ID A0A195BDV9_9HYME Unreviewed; 746 AA.
AC A0A195BDV9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
GN ORFNames=ALC53_07187 {ECO:0000313|EMBL:KYM82399.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM82399.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM82399.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM82399.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM82399.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica WGS genome.";
RL Submitted (SEP-2015) 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|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367001};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, 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; KQ976513; KYM82399.1; -; Genomic_DNA.
DR RefSeq; XP_018048953.1; XM_018193464.1.
DR AlphaFoldDB; A0A195BDV9; -.
DR STRING; 520822.A0A195BDV9; -.
DR GeneID; 108687610; -.
DR OrthoDB; 1123734at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000078540; 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:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0023051; P:regulation of signaling; IEA:InterPro.
DR CDD; cd16708; RING-HC_Cbl; 1.
DR CDD; cd09920; SH2_Cbl-b_TKB; 1.
DR CDD; cd14318; UBA_Cbl_like; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR014742; Adaptor_Cbl_SH2-like.
DR InterPro; IPR024159; Cbl_PTB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
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 Pfam; PF02762; Cbl_N3; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF47668; N-terminal domain of cbl (N-cbl); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51506; CBL_PTB; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367001};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367001};
KW Reference proteome {ECO:0000313|Proteomes:UP000078540};
KW Transferase {ECO:0000256|RuleBase:RU367001};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU367001};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367001};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 33..338
FT /note="Cbl-PTB"
FT /evidence="ECO:0000259|PROSITE:PS51506"
FT DOMAIN 368..407
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 701..741
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 420..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 83870 MW; 6E77EE29538E5243 CRC64;
MSSSGHSSRT RAVHIGSIFQ KLHGRFADAM TPPKLSTDKR TLDKTWKLMD KVVKLCQHQR
MNLKNSPPFI LDILPDTYQR LRLIYSKYED RMQMLHSNEH FCVFINNLMR KCKQAIKLFK
EGKEKMFDET SHYRRNLTKL SLVFSHMLSE LKAIFPNGMF AGDQFRITKA DAAEFWKERF
GNSTLVPWKV FRHELNQVHP ISTGLQAMAL KSTIDLTCND YISNFEFDVF TRLFQPWSTL
LRNWKILAVT HPGYVAFLTY DEVKARLQKY CITKPGSYVF RLSCTRLGQW AIGYVTSDGD
ILQTIPHNKS LCQALLDGYR EGFYLYPDGR NINPDLTWAV QPTPEEHIKV TAEQYELYCE
MGSTFQLCKI CAEHDKDVRI EPCGHLLCTP CLTAWQDSEG QGCPFCRAEI KGTEQIVVDP
FDPRRTHRPG AHSASASNAS TPTRDLDPDT EDIMELCNGN CSLICDDSDE EDDSSLTNSP
VPPRRIVPSP PLPPRRPSPS PTPNNHLRNG RHLTVPKENA PPPPSAVTVI LNYTDNTQQN
NKVNTEARYD MLHRASSPSS VPPIPPVPST TVVKVHPRRS YGNHATGTPQ RQSQPPPTLP
EKACRVTATN STMSQTGGPS NNVPPVPPPL SAPRPPKTSK EGGIRQDHHY ENTIVICGTS
QHVVKNINLE ANRARLTALM RTRDDPGGGP ITKPESAAYE NVNVEHITRL TALGFAQDAV
IRALGITRND LEMACDILHE FATKSS
//
