ID   SPK1_GIRTI              Reviewed;         497 AA.
AC   P42687;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-NOV-2023, entry version 110.
DE   RecName: Full=Tyrosine-protein kinase SPK-1;
DE            EC=2.7.10.2;
OS   Girardia tigrina (Planarian) (Dugesia tigrina).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Seriata; Tricladida; Continenticola; Geoplanoidea;
OC   Dugesiidae; Girardia.
OX   NCBI_TaxID=6162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7510865;
RA   Burgaya F., Garcia-Fernandez J., Riutort M., Baguna J., Salo E.;
RT   "Structure and expression of Spk-1, an src-related gene product found in
RT   the planarian Dugesia (G) tigrina.";
RL   Oncogene 9:1267-1272(1994).
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. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- CAUTION: It is uncertain whether Met-1 is the initiator. {ECO:0000305}.
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DR   EMBL; X75310; CAA53058.1; -; mRNA.
DR   PIR; S43532; S43532.
DR   AlphaFoldDB; P42687; -.
DR   SMR; P42687; -.
DR   BRENDA; 2.7.10.2; 2016.
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; cd00192; PTKc; 1.
DR   CDD; cd00174; SH3; 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; 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; Nucleotide-binding; Phosphoprotein; SH2 domain;
KW   SH3 domain; Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..497
FT                   /note="Tyrosine-protein kinase SPK-1"
FT                   /id="PRO_0000088138"
FT   DOMAIN          33..94
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          100..200
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          220..482
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        342
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         226..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VARIANT         212
FT                   /note="D -> A"
FT   VARIANT         235
FT                   /note="H -> D"
SQ   SEQUENCE   497 AA;  57447 MW;  412FD10588997524 CRC64;
     MGQKFSIKCK KQSKNKNTSK CQKIPKKAYE GPPGSYMVKA KYKYAASGDT DISFEEKEIM
     YVLEQFDEFW LKVVKQKDNK EGLVPSNYVS KQDGSPQSVE AWREIQRWEA EKSLMKIGLQ
     KGTYIIRPSR KENSYALSVR DFDEKKKICI VKHFQIKTLQ DEKGISYSVN IRNFPNILTL
     IQFYEKNGIG NTHIPLTDPM PDNYQPPVHF QDIEINRENI EILNEIGRGF FGSVHRAKWG
     RSYEVAAKML QSSKAEREKF VLEAKIMHKL RHRKIVELLG VCTEPQDMPM LIIVEYMKNG
     SLKEYLKTPD GKKTNLNQMV HMMAEISEGM AYLESEKVVH RDLRADNILV ANDLTRKVAD
     FGLTELTDGS LGDQEKKTLR FPYKWTAPEA AKSKVFTSKS DVWSYGIVMF EILTWASSPY
     PDIPAKEVIE KVSKGYRMPN PEKFITGVCC PDEIYKIMIW CWDANPEKRP TFLVLQEKMD
     LLIVDTLTNN AYYSHSK
//