ID A0A1I8B295_MELHA Unreviewed; 1181 AA.
AC A0A1I8B295;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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};
OS Meloidogyne hapla (Root-knot nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne.
OX NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig123.frz3.fgene9};
RN [1] {ECO:0000313|WBParaSite:MhA1_Contig123.frz3.fgene9}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 AlphaFoldDB; A0A1I8B295; -.
DR WBParaSite; MhA1_Contig123.frz3.fgene9; MhA1_Contig123.frz3.fgene9; MhA1_Contig123.frz3.fgene9.
DR OMA; IACSIND; -.
DR Proteomes; UP000095281; Unplaced.
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; cd11845; SH3_Src_like; 2.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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; 2.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 2.
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}; 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 77..137
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 143..244
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 267..545
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 703..763
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 769..864
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 889..1147
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 569..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 917
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1181 AA; 134304 MW; 6FF3D072B33277CD CRC64;
MGNCLSRSRR RVAKSGLDEQ NANIISKNSS NAMVCSSYQY RSGSKTFPDA FTNIIDSNQK
LLGQQQLNDS PQNEHNPSPE KLIAMFSYES RSEGDLGFEK DDIMYLLDNT NPDWWYVKNS
KGVPGYIPRN FVAFLKTPES FDWFAGRISR SVAERLVAGK HLPPGTFLVR ERESDKLEYA
LTIRDIDQGL GVPCAKHYKI KKMETECGFY ITKRMIFPSL EALVSYYSDR SDGLCNKLTL
AAPKMTPVGP DLCYDTQQNW EIPRHEVQLL RRLGEGNFAE VYYGHWRGKV DVAIKMMKPR
TMSSEDFISE ANTMKQCQHP NLVRLFAVCT KEEPFYIITE YMKNGNLLDF LRAETKEDQQ
KLSSPKNPLT IQELVVICAQ VADGMKYLEE RKLVHRDLAA RNVLVGEKIS GVPIVKVADF
GLARKLMDDE QIYEAQTSTQ FPIKWTAPEA AMLKIFTVKS DVWSYGILLY EIFTKGAVPY
AGMSNSEVLV KIESGERMKC PYNSNPDESV LIKRIYEQVM LKTWEQQPER RPTFEALYHY
FDDFFNFTSF LNNSGPSFVS MGKCFSRQST VKGSHDDSEN SRSSAGISDR RRRHSVDSQS
VDSRDLDSVH KQRYVGPRQP HQQQHKLSAS QFGYYRAAGA LPSGANRSRY QPGDGQRAPY
FGNYPRHYIV NGEGSGKSTA ITSLGGSPSV GMAGRKQQNE TVEGESKVIA IYEYQNHVKG
DICFDKGDVM ILLNDSNPDW WYVRHLKNGE GYAPKNFLAK MESLESEEWY AGKIQRSTAE
KLVLAGKMPR GTFLVRKREG GEYALTINDL KDDSLDVKHY KIRPLDNGSG FFITTRKVFP
TVRDLIFYYS KEPGGLCCRL TYPAQKIAPI RPDLSYDTAK NWEIPREELQ LVKRLGDGNF
ATVYLGRWRG VIEVAVKMLK PGTMSVEAFL EEAQIMKQCN HPKLVRLYAV CTVGEPYYII
TEFMRNGSLL HYLRNLNSRL SIHALVDTCA QVASGMMYLE SRKLVHRDLA ARNVLVGDKI
SGVPEVKVAD FGLARKLMNE NIYEAQVGAK FPIKWTAPEA AQYGNFTVKS DVWSYGILLN
EIFTFGTVPY PTMHNKEVIA QLEEGYRMPC PKGCPEAIYL EMLKCWDRNP DKRPTFEYLF
TFFDDFFISS QPNYVPPSVD GVPFEVHSMD TDEGSSSRMP K
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