ID A0A0R3NY74_DROPS Unreviewed; 611 AA.
AC A0A0R3NY74; A0A6I8V8I6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN Name=LOC4817015 {ECO:0000313|RefSeq:XP_015036027.1};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_015036027.1};
RN [1] {ECO:0000313|RefSeq:XP_015036027.1}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_015036027.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_015036027.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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,
CC ECO:0000256|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR RefSeq; XP_015036027.1; XM_015180541.2.
DR AlphaFoldDB; A0A0R3NY74; -.
DR SMR; A0A0R3NY74; -.
DR EnsemblMetazoa; FBtr0380799; FBpp0341157; FBgn0080779.
DR GeneID; 4817015; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0080779; Expressed in female reproductive system and 3 other cell types or tissues.
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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR CDD; cd05059; PTKc_Tec_like; 1.
DR CDD; cd09934; SH2_Tec_family; 1.
DR CDD; cd11768; SH3_Tec_like; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF459; TYROSINE-PROTEIN KINASE BTK29A; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362096};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362096};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
SQ SEQUENCE 611 AA; 67491 MW; E4FA28378893E64D CRC64;
MIPCVSLAET SVIGNMKERV KEMKVFGCRL NFWNHIGHSL TSSKAKEGNG SSPAQNSTRS
ISPNSSTTNS QFSLQHNSSG SLSGVGVGNG NGVVVGGGGG GGGSIGLGVG GGGGSCTPTS
LQPQSSLTTF KQSPTLLNGN GTLLDANMPG GIPTPGTPNS KAKDNSHFVK LVVALYPFKA
IEGGDLSLEK NAEYEVIDDS QEHWWKVKDT VGNVGYIPSN YVKPKALLGL ERYEWYVGDM
SRQRAESLLK QGDKEGCFVV RKSSTKGLYT LSLHTKVPQS HVKHYHIKQN ARCEYYLSEK
HCCETIPDLI NYHRHNSGGL ACRLKSSPCD RPVPPTAGLS HDKWEIHPME LMLMEELGSG
QFGVVRRGKW RGSIDTAVKM MKEGTMSEDD FIEEAKVMTK LQHPNLVQLY GVCSKHRPIY
IVTEYMKHGS LLNYLRRHEK TLIGNMGLLL DMCIQVSKGM TYLERHNYIH RDLAARNCLV
GSENVVKVAD FGLARYVLDD QYTSSGGTKF PIKWAPPEVL NYTRFSSKSD VWAYGVLMWE
IFTCGKMPYG RLKNTEVVER VQRGIILEKP KSCAKEIYDV MKLCWSHGPE ERPAFRVLMD
QLALVAQTLT D
//
