ID F4WYJ6_ACREC Unreviewed; 1285 AA.
AC F4WYJ6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Discoidin domain-containing receptor 2 {ECO:0000313|EMBL:EGI60728.1};
DE Flags: Fragment;
GN ORFNames=G5I_11049 {ECO:0000313|EMBL:EGI60728.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI60728.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the PPase class C family. Prune subfamily.
CC {ECO:0000256|ARBA:ARBA00010331}.
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DR EMBL; GL888450; EGI60728.1; -; Genomic_DNA.
DR eggNOG; KOG1094; Eukaryota.
DR eggNOG; KOG4129; Eukaryota.
DR InParanoid; F4WYJ6; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.60.120.1190; -; 1.
DR Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR048525; DDR1-2_DS-like.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR038222; DHHA2_dom_sf.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR24416:SF580; DISCOIDIN DOMAIN RECEPTOR, ISOFORM F; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF21114; DDR1-2_DS-like; 1.
DR Pfam; PF02833; DHHA2; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM01131; DHHA2; 1.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00023137}; Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|EMBL:EGI60728.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 793..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..501
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1002..1279
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGI60728.1"
SQ SEQUENCE 1285 AA; 146156 MW; 869FA23AB52D4DE3 CRC64;
SQLSIYQTIR VVLGNPTCDL DSAVSALVQG LLEYSEINKC ELTDVAVIPV MNIPEKEFRI
KTEVVYSLKS HNIPLNLLTF RDQIDLQNIQ NDANKKLELI LVDHHTLANE DFELKPSIVM
IIDHRPLDPA WSWPNVLLNI EIVGSCATLV ARNVLQKNPD ILDTQLSSLL RGPILIDTYN
MSDEAGRATA TDVDILNVLE QLGRLTSDRT DIFKKIMHAK TDISELTLEE LMIKDLKVTN
GIPLVGFSLL VEDFLVRENA KEVIEQFANE RNCNVVVLIG QDVTKEHVSR DIAIFSTLCN
QLANDIIQAL VESTQPSLNL ELIKEIREEN HSLCLYKQRN VKVTQKCILP LGMEEGKIPD
EAITASSSYE MKSVGPQNAR IRQEKNGGAW CPKAQISSAI REYLEIDLTR DHLITWTETQ
GRFGNGQGQE YAEAFFLEYW RHEKWHQYKD LRGNKVLRGN SNTYLVEKQK LDLPFVASRV
RFVPYSQHPR TVCMRVEIYG CVWNQGIASY TAPKADTDGP NRCNVEDASY DGTEIENLML
NGLGQLTDGI VGSEIEILES NRITNWIGWH DRDNIELFFE FQFSRKFRNC TIHVANLPDL
NVEMFSIVNF WFSLDGKEYH ETPETFQMFN EPKIPSNSNE KDGKSKSSAL ISIPLQLRLG
KFVKIDIKPQ SEWLLLSEIS FETDVKNNTD EALAHLSWIY TNSNENISQI INQDQIARIK
QIDDTEIKGE IGDLEIETDD KIGGEVSDGR KINIQHRGTM MGKSKTVSNE TTLVLNESNL
TPDAFPVNNS PTYIGLISAA LTIIVFFSGC TIFLIKQRGR NKVALLQKHT ALLCGSPAPG
ITINTKDIKL PTPIVVNNLS QSRLSLKSKI ASNNDYKFDD GDSSEQHSIY EKINKISPQP
YVKCEARSNY KTEHFDTKTS EDFTDEVECI VPTMLKKLSH SQTGKINQRV YESYYAATDI
LTIKRRDQHP IVSLFTPLLI RDSIVSYKRG TYDVPRISRH RLRILDKLGE GNFGLVHLCE
AKGIQNPDLG ILQNRQVVIV RSLWRGVVDS LREDFMNDMH ILAEIRDVNI ARIIAIVEEE
PFSAIFEYGE LGDLSSFLKN HDHAAPISYE CSLNLVTQIA SGMKYLESLN VPHCDLAARN
CIVCKDLLIK VSDQAMYCSK YDSEYYVDEC YAKIPLRWMA WEAVLSGKRS CPSDVWSYGV
TVWEVLTRCE DVPYADMTSE QVLENCGLWY SLDNGSKKKC PRILEQPMFC ADDLYRLMLR
CWCKLAEDRP NFQEIYCYLK KLTLD
//