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Database: UniProt
Entry: A0A183I195_9BILA
LinkDB: A0A183I195_9BILA
Original site: A0A183I195_9BILA 
ID   A0A183I195_9BILA        Unreviewed;       308 AA.
AC   A0A183I195;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   ORFNames=OFLC_LOCUS13507 {ECO:0000313|EMBL:VDP13926.1};
OS   Onchocerca flexuosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0001350801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:OFLC_0001350801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP13926.1, ECO:0000313|Proteomes:UP000267606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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|RuleBase:RU362096};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR   EMBL; UZAJ01040234; VDP13926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183I195; -.
DR   STRING; 387005.A0A183I195; -.
DR   WBParaSite; OFLC_0001350801-mRNA-1; OFLC_0001350801-mRNA-1; OFLC_0001350801.
DR   Proteomes; UP000050787; Unplaced.
DR   Proteomes; UP000267606; Unassembled WGS sequence.
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; 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; 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   PANTHER; PTHR19969:SF15; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; 1.
DR   PANTHER; PTHR19969; SH2-SH3 ADAPTOR PROTEIN-RELATED; 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; PR01887; SPECTRNALPHA.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362096};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362096};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW   Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096}.
FT   DOMAIN          61..121
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          127..208
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  35209 MW;  E1F92EFBCF8A6D07 CRC64;
     MGNCFSGSPR QSSPSSGILN ERNSPKFSTD HGSIEPLKEA NCSEALTPRR QENHSLQDPT
     PGKEILVALY AYESRADGDL SFRKGDVMYL LDQSNSDWWY VRHSKGGTGY VPRNFVARQQ
     TVESEEWFAG RIARNRAERL VLASNLPKGT FLIREREADT REYALTIRDS DDQRGGTVKH
     YKIKRLDGDA GFFITTRRTF ATLRDLVKVA DGLCCQLSFP APRIAPTRPD LSHDTQQVGM
     HNREVIEQVE LGYRMPLPRG CPEQIYTEVM LKCWDKIPDR RPTFDYLFHF FDDYFVSSQP
     SYVPPSQN
//
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