ID W2TV38_NECAM Unreviewed; 1208 AA.
AC W2TV38;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN ORFNames=NECAME_06130 {ECO:0000313|EMBL:ETN85965.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN85965.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
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}.
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DR EMBL; KI657626; ETN85965.1; -; Genomic_DNA.
DR RefSeq; XP_013308192.1; XM_013452738.1.
DR AlphaFoldDB; W2TV38; -.
DR STRING; 51031.W2TV38; -.
DR EnsemblMetazoa; NECAME_06130; NECAME_06130; NECAME_06130.
DR GeneID; 25346162; -.
DR KEGG; nai:NECAME_06130; -.
DR CTD; 25346162; -.
DR OMA; TYGMAPY; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000053676; 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; cd05052; PTKc_Abl; 1.
DR CDD; cd09935; SH2_ABL; 1.
DR CDD; cd11850; SH3_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; 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:UP000053676};
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 106..179
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 185..275
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 302..553
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 568..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1208 AA; 134543 MW; 69ACC949A696F2D6 CRC64;
MKFGVVYTES GCTESADWAE SVAAIASVHD SDNMERRPSS VDTFRALHQR ESSSWSSRAF
KPEEWDGWVG LFLYMTKIFM PYSNLLSSTD FSEDLLSASM GGGDDATSPL FITLYDFHGV
GEEQLSIRKG DMVRVIGYNK AGEWCEARLA ATRQSDLASQ KRIGQIGWVP SSYIAPLNSL
DKHSWYHGKV SRSESEYILG SGINGSFLVR ESETSIGQYS ISVRNDGRVY HYRINVDAND
RLYITQDAKF KTLGELVHHH SVQADGLICN LLFPAPKKER PPCVFSLSPT QPDEWEVERT
EIVMHNKLGG GQYGDVYEGY WKRHERTVAV KTLKEDAMAL HDFLAEAAIM KDLHHKNLVQ
LLGVCTREAP FYIITEYMCN GNLLEYLRKS DRSKLPPTVL MYMATQIASA MAYLESRNFI
HRDLAARNCL VGSENVVKVA DFGLARFMRE DTYTAHAGAK FPIKWTAPEG LAFNTFSTKS
DVWAFGVLLW EIATYGMAPY PGVDLSNVYS LLEKGFRMDS PPGCPPSVYR LMLQCWIWSP
SDRPRFRDIH ASLESLFPHS NIDEEVDRQL EKSRLTSQRR SRRSDVVPVS AVRFQDTNNR
RSFSGAGASQ RASAEVFPPP PLRSSHHESS LQESAQPSLS SFRDPTADQL RPTPRHLPLP
TPPQSSKPKL LKTALSNASH SMDRGQGNEE VLISPLAEKN IRKAISRFGT LPKTDRIDAY
LESMKRDQPD NSDVGDAEST GMGHALSDDS LDELPIPDPM EGKSQVLVQL KSRLKKTSSE
SPVSPESSQF TSSPPESSAP RSSKLVVTRP APEPPTRSNA ASLPVLPKTD SGKKKVDKVD
GFCQTDSQTT GWKPRRSAKR GPLERVNHIR IKREGKLGDE LAEGELKARI RTLRHVEKPD
DKSTSEFAAN SADETASTSS ASAPEVARVR QLITQKVAPL QHHRPFSVQA SSDDSDSSAS
TLAVNMKHVE KRNGGSDSDG PRPFSTLQRP KLREVVSKDR VPSANEELDS GMVRTQSLRD
ITTKFEKLTA APTKTPISVR GGLVGTAANK RFSLLESKPH SSSVTSETSP SSSPDDVVAT
PLSSCEQQSV SKESLLALYR TLEGCMRDLR NERVGRVTQT SRTDSRLAML IRLSDVMQQF
HSTCAIYAEQ ITPHSKFRYR ELLNRLEVFV RQLRTCASGS ANNPDFAESH ILPQFEVTFR
QILQLINR
//
