQKYTEY LSVMQNLLMD NGISFIANVK FPRERKMLPM
TTYLETLKKK RSKIIIADIN DEAARAVMCE ASKLEMTMKH GYVWFLPSWL NETWYNTTYY
NQRFNESVDC PTNVMVNAIN GYFSITHSYW APNDAIMQEN RTVAEWKKSY REKTNNITSD
YAGFAYDAVW TYALALDKLI RHDPEALTDL HSENATKKLV KYVQETDFNG VSGKIKFRGG
PSRFSTTIHV TQWCNHTRTI VGWFYPNITD NSTEILGGVL NLNLTSIKWM SGRVPDDGRE
PADSCLVDGV ARALNVSCEW AMVLLNVVFC SGLIGMIAFA FCYYKKKLDN RISKTQLYMQ
HLGLDMTNLD DLDKWEIPRE HVVINRKLGQ GAFGTVYGGE ALIDPENGWV AVAVKTLKMG
STAEEKIDFL SEAEAMKRFD HKNVVRLLGL CTRNEPVYTI MEFMLYGDLK TFLLARRHLV
RTKSEEYMEV SSKKLTSMAL DIARALSYLA EKKYVHRDVA SRNCLVNASR VVKLADFGMT
RAMYESDYYK FNRKGMLPVR WMAPESLSLG VFSTSSDIWS YGVLLYEIIT FGSFPFQGLS
NNQVLDYVKN GHTLDIPSGV KPQLEVFLKS CWNQESKRRP KASEIVEFLA NNPQLISPCI
EGPIAAVEME GTDDLEVHLP GEFRKQSSVT SRHFPNGDIT RSQTIQINNE ADMIQLEHVC
TREPLLKSST SFTGNTTGYV HLQSSQPDLL SDSEIDYSQH NGNLYTKCN
//
