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Database: UniProt
Entry: A0A3S3PAD4_9ACAR
LinkDB: A0A3S3PAD4_9ACAR
Original site: A0A3S3PAD4_9ACAR 
ID   A0A3S3PAD4_9ACAR        Unreviewed;       597 AA.
AC   A0A3S3PAD4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=SH3 domain-containing kinase-binding protein 1-like protein {ECO:0000313|EMBL:RWS11313.1};
GN   ORFNames=B4U79_07007 {ECO:0000313|EMBL:RWS09848.1}, B4U79_07280
GN   {ECO:0000313|EMBL:RWS11288.1}, B4U79_14328
GN   {ECO:0000313|EMBL:RWS11313.1};
OS   Dinothrombium tinctorium.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombidioidea; Trombidiidae; Dinothrombium.
OX   NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS11313.1, ECO:0000313|Proteomes:UP000285301};
RN   [1] {ECO:0000313|EMBL:RWS11313.1, ECO:0000313|Proteomes:UP000285301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-WK {ECO:0000313|EMBL:RWS11313.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
RN   [2] {ECO:0000313|EMBL:RWS11313.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UoL-WK {ECO:0000313|EMBL:RWS11313.1};
RA   Dong X.;
RT   "Trombidioid mite genomics.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RWS11313.1}.
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DR   EMBL; NCKU01002317; RWS09848.1; -; Genomic_DNA.
DR   EMBL; NCKU01001777; RWS11288.1; -; Genomic_DNA.
DR   EMBL; NCKU01001768; RWS11313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S3PAD4; -.
DR   STRING; 1965070.A0A3S3PAD4; -.
DR   Proteomes; UP000285301; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd11875; SH3_CD2AP-like_3; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR14167:SF92; CIN85 AND CD2AP RELATED, ISOFORM J; 1.
DR   PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR   Pfam; PF14604; SH3_9; 2.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS50002; SH3; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:RWS11313.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:RWS11313.1}.
FT   DOMAIN          1..60
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          164..225
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          131..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          559..593
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        143..157
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..316
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  65936 MW;  FEEC69514C7F7072 CRC64;
     MRTKRARVVY SYTPQNVDEL ELRTDDVIDV LDVVEDGWWR GRLRGKIGVF PSNFVQELID
     SSMDSSLGSS ALPIDDAVTD SCDGKIISRG KCDTNECPNI DLDVIKPKQV IGIPTPLRLG
     TNLGSNLKQA LKPVEDKSKP PPKKPPPPTP SDSDTCAPRL PPKPMREQAK VLFAYEAQND
     DELTIKEGDV ITIISKEIED QGWWKGELNG KIGVFPDNFV ELIKMPSQEE LTLPPRLKKP
     ERPSEKPSSS ISPSITSSKL GANSSIGEES SKLSAISTKK AKAPPNPHKG SSVTKPDVVP
     HEVSARDEHY EANNEEGSEQ QHFGNIDTAN KLTHLTANRA KGPKDRRPPS MLGVPKELEN
     GFIKENGTYT ETKSSVNSST AQSEQTKSSQ QSPPQPQPVP PWMLELRKTQ EKKNEEKRKA
     AINEDSPTVV NKSAPAPGSP SKTSPSRFSG DFSQKFTAKE QQPTSLPSDV NETMTVTTPP
     FKPAKAVKPN TVSSPSSVSN TKLSKAQSDT HNLNNLSNKD VLDLQNEVRL LKETTVQKTE
     FDELLKQFNE LKDLVEYQKQ SFESVRKDLI NDVAEAKQKL ATLQIEVERL RRLTTTV
//
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