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Database: UniProt
Entry: A0A0V1ML87_9BILA
LinkDB: A0A0V1ML87_9BILA
Original site: A0A0V1ML87_9BILA 
ID   A0A0V1ML87_9BILA        Unreviewed;      1000 AA.
AC   A0A0V1ML87;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Epidermal growth factor receptor kinase substrate 8 {ECO:0000313|EMBL:KRZ72319.1};
DE   Flags: Fragment;
GN   Name=EPS8 {ECO:0000313|EMBL:KRZ72319.1};
GN   ORFNames=T10_7566 {ECO:0000313|EMBL:KRZ72319.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ72319.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ72319.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ72319.1};
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   -!- SIMILARITY: Belongs to the EPS8 family.
CC       {ECO:0000256|ARBA:ARBA00006197}.
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:KRZ72319.1}.
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DR   EMBL; JYDO01000080; KRZ72319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1ML87; -.
DR   STRING; 268474.A0A0V1ML87; -.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01210; PTB_EPS8; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR039801; EPS8-like.
DR   InterPro; IPR033928; EPS8_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041418; SAM_3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12287:SF23; AROUSER, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR12287; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE EPS8-RELATED PROTEIN; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF18016; SAM_3; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:KRZ72319.1};
KW   Receptor {ECO:0000313|EMBL:KRZ72319.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:KRZ72319.1}.
FT   DOMAIN          615..674
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          209..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          976..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..765
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..804
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..844
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRZ72319.1"
SQ   SEQUENCE   1000 AA;  112497 MW;  15F27BC6E093C897 CRC64;
     LGIASMPVLG QNSYFRSSSS VGPLPASMNG NVRRLNGNFG GSMPSFVDGQ TFDVDMRKAY
     MQEDSPSYFV EHLATFGVGP QFGLQWPSDG IRKLKQMERS SAIWAQRMIL RLRHTAVVVE
     DENGDVVEQF PLNLVSEPTA HVSSDPRDLY NNLLVFIVNG SKGKKTATPT EMHIFQCVQV
     SASEVADDIK QFLRGRFKAV PTGRRISGFA MPSGGLEGSP EMTTTDGTSL HGRSILSRSD
     QRYFNQDRPR VNTVPVMMEN GRSPSNFNYR EIDQKSTFSD SSVEFFERDV NILNRCFDDI
     ERFVARIQSA AIAQRELEAL QQQRRAMKPS SRSTQNRMPG DGILLMRAQL PPELEFFDIL
     QKFKLCFNLL AKLKNHIHEP NAPELLHFLF TPLAIILDAC QWGFGRNIAP QVVSPLISRA
     AKALLLNCLT SKESEIWASL GDAWRTTAEE WTGTLPGHYS PTFAHNYGPY STTTTAAVPD
     SGQAVRQNRN LFIDAQLSGD FSRVSLERER LDFEKEKLQE EERRIQFEKR ILEEERRRLL
     EEKRQFYEEQ EQRSVVSERL PRPPPAANGL YSSTMSRSRP DLYRETLREQ ESRRNFPPSN
     VTDDVSFFFE QARARGSQIA QVVYERHGMN EKELTVRKGE FLEVLNNKKN WWECRNAHRQ
     VGFVPHTILS VVDSGIHHNN SSTPHQQSKS FDEPLFVRPP PPSTSTFGPA MGNSGTAFGS
     YATTEDDSAK RSSPVSRTAT PANNNGDTPE VIRQRRGKLD EPKNKEVMMF SSTCLVNSKR
     PYVACAPPVP PPAPPPPPPP LPRTSSGSVE YDEKKASTSN GTIPHGLNTK ENGTSIRNGK
     LPSNVTTVDS RRMLNEELLM TLNKSNLKGS FDFKAKPWPS SSLVTVQEMS SISSKQDVAE
     WLQAKCFSGR AINLLREHDG EKLLSMNKVQ LEELIGREEG ARLYSQLQLQ KTTAKYLLKS
     DSQLNSILAN RRNLNEEKMD DEKSLESQSD DVDSEITIAL
//
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