ID   F1KQL9_ASCSU            Unreviewed;       564 AA.
AC   F1KQL9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   SubName: Full=Epidermal growth factor receptor kinase substrate 8 {ECO:0000313|EMBL:ADY40173.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY40173.1};
RN   [1] {ECO:0000313|EMBL:ADY40173.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
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DR   EMBL; JI164285; ADY40173.1; -; mRNA.
DR   AlphaFoldDB; F1KQL9; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR039801; EPS8-like.
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; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Kinase {ECO:0000313|EMBL:ADY40173.1};
KW   Receptor {ECO:0000313|EMBL:ADY40173.1};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:ADY40173.1}.
FT   DOMAIN          438..497
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          293..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  64307 MW;  819D1C06844BDF50 CRC64;
     MLSIELPFIS GFKGPIALKA FILLVANSNS YAPYIHLLSR MTYFLSKWKL AALKGRLSIV
     FSGSAPRGYR DDASASSDSS EYFERDVNTL NRCFDDIERF VARIQSAAIA QKELEAQHHR
     LRTAQRKRGS NAQTDPQSGI LQMRAQLPAE IEFVDILQKF KLSFNLLAKL KNHIHEPNAP
     ELLHFLFTPL TIILDACHWG LGRNIAPQVI SPLLSRESRE LMQNCLTSKE SDVWMALGDA
     WRIPPEDWIL PLPKPYRPVF LDGYAPYGPP DNYEPTVSQG YNRYMPQPQP IHRGVSAPPP
     QTHNAYPHQP PIRDRSVDNL NVDLDRMSLE KERLDFEREK IAERERRLIE DERRINQEKQ
     RLAAEKELMA QEAEQRSMAS SYAPRHESRQ ESPAVARRPA LYPSQVNGDQ GVLSPLGPIP
     QPDQSPRQKA FLEDIVARRA KLVQVTYDRV AQNPKELTVS RGEYLEVLND NKNWWECTNV
     HHRVGYVPHT ILSVVQIDRD ISPRSLPPQD PSLHTSERSG IAVAQSVPSG HQGSSLSPRP
     GMMNDDTPEY IKQRQGKRGE FRYF
//