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   03-AUG-2022, entry version 128.
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}.
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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   GeneID; 100198593; -.
DR   KEGG; hmg:100198593; -.
DR   OMA; GMMNMEV; -.
DR   OrthoDB; 539311at2759; -.
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   Gene3D; 3.30.505.10; -; 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   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; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 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