ID H2KVK0_CLOSI Unreviewed; 652 AA.
AC H2KVK0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=E3 ubiquitin-protein ligase CBL {ECO:0000256|RuleBase:RU367001};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367001};
GN ORFNames=CLF_112541 {ECO:0000313|EMBL:GAA27807.2}, CSKR_114434
GN {ECO:0000313|EMBL:KAG5452673.1};
OS Clonorchis sinensis (Chinese liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA27807.2, ECO:0000313|Proteomes:UP000008909};
RN [1] {ECO:0000313|EMBL:GAA27807.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Henan {ECO:0000313|EMBL:GAA27807.2};
RX PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA Yu X.;
RT "The draft genome of the carcinogenic human liver fluke Clonorchis
RT sinensis.";
RL Genome Biol. 12:R107-R107(2011).
RN [2] {ECO:0000313|EMBL:KAG5452673.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5452673.1};
RX PubMed=29454982;
RA Wang D., Korhonen P.K., Gasser R.B., Young N.D.;
RT "Improved genomic resources and new bioinformatic workflow for the
RT carcinogenic parasite Clonorchis sinensis: Biotechnological implications.";
RL Biotechnol. Adv. 36:894-904(2018).
RN [3] {ECO:0000313|EMBL:KAG5452673.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cs-k2 {ECO:0000313|EMBL:KAG5452673.1};
RX PubMed=33677057;
RA Young N.D., Stroehlein A.J., Kinkar L., Wang T., Sohn W.M., Chang B.C.H.,
RA Kaur P., Weisz D., Dudchenko O., Aiden E.L., Korhonen P.K., Gasser R.B.;
RT "High-quality reference genome for Clonorchis sinensis.";
RL Genomics 0:0-0(2021).
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; DF144665; GAA27807.2; -; Genomic_DNA.
DR EMBL; NIRI02000023; KAG5452673.1; -; Genomic_DNA.
DR AlphaFoldDB; H2KVK0; -.
DR STRING; 79923.H2KVK0; -.
DR InParanoid; H2KVK0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008909; Unassembled WGS sequence.
DR Proteomes; UP000286415; 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 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; 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; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 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 PROSITE; PS51506; CBL_PTB; 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:UP000008909};
KW Transferase {ECO:0000256|RuleBase:RU367001};
KW Ubl conjugation pathway {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 20..327
FT /note="Cbl-PTB"
FT /evidence="ECO:0000259|PROSITE:PS51506"
FT DOMAIN 358..398
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 438..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 74278 MW; F290957AB8282451 CRC64;
MNRLPHPLSA FDYSAILDEE GDILDLQKKT IGSCYKWLDR VVHLCLNPRL NLRASTPCLL
DTIPDIYEKL QHIVSCYQDD YTTLSHIRYF RIFIHSVISK SKQTVRLFKE AKESIFIDQS
TPRSQLVKLA LVFSHMQRDL EALFPDNKFC NTYRITKPDA AKWWLDNFGS DSIIHWSAFE
SAFRKTFPLD LRDHIDALHS TIDLTCNNHV SIFEFDVFAR LFQPWSNVLQ SWRVLTILHP
GYMAFMTYDE VKTVLEPFRK HPGPGSYVFR LSCTKLGQWA IGYIAEDLRI FQTLVRNKPF
AQALLDGERE GFYRYPNGKK SPPNLLHDLI HSLPQVRLRV TREQYQVYCE IGSTFELCKI
CDENDKNVQL EPCGHLICRD CLSTFQSTGL NQTCPFCRLE VKSVQDVIVE PYKPSELSSP
QAAADSCLSL VDVEGKSTEQ PNQVPWASQS CGTLQESPRK PPPVPPRNST LSPGSDFVHP
RSPVTGLSRG CCSKSCCELS ECVPLQPCTS NSKKSTGQCE LNYAQLDLFW SDSDCDSIPE
YRTDTKRFGH SPKLIDETAT NEPSSVLSSN PPTDGHCSYP INTVPHESPD NPAPDTPSLD
PSPVTFEATV RYLMSLHQDM DKHNAQLLLC ITQNQVHMAD QIWRHFMPRS RK
//
