ID A0A151WZU4_9HYME Unreviewed; 1498 AA.
AC A0A151WZU4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN ORFNames=ALC60_07439 {ECO:0000313|EMBL:KYQ53429.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ53429.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ53429.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ53429.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ53429.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
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 ECO:0000256|RuleBase:RU000312};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; KQ982629; KYQ53429.1; -; Genomic_DNA.
DR STRING; 64791.A0A151WZU4; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR000998; MAM_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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF604; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF12810; Gly_rich; 1.
DR Pfam; PF00629; MAM; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50060; MAM_2; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Kinase {ECO:0000313|EMBL:KYQ53429.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|RuleBase:RU000312, ECO:0000313|EMBL:KYQ53429.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Transferase {ECO:0000313|EMBL:KYQ53429.1};
KW Transmembrane {ECO:0000256|RuleBase:RU000312, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 861..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1139..1157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..232
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 280..460
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 946..1219
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1328..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 977
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 238..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 245..263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1498 AA; 165291 MW; D27991ACC9525CF8 CRC64;
MINDTRPRLA TTIAGYSQTS RTCNRRHVSV HNGGSGRLLF GIVLISWYIT VTCGSKVSMW
HGKSFKDLLA AVPSKHSPHY SQMGYCDLDT DCDWSWNDTH GFKKVKARTS PSRAFPNTDS
NNSSNGHFLW FSGKGDAHIW SKSIPRTGPR CRIEFSLYMV EMENGFINLV IQTNNMSSIA
VTKSGNNTSM WKKISFSLRA IDQSYKLVLE VYVPYSNSSI GVDNLRLVDC FPEFIGDCTE
DMFRCSNGSC LNRTRICDFT KDCAHGEDEG LECDKIPKNA RCNFEDGWCG WTNVPERPLN
WTLHKGPTPT ERTGPSYDHT YRNETGTYAF VNMASKDVPV PITYGSRGTI TSPLYNPTPP
YTSNPKSPYY KSCQVRFFYH KYGPHAASLG LFLVQVRPHG NHTENLWWSY GTNSDIWYNE
AVALPDIKYR YHLQFEASRG YSAKSDIAID DISLSPECFG IGVPREVVGN FDYYTPIIES
EIMPPQHPDF VNETVIRITT CGASGRTGPT VEKCTEKYNN TNVELFVPSS TQEEERSAFN
LYGVQRWTAP RGEYYTLIAV GARGGLGSGN TGITLGAFVR GVVELQKGDQ LYFMVGQEGT
DACAKNLGLK ATVCQSNQFA DLSPQQTSSK MREVKNIEFK NPGGGGGGAT AIFTLKANGD
PEPILIAGGG GGLGLNPSMD NGLQHGRGPF PVGRLSSSPS NFSERMGGPG ASWNGTWHNF
QRKAWGTPLI YGGKGGIGCE SGNKNYANGG FGGGGGGCQS GGGGGGYIGG NAGQNDGSGE
GGYSYASQKL TDIYFKTAAH SGQGEVFVIP AISGCGCDYR CVALDQYLSE TKCLCPQGWL
LSNDSKSCIM VDDSKDGHQT YMIQLVVVII GLLTIIGICL ISYKRYQKQK ALSHRRQVMF
GNGTELAALR PGHQSDTMMT EYNPNYEFAG NLYSFKDLPQ IPRECIDLVK PLGQGAFGEV
FQGVYKYGGD EHPVAVKTLP SLSTTQAEAD FMMEALIMSK FNHPNIVHFI GVSFDKHPRY
IVLELLAGGD LKNFLREERP RSDRPTSLTM LDLIMCGYDV ANGCKYMEEA RFIHRDIAAR
NCLLTTKAPG RTVKIADFGM ARDIYRSDYY RKGGKAMLPI KWMPPESFLD GIFTTKTDVW
AFGVLLWEIM SFGYMPYTGC ANREVMSMVQ SGGRLEKPAG CPDPIYGIMT RCWHPRPDDR
PSFSTIAERI GYCLQDPDVI NKPTPNFDIL PHICDREITV MRPDPEAECI NVRSNLDGGY
IQPRVTNPRS VARHVDQAMG GTAYDSENEK SIENCKYGES YAKSTGCQQG FSCNTCDSSM
DTFEQIYNSD NDEDRDDDVI ENSKDKSRID QDRQESRAIH RNSDIEDHDN VDNGNNRPED
ECHLTANIDS AITDRKNGNE STTTTDTNSD SLIAQSSDTP PDTITNSSPN TRSCSPNRII
GLNANVSNVN GMVKKNTLKA TLSLDPSALC RGTIPYEKIT TRTQRSSTPG SMELRKVT
//
