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
//