ID T1J0A0_STRMM Unreviewed; 353 AA.
AC T1J0A0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR006943-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR006943-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) 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};
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DR EMBL; JH431734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1J0A0; -.
DR STRING; 126957.T1J0A0; -.
DR EnsemblMetazoa; SMAR006943-RA; SMAR006943-PA; SMAR006943.
DR eggNOG; KOG0197; Eukaryota.
DR HOGENOM; CLU_000288_7_2_1; -.
DR OMA; FNITSEM; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; T1J0A0; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
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: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; cd05034; PTKc_Src_like; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 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; 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 PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 1..58
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 83..340
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 353 AA; 40636 MW; 0DAA02C3DA8093FE CRC64;
MKDWDPQRGD HVKHYKIKCL DNGGFFVTTR HTFSTLQELV LFYTDAPNGL CYKLTSSCLK
PKPHMWDLSP ETRDRWEIDH SEVILERRLG SGNFGEVWYG KWRGTTEVAV KTLKAGTIMS
PQAFLQEAAI MKTFRHDKLV SLYAVCSVKE PIYIVTEYMV NGSLLDYLRC ADGKHLKLPH
LIDFAAQIAN GMMYLEVKLL VHRDLAARNI LVGENNVVKV ADFGLARIID DSEYTARQGA
KFPVKWTAPE AVLYGKFTIK SDVWSYGVLL MELVTHGQVP YPGMHNREVI EQVDRGYRMP
KPLNCDCPDA VYDIMLQCWD ADPNKRPTFE YLFSYFDDFS VSTEPRYRDA EEF
//
