ID A0A2B4SFM1_STYPI Unreviewed; 633 AA.
AC A0A2B4SFM1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000604};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000604};
GN Name=SYK {ECO:0000313|EMBL:PFX27398.1};
GN ORFNames=AWC38_SpisGene7917 {ECO:0000313|EMBL:PFX27398.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX27398.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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|PIRNR:PIRNR000604};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SYK/ZAP-70 subfamily. {ECO:0000256|PIRNR:PIRNR000604}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX27398.1}.
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DR EMBL; LSMT01000104; PFX27398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4SFM1; -.
DR STRING; 50429.A0A2B4SFM1; -.
DR EnsemblMetazoa; XM_022931849.1; XP_022787584.1; LOC111327628.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
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 InterPro; IPR012234; Tyr_kinase_non-rcpt_SYK/ZAP70.
DR PANTHER; PTHR24418:SF421; INACTIVE TYROSINE-PROTEIN KINASE WSCK-RELATED; 1.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 2.
DR PIRSF; PIRSF000604; TyrPK_SYK; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
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; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000604, ECO:0000256|PIRSR:PIRSR000604-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000604};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000604,
KW ECO:0000256|PIRSR:PIRSR000604-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000604};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000604}.
FT DOMAIN 9..101
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 162..251
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 359..619
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 265..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 482
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-1"
FT BINDING 365..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2"
FT BINDING 391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 633 AA; 71583 MW; 7FC7E774BCEAD150 CRC64;
MADPLFQHWF HGRINRTEAE EILARHGKKD GLFLLRESTA SAGSYALSMC HNNKIIHYHI
QRHSDGTVAI EDGKKFLGPV ELIHHHHTCL DGLLSKLTDP CNRLPGVPPK TYSGANQEHI
KDAAIAAMAS MGIQDGDETT ATLMRAKLEC AIGSVLHKNQ LWFHGVISRD EAERRLSVLG
YQNGMFLIRE RDSGYVLGLC HEGSVVHYLF DVDQQGRLSI KSGPKFDNLM LAVDHYAQRE
DGLLCKLKEP CNVELFEGRR RISVGARPPS VSDQEPRIVT GNRPPSRSFT ETSPFASNPF
LQGGTANVPD LLHGAAATAG ASRGAAFDAI YDSVKMKKSS FYFNQFKDMQ ARKLRRENLK
LERELGHGNF GSVLKGEYTK SNGEQIPVAV KKLKSEEMNN PHSEIMHEAE VMMKLDHPNI
VRIIGICKDT TVMLVMELAP EGPLHKYLKK HKSLPMFKIF VIMLQVAEGM QYLENMQFVH
RDLAARNILV VNEDFVKISD FGMSRAMGAG SDYYKAGKPG KWPLKWYAPE CIYYRKFSSK
SDVWSYGVTL WEATSYGKKP YEGLNGQVIL EKIEAGYRLQ CPENVPPNVY EVMRSCWEYR
EEKRPTFQFL AQQLADALME LKSTEEYQKQ YLV
//
