ID A0A183KGE7_9TREM Unreviewed; 601 AA.
AC A0A183KGE7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=SCUD_LOCUS14094 {ECO:0000313|EMBL:VDP55244.1};
OS Schistosoma curassoni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001409701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SCUD_0001409701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP55244.1, ECO:0000313|Proteomes:UP000279833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dakar {ECO:0000313|EMBL:VDP55244.1}, and Dakar, Senegal
RC {ECO:0000313|Proteomes:UP000279833};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; UZAK01036406; VDP55244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183KGE7; -.
DR STRING; 6186.A0A183KGE7; -.
DR WBParaSite; SCUD_0001409701-mRNA-1; SCUD_0001409701-mRNA-1; SCUD_0001409701.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000050789; Unplaced.
DR Proteomes; UP000279833; 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 InterPro; IPR003769; ClpS_core.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
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 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:UP000279833};
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 168..239
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 168..239
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 30..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 67541 MW; 293DFED7846738A6 CRC64;
NDSISIDRLK AAYLEGNPIH VDFPSVQSHN ATPTLIIPQP TTNTSDDTPN ASENIPKTTR
SGRRQFTETL LSSDDASFER LLFDEVRTQA LEVCTPQVFK PSENISTEPF GESDFESSKS
EYAALERTLF RSFELFIAGR EFIKTQDAGE CADQLEAYLQ SVAPSEQGIC GRIFQANEPT
YCCRDCAIDS TCVLCRGCFF NSAHIKHNYK ISTSIGVGYC DCGDPEAWRS DAWCKLHKNT
SKCEGAEENN LSKLTDTENT DVKLRAELEN LRRRINGLPS DIVMRTGKLL KPLIKSAILC
LTDLIQGTPR LSTEPLSSRL HQEKCPLSED GDEKQTTVDL WSTDDGVVDY KMDNENSWDN
WPPPLSHIPL VSPSEDAAKL GQDAWPRTAP KRRSAVDVEA RCLAQLERAR KYHPRLFPPR
PMRTASERTA ASRSFLVLLY NNEYHNYEQV IKTLRRVLDC TTQQGTHYAV LVNCDGRAVL
QTNLTASQAS NLASILMRTS TSLSTRPINC AAQHTDVYSM EVFFTLFIRW LRRFCDQVPS
LRPIICHAIL GHLPADKNGI DVSESSQSND ILPILLPGEI VEQDSFLSHI LERHSLTWRC
K
//
