ID STK_HYDVU Reviewed; 509 AA. AC P17713; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 08-NOV-2023, entry version 132. DE RecName: Full=Tyrosine-protein kinase STK; DE EC=2.7.10.2; DE AltName: Full=P57-STK; GN Name=STK; OS Hydra vulgaris (Hydra) (Hydra attenuata). OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata; OC Aplanulata; Hydridae; Hydra. OX NCBI_TaxID=6087; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2479820; DOI=10.1128/mcb.9.10.4141-4151.1989; RA Bosch T.C.G., Unger T.F., Fisher D.A., Steele R.E.; RT "Structure and expression of STK, a src-related gene in the simple metazoan RT Hydra attenuata."; RL Mol. Cell. Biol. 9:4141-4151(1989). 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:0000255|PROSITE-ProRule:PRU10028}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M25245; AAA29217.1; -; mRNA. DR PIR; A34094; TVHAST. DR RefSeq; NP_001274717.1; NM_001287788.1. DR AlphaFoldDB; P17713; -. DR SMR; P17713; -. DR EnsemblMetazoa; NM_001287788.1; NP_001274717.1; LOC100198593. DR GeneID; 100198593; -. DR KEGG; hmg:100198593; -. DR OMA; NYIAPVK; -. DR OrthoDB; 1614410at2759; -. DR BRENDA; 2.7.10.2; 2720. DR Proteomes; UP000694840; Unplaced. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd05034; PTKc_Src_like; 1. DR CDD; cd09933; SH2_Src_family; 1. DR CDD; cd11845; SH3_Src_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:SF447; TYROSINE-PROTEIN KINASE SRC64B; 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; PR00452; SH3DOMAIN. 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 2: Evidence at transcript level; KW ATP-binding; Kinase; Lipoprotein; Myristate; Nucleotide-binding; KW Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain; KW Transferase; Tyrosine-protein kinase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..509 FT /note="Tyrosine-protein kinase STK" FT /id="PRO_0000088162" FT DOMAIN 59..120 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 126..218 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 240..495 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 360 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 246..254 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 268 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 390 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000250" SQ SEQUENCE 509 AA; 56886 MW; D0614B12B35F9953 CRC64; MGPCCSKQTK ALNNQPDKSK SKDVVLKENT SPFSQNTNNI MHVSHNQPPN INPPMLGGPG VTIFVALYDY EARISEDLSF KKGERLQIIN TADGDWWYAR SLITNSEGYI PSTYVAPEKS YEAEEWYFGD VKRAEAEKRL MVRGLPSGTF LIRKAETAVG NFSLSVRDGD SVKHYRVRKL DTGGYFITTR APFNSLYELV QHYTKDADGL VCALTLPCPK DKPVTGGIAK DAWEIPRESL RLNRKLGAGQ FGEVWAGVWN NTTQVAVKTL KPGTMSPASF LDEAGVMKKL RHKHLVQLYA ICSDREPIYI VTEYMSGGSL LDYLSKGEGV NLQLPTLIDM AAQVASGMAF LEAQGYIHRD LAARNILVGE NYICKVADFG LARLIEDDEY TAHEGAKFPI KWTAPEAALY NRFTIKSDVW SFGILMAEIV TKGRIPYPGM TNAQTIAEVE KGYRMPIMPG CPEPLYNIML QTWNKDPENR PTFDYLQGVL EDYFVSTEQG YRDLGEANS //