ID A0A0V1HDJ0_9BILA Unreviewed; 3214 AA.
AC A0A0V1HDJ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=MYO15A {ECO:0000313|EMBL:KRZ08473.1};
GN ORFNames=T11_18509 {ECO:0000313|EMBL:KRZ08473.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ08473.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ08473.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ08473.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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 -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004184}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. ROCO subfamily. {ECO:0000256|ARBA:ARBA00008171}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family.
CC {ECO:0000256|ARBA:ARBA00006998}.
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:KRZ08473.1}.
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DR EMBL; JYDP01000086; KRZ08473.1; -; Genomic_DNA.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; 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 GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13201; FERM_C_MyoXV; 1.
DR CDD; cd00124; MYSc; 1.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.25.40.530; MyTH4 domain; 3.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
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; IPR019749; Band_41_domain.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041795; MyoXV_FERM_C.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000159; RA_dom.
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; PTHR22692; MYOSIN VII, XV; 1.
DR PANTHER; PTHR22692:SF26; MYTH4 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW 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};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT DOMAIN 95..192
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 205..620
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 351..1034
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1197..1346
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 2310..2374
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2466..2621
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 2626..2945
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 2634..2715
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 2928..3192
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..933
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1520..1604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2367..2416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2373..2391
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2392..2416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 444..451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 3214 AA; 368990 MW; 0A7E6956570BAD43 CRC64;
MSEKSKMTKE SMKSDSDSKS KEKEDSQRRK TAFGKLVNKL SSRLKSSDES SAKKNAVIVK
EATLEDIRKS NLIKPSKDGT IDLNQPIQPL EKYHYYHGCV SRYDAEEILI NHTPGNFLIR
ASRRPGNSLA IVLSIRTTSG ISHFEIPVDN FGRFYFNDFA FDNLHSLLMH HFKHFYPVSL
TSDYCVYLKH AIDRTYWEFD DRQVHLEDTP LGEGNFGAVY RGYVDIDGKR QMLAVKTLQD
PDNDEGREEL LREARVLRKL EHVNITKLIG VTISSGATMV LLEFLNEKAE SFTFEKGDLV
WYKTKQGYAL PGKITEVDSA SSTAWVQSND KKEEIAEFQF TDLQKRASDA MSFEDLIQLD
DLCNPAVLWA LKTRFEYGKT YTYIGEMLIS INPYRHFDVY GPEIMEQYRK KMTTSLPSHV
YGFAEMVQRR LYAFDTSQWI IATGITGSGK TELCKLMVQY FAEGCGREMK EAAFNDKLYH
AMHILQSFLN AKTAANDNST RGGKIYSLQY QNKKLTGAKL AYCLLEKTRL VSHVRGERNF
HIFYEMIAGL KQQTRQSFGL NKPENFFYLN QGKCVNLGSR EENNFELLEN ALEIIKITLD
QRHYIFRLLS AILHLGNIYF EEQTEDSNRK LVIANQNEVQ WVAYLLQMDP DEITHRLTTK
VIESRDQKVV HALTLDRALD IRDAIAKELY MGLIRWIIMK INNQLCNNDN DCNEINILDL
YGFECFKVNS FEQLCINYIN ERIQRLFVRV QFCSEQMEYI REDIVWDRNV GANLLNNSIF
NILVKQPNGI LSLLDDECSF PKGSDESFLI KCQNNYDDSP LFTAKTKRQL GFVVQHFFGH
ARYNVVGFVD KNREVHSAQT VEFLLESQNI LIAQMFEKQK LALSKRSAEN ENFDTYRIRA
PTFAMQLHEE FNQLTKRIEK YMVHFVRCIN PNKTKEADVL DMQFVLEQIK CLGLTEVLHM
QKFGFTIKMK FRDFLVRYGC LKPETATVEG KDEKNMCLYI LTSLAHQYFQ DFRIGKTKVF
MKDIVAEHLD SILSERLSSS VIIIQKYCRG LLARRKFHHL YDWITHLQAI VRGSQARKKF
SLIKAKVAEE AQQYAKQSRN LEVFRELSIK PNSQDGNANL QQRNSCAIVS VNHLEMPQNL
SEMLLTKTNL DADKNIVRAD RRIASHHEQE FILPHDLHEY SFNKYAQQYF KNHTWQMRRD
PINTPFLHKD SEADMQLSLT LFRLILRYMN DTSLSSSQEI ILSNYIIQKG IDNKNLRDEI
YAQVINQIHG NPNQANAERG WRLLGLCVSA FPPTDAMFKY ALNYVMNADC DGFKNLLKTK
LLQSIHDNNT TVRRYPPCIL EHKAIRSKAK MALLSYLSDG NKVGSQIDSW TKAEEFAELA
LKNGGISECT GWTVSLECQD AVIRLNGNQY LLDVLSYIEL PQLFPAQKSD YLITMKQHKK
PHLEPSTIQE RLEALERRPN LRTLVSDDFH SSKLKKGGSI TSLVHRARLQ HGEKLDSASV
KQEWLNWNEK CAAQSKIRPD HLNLDHDGSV TNNARCQSRM SSNSYQTDHS ILTADTSNQT
RPPSSVNTLR SSKFCETSHP SVDENQRKTF SWSKTSTRQE APALANNLSS QAEQSENKQN
CQNYDKENVD KKNSIPAEQA AIQDIAYMSI NRRPISNYSS LSSHFRAISI PGRNSEVDEF
LDQLFNPVLG NMNDPKSLAA TIKGGGDESD NKNQPVAVEQ AQTMYSSVYS FMPQMFMPNQ
RDSQVQGMQQ FSNVKAQGNF NADQANVLMP VPLMPVSFGS YMQANSIGQE VFKGPSNMLP
LSMIQNSSPK AWTRLHEYQH PSPPNGVGSD VMYTSFNPHT VNPNSTDEHC MHENNFNNDL
SNKVKEEMTS LSEAGSFFPN SSQLWKGRDE MKSKNEDDSD QKLFYQWEQI SKSDAAAKCK
PLSTPTKTLI KEETGSLLSR DSFASRDIIN RNNTKSVASL DASKEHENID NSNYSTLTTS
ESKIHQKESD NMKNYKTLSR EHLYGNLTYD SENRWINPCE NLYQTEDAHC RSNTPTAYRL
EQPQLTNAES FDTLTVSHRD ASEFGYDSRV SMRDGLMKIP PSICSTLTRE SRIDSRPSFK
TQDYFSSTLV GLKEKRRGPA LTYGNVAWKL VIRKELFFPN DSLQDPAALD AVFYQIVRDT
FNEKDSFRLE KAERNQMIRL LTSNGIELET LTSANISPSF KKHVVQIARS WPLYFCRLYP
VTVSNKFGED RPHYVGISES GIWLIDRQGE GNDETLRIVE CYEFEDIDHT EATENEFLLS
TVNGVIIRVS TKSAEEITNL ANKYMFGPNQ GKEYVRATAD YITEEPNLLS FRKGDIIQLV
KTMPDAHPGS GWLYGKINTK YGFFPKEHLD PISDSEEEEE DDDDENEEQT SEVPNGLEAS
NQMTPTSPPP VSAHSTQDKL TMMEFAMLHF REAQKYESTQ NSTLTTLKRK SKKEWTWKDV
ADLVKFTKSP IQNPLLKLDK GDVCKLAVDC FLNLMMYMGD YPLKKDTNYL DCVYKITAAC
REHPILRDEV YCQVIKQITN NKSSKPDSAL MGWRMLSILT AYFDSSDVFR PYLQKYLSDS
ASDNRRAYHG TAMECFQNFR QTLQFGGRRF ILSPQELESI SQGKNLKRQV YHLPGGTKKV
INTKSVTVVE EIIKELCIDL NVRSSLEQQE FSLCVVIESD NVMRILSNDE YILDITSELE
EMKREYFLLL KRIVWMHPLR KDSELYTDIM FFQVLPDYIE GLLVVMRGPD SVSAATMDDI
ATLGALLACA DDDWDGQMVT ARDIVHLLPK TVHNIRHVTL ELWTDRINQK LRQLSPKTLP
IVARAKFLDL LQTWPLFGST FFYIPSVSDP RAKGECLMAL NRHGVQFLDI HTHEVLFEFR
LNEILSTQKS YPDGTTSMNQ QSTVEHMDIK IGNMLQQHVL TLRTDQGAEI SRLFGQYIYV
DSQSRGLLDI DGKRQMLAVK TLQDPDNDEG REELLREARV LRKLEHVNIT KLIGVTISSG
ATMVLLEFLN GGSMDNYMKK HQLSPYTKMK LLSDAANGIR YIHSKNVIHR DLAARNCLLL
LNKNNHPERV KIADFGLCVE TAEVYHMANF QCIPVRWSAP ETLKDKVWSQ KSDVWSFAVI
IWEFFNEGCV PYYEIEPFSP KILLNALAGG YCLLSTPEMH PQLVNLMTSC LNFNSDQRPT
MDKVYEKLQV LLSSAVVIKF YLFYTNTHTL YIYI
//
