ID F2UPS8_SALR5 Unreviewed; 539 AA.
AC F2UPS8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN ORFNames=PTSG_10481 {ECO:0000313|EMBL:EGD79633.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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; GL832987; EGD79633.1; -; Genomic_DNA.
DR RefSeq; XP_004988861.1; XM_004988804.1.
DR AlphaFoldDB; F2UPS8; -.
DR STRING; 946362.F2UPS8; -.
DR EnsemblProtists; EGD79633; EGD79633; PTSG_10481.
DR GeneID; 16069403; -.
DR KEGG; sre:PTSG_10481; -.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; F2UPS8; -.
DR OMA; NYIAPVK; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000007799; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05068; PTKc_Frk_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 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGD79633.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 87..148
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 154..248
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 271..525
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 539 AA; 60693 MW; 4C858DFD835E1D11 CRC64;
MGCKNSKPAS NYPTGVPNGN GAHGFTMDSM AQPPASTVPS QFNSPPAQLP QSRHSSMGNS
MSQASFGTPT QRPLPQPPGQ AAAPVQQQDN LYVALYDYDA RTADDLTFHK GDEMVIMNSS
DGDWWQAKLI TTGQMGYIPS NYVAQKQSIQ AEEWFHGMIK RAEAEKVLLH NGSHGDFLIR
ESESKPGDYS LSIREGDNVK HYRIRKLDDG GFYITRRATF RNLHELVSHY RLKADGLCTS
LNKAVRPLTQ VAPPDLSHDT KDQWEIPRES LRLEKKLGSG QFGDVWKGFW NNTTPVAVKT
LKPGTMSPSE FLREAQIMKK LRHPKLVQLY AVCTDKEPIY IVTELMKHGS LLDYLHDKGR
ALRLPQLVDM AAQIAAGMAY LESQNYIHRD LAARNVLVGE NNICKVADFG LSRLLENEDE
YTAREGAKFP IKWTAPEAAL MSRFSTKSDV WSYGILLTEL VTYGRIPYPG MTNAEVLQQV
ERGYRMPSPP GTPEPLYQIM LDCWKANAEE RPTFETLQWR LEDFFVNTEN NYTEASTFE
//
