ID   A0A0N4U506_DRAME        Unreviewed;       187 AA.
AC   A0A0N4U506;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
GN   ORFNames=DME_LOCUS6263 {ECO:0000313|EMBL:VDN56290.1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000190301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000190301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN56290.1, ECO:0000313|Proteomes:UP000274756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       specific E2 ubiquitin-conjugating enzymes, and transfers it to
CC       substrates, generally promoting their degradation by the proteasome.
CC       {ECO:0000256|RuleBase:RU367001}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU367001};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|RuleBase:RU367001}.
CC   -!- DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB)
CC       domain, a short linker region and the RING-type zinc finger. The PTB
CC       domain, which is also called TKB (tyrosine kinase binding) domain, is
CC       composed of three different subdomains: a four-helix bundle (4H), a
CC       calcium-binding EF hand and a divergent SH2 domain.
CC       {ECO:0000256|RuleBase:RU367001}.
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DR   EMBL; UYYG01001155; VDN56290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4U506; -.
DR   STRING; 318479.A0A0N4U506; -.
DR   WBParaSite; DME_0000190301-mRNA-1; DME_0000190301-mRNA-1; DME_0000190301.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000038040; Unplaced.
DR   Proteomes; UP000274756; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0023051; P:regulation of signaling; IEA:InterPro.
DR   Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR024162; Adaptor_Cbl.
DR   InterPro; IPR014741; Adaptor_Cbl_EF_hand-like.
DR   InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR   InterPro; IPR003153; Adaptor_Cbl_N_hlx.
DR   InterPro; IPR024159; Cbl_PTB.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   PANTHER; PTHR23007; CBL; 1.
DR   PANTHER; PTHR23007:SF11; E3 UBIQUITIN-PROTEIN LIGASE CBL; 1.
DR   Pfam; PF02262; Cbl_N; 1.
DR   Pfam; PF02761; Cbl_N2; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF47668; N-terminal domain of cbl (N-cbl); 1.
DR   PROSITE; PS51506; CBL_PTB; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|RuleBase:RU367001};
KW   Metal-binding {ECO:0000256|RuleBase:RU367001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW   Transferase {ECO:0000256|RuleBase:RU367001};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU367001};
KW   Zinc {ECO:0000256|RuleBase:RU367001};
KW   Zinc-finger {ECO:0000256|RuleBase:RU367001}.
FT   DOMAIN          1..187
FT                   /note="Cbl-PTB"
FT                   /evidence="ECO:0000259|PROSITE:PS51506"
SQ   SEQUENCE   187 AA;  21870 MW;  988B7B5E85C7B967 CRC64;
     MDNIVKFCQQ PRLNLKNSPP FILDILPDTF QTLSTIIARD SNCLKENYYL QLFVENLHLK
     CKQTLKLFKE DRERIFDEGS SSRRNLTKLS LIFSHMLAEL KAEFPDGIFI GENFRITKKE
     ADAFWKESFG NKTTVHWLEF RAALNKVHKL NTGLETLALK STIDLTMNEH ISNFEFDVFT
     RFTSLQI
//