ID A0A0K0DNA7_ANGCA Unreviewed; 1171 AA.
AC A0A0K0DNA7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0001323701-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0001323701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
CC {ECO:0000256|RuleBase:RU366018}.
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DR AlphaFoldDB; A0A0K0DNA7; -.
DR STRING; 6313.A0A0K0DNA7; -.
DR WBParaSite; ACAC_0001323701-mRNA-1; ACAC_0001323701-mRNA-1; ACAC_0001323701.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000035642; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd19672; UBR-box_UBR1_like; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF24; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000035642};
KW Transferase {ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 91..162
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 91..162
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 980..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 132865 MW; 3CB7E50173C0324D CRC64;
MIVDLVSAAR QADWDRAREL LFHHWGSECP KLYAPNPEHP WEISEDEKDI NTALFVPLAG
AFCADSSVTD SSLRPLIEQT GFSGEKHRTG QICGHVFKSG ELTYSCKDCA TDATCVMCHE
CFHLSEHKAH KYKMHTSNGA GYCDCGDKDA WSRGYACKLH EMNEDDNIPF SLPESLEARL
RGLTCLILQY STKLICWEKA DVLPLDLSLI AVEKPEVSSV APYVTVLYND ETHTYETVIR
ALEMFIHCTK DQAMLIATIV DREGRSSVKV GAKLDCERVK SDIQRRTLRD VNRRTEKTGP
LDVKVMDGAL VAHQNHAIAL LAWLNSQIDA FPVLGSIVGD VLLNTVVEKD NDGLEVDETI
LVRLLRFDKK MWKSARANTH QMLMKTVLMN FEQKVSFSKT FLEHYEDIYA EFIDDDHDID
ISVVSLTVQF LTVPSIARQL ITEDGAMRTI FSSLVKHTDQ FAREPKDLLS RFDFAKHTFP
VTGMDEVKRQ SVEHQVWELE WETAFNIQLR IQDILGYVIA WTRADRTTNR AVLLLCLESL
TLHPPSTLEE PAGATHTVVE AFKNLLLVNG DSTVVIPFDV LRGAVSIHQP LWRLTAGLFT
ASPDLLHFLI SLETTSLSDD EVHIRQQIRK MATTLYEMPL RVLVLCAQAH AQLWRRNGFS
LVNQIHNYYS PLCRTEMFDR DLLMMQVGAA IRPPTDFLLH IICRFRLVQW ADQSGDGASK
HPTPFGKMEP EETGKIIVIL AEEMLHLLIM IVGERYYPGV GKCTFTEKMQ REVIHVLCTG
PQPFSHIQKK MSHDPMVERV SLHDVVSSVA NFVKPTSTSA GQFHLKDTLL SEYNPFFYHY
SKSDLSQAEQ YQQKVRLKLN RKLQACPPPV PCEFEPFFIP VRNILKTPCL IKILKLVLDR
TGKRSRFSSD RLLHRALYLI GMALHEQARD LQGFPFIEIA AKEELLQSLE SLAGSTEVAS
HADLLWWTIQ NYKEIQRLST TGNTTEKGKE SVDNQETTND ARAKRAERAA RMREQAMMKM
SKMQKSFLKV MEIENPVSSD QNQPGSAVSD FRGDDDEDFV SKQEDHGFPV CLGPQRSRVE
EVLPRKVTCI LCQEEEILCP KSGKAFVCAA YVQKSLLFAQ HGEPENDAKL RDLAPANLLF
GIDASTCSHT MHYECFHRSE TLFFFAASYL L
//