ID A0A151I1R5_9HYME Unreviewed; 1140 AA.
AC A0A151I1R5;
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=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN ORFNames=ALC53_08710 {ECO:0000313|EMBL:KYM80826.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM80826.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM80826.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM80826.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM80826.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica 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=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001149};
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DR EMBL; KQ976553; KYM80826.1; -; Genomic_DNA.
DR RefSeq; XP_018050970.1; XM_018195481.1.
DR RefSeq; XP_018050971.1; XM_018195482.1.
DR AlphaFoldDB; A0A151I1R5; -.
DR STRING; 520822.A0A151I1R5; -.
DR GeneID; 108688934; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000078540; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd00192; PTKc; 1.
DR CDD; cd09921; SH2_Jak_family; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR041155; FERM_F1.
DR InterPro; IPR011009; Kinase-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; IPR036860; SH2_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
DR PANTHER; PTHR45807:SF7; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
DR Pfam; PF18379; FERM_F1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KYM80826.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000078540};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 9..302
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 443..724
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 866..1137
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 827..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 903
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1140 AA; 131926 MW; 410E8D2D69B27E3E CRC64;
MDDDSRLSHY VYIYMANRDK PLKFAFTIGE TIEYLCIKIC HNFNISPLAR HLFALQSYSS
KLWFPCGHIL EEDSEKYRFN FRLRFKPSSM DRLREIDLNA YNYYFEQVRK DVLDNKVPDI
VYEKHKHELI GLGVSDMYRV MLEEELPREI VESEYKKYIP KECIKRHAFF IRKPIHNALT
KLSGYDAAYV KEQYLKQFER MAPNYPYEEY TALMDKDVPN LRAKVLLRVT IEQVKYCEID
IGTWKTICRI EDISTLSIGK NNTVLIGRRT GIPLCVQFDT KAILLSFVSA LDGYYRLSVK
WNFNLCSGDL SIITPSLERL QKLRCHGPVG KDFSYTKLKE KCANEPGSYI LRESETEYCV
YYIDVYNKDG TISSQEVVET KPDKFVMTNS SRVYESLRHL ISSFQNPNES IYFGKCLGFS
EYDKSKLLLC ALENIVNEVA ADEEIITTLL QGGPRCVPWN ELQVYKAIAK SDEDLDCSTT
MTSLHRAIWR VAKGKKLEVM MKILKTEENN YTKEFLELVG KWSQLRSVAL VRLYGITVAP
TIGMLLELVN LGPLDKYLCN NSKSVLTVDM VEATVCLATA LWHLEENHVI HGNIRCRNVL
VHSHTDNSFI VKLGDPGLFT YTEDDIYWIP PECYLDFASA KYSLQADIWA LATTIWEIFS
RGASPPKYHK THTVKMYYKC GNRLPPPKDC PNEIYKLMLE CWGKNNSIAR KQPQAIMRDI
NQILYEVYNA RRTHTYATIC PKFFRDADGN NDENSSIYTE ESKSNSESQT SLVTDYTNIT
WNDHTTEQLI SYQNQDSNID ELSFYLRWLN SELYKMPFAG NGNDCGPSCE DSSGKTNKSK
SNDKACNSKD CSQWQRTYEI NENLDVILQG RIGEGFYGEV YKGTLRRRND KEIDSEQDVA
VKKLKTQEDS ENVLDFEREI KIMERLNHPN IVKILCSVDR ILVMEFIQYG SLLSYLSSHR
YSLACKTLLG FALDIVAGME YLGSMNIVHR DLAARNILVA NEDRVKISDF GLAQVIAASD
YYVFKTLRNI PIKWYAPESL RHNKFSTRSD MWSFGVTMYE VFSYGVDPQL SVRVAEKEIL
MTTITDLSNA LERGHRLPCP NNCPQEIHRK LMLSCWQLNS HERPIFATLR EDIEQLLCNY
//
