ID A0A0V1KW03_9BILA Unreviewed; 1186 AA.
AC A0A0V1KW03;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN Name=abl-1 {ECO:0000313|EMBL:KRZ51551.1};
GN ORFNames=T02_11598 {ECO:0000313|EMBL:KRZ51551.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ51551.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ51551.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ51551.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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,
CC ECO:0000256|RuleBase:RU362096};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
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:KRZ51551.1}.
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DR EMBL; JYDW01000223; KRZ51551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1KW03; -.
DR STRING; 6335.A0A0V1KW03; -.
DR Proteomes; UP000054721; 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:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
DR CDD; cd09935; SH2_ABL; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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; IPR035837; ABL_SH2.
DR InterPro; IPR015015; F-actin-binding.
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:SF162; TYROSINE-PROTEIN KINASE ABL; 1.
DR Pfam; PF08919; F_actin_bind; 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; SM00808; FABD; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW ECO:0000256|RuleBase:RU362096};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054721};
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|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
FT DOMAIN 81..170
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 176..266
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 293..549
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1186 AA; 130540 MW; DFB3A58625AE64F5 CRC64;
MGAKAGKHSA SFASHSSLKP VHLPPPPCSF PDSALLNLEP DVYSTEEPVG SESLNQHSFP
VDRWSSNENV VNDGEQSPSD SGGQKFVALF DFFGYKADQL TLRKGDQIRV LNYHESGDWC
RAELVQLKSD DNTTTTSTGG CGGGGGGGGG RRVVGRIGWI PSAYVAPANS LEMHLWFHGK
ISRSDAEFLL SSGINGSFLV RESESCPGQV SVSLRYEGRV YHYRVQEDAE GKLLITNDHR
FSSLAQLVHY YSRQADGLAC CLLYPAPKKD TASSNFSLTQ SQPDEWEIDR TEVVMKQRLG
GGQYGDVYEA YWKRYNKSVA VKTLKEDTMA LNEFLSEATI MKDLRHRNLV QLLGVCTQEP
PFYIITEFMI NGNLLDYLRS ASDSSQLTPN VLIYLALQVC NGMAYMESRN YIHRDLAARN
CLVGENYLVK IADFGLARFM AEETYTAKAG AKFPIKWTAP EGLAYNTFST KSDVWAFGVL
LWEIATYGQT PYPGVEFSEV YTLLEKGFRM ESPAGCPASV YRLMLQCWRW SPADRPTFRE
IAVALDGLFN AKHFDDEAET GAVVQHVARA SRHHISSPSE DRAHSMSSFA RHKSISPTNI
QSSEASIQRQ THCRGSSTFT GQQHQHPPTP PPRSAVDRHR HVHHTRAGSS TLSNADNKFA
KEATVGMKEK TVKKVINQFG TFPKGNRIDA YFDSFHQDQQ KPGKFEKATY TTAAAGKNDE
KKYVGSSSMS SSSLSSMCSS VFTNEPAGSS RKSSTSTTKS ALNEANKPRP TKYSRTSRPL
PPVRRGPPGV AGGGSSSSFG RSKSSFSFNS ANIDASEPPT VNKTNQPDDV HREKSFHTDT
QWKGGNWPKL SSRKAAVRKT PSGLTASPAG GGQPVRSYSQ MFANDLHSTI RSLRHVSVAG
CENSGRRSSA LETAPNKGVF MVTAERAKIR QLNKVAPLPY HRTLDRTGQV ASTDHGYRQF
SSQNNWNDDA KQQRWSYAER CNNDNSSQPA IAALVKLPKA VVRPVAPARQ TALSSPLNEC
CCPSSSFKDS DEINGENFEQ KKNLPVADLS EFNNITTITT TNNNNSNNGN CCSTATEATI
SKESIVGLYN TINLGIVELK RSQIHSSSGF IQLSDKLHQL KQMCGIYAEN ISPHGKFRFR
ELLCSLDALV SRLRSSSAST TTDADATDLL RDIDTTVRDL ISLVQR
//
