UniProt: A0A183AHA4

Database: UniProt
Entry: A0A183AHA4_9TREM

LinkDB:  A0A183AHA4_9TREM 
Original site:  A0A183AHA4_9TREM

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (2)   
   SMART (1)   
All databases (21)   

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ID   A0A183AHA4_9TREM        Unreviewed;       380 AA.
AC   A0A183AHA4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=ECPE_LOCUS6339 {ECO:0000313|EMBL:VDP78119.1};
OS   Echinostoma caproni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC   Echinostoma.
OX   NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000635201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ECPE_0000635201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP78119.1, ECO:0000313|Proteomes:UP000272942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Egypt {ECO:0000313|EMBL:VDP78119.1,
RC   ECO:0000313|Proteomes:UP000272942};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 2 family. {ECO:0000256|ARBA:ARBA00010800}.
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DR   EMBL; UZAN01043335; VDP78119.1; -; Genomic_DNA.
DR   WBParaSite; ECPE_0000635201-mRNA-1; ECPE_0000635201-mRNA-1; ECPE_0000635201.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000050740; Unplaced.
DR   Proteomes; UP000272942; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR   GO; GO:0030677; C:ribonuclease P complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR   InterPro; IPR045103; RNF5/RNF185-like.
DR   InterPro; IPR038085; Rnp2-like_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR   PANTHER; PTHR12313:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF01900; RNase_P_Rpp14; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF160350; Rnp2-like; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272942};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          46..87
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   380 AA;  41389 MW;  FB40D2205349D9D1 CRC64;
     METSDIPTTS RRQNAGDNKN TEHETTPDST ENESAKPSST TGSFECNICL DPAQDAVVSM
     CGHLFCWPCL HRWFETSETR QVCPVCKAAI SRDKVIPLYG RGADHTRDPR SKIPPRPAGR
     RVEPEPAQAG LGGVFNNLFG TPDGGSNFRM SIGIGAFPFG FLATAFNVGG GAGSGGTGSD
     SYTGSNGSGS LDGTWNADAE TIFVNALNLS IMTRIKYRYM VCFVSIQSVN SRQPPGFPGC
     PLDDTVALRT TEANLTFAIR KSVQKCHGTI GLGTCMARLR LIYWCPQSGL LVLRCLRNQL
     VPIHAALSMI TRLETGGQER LALFDVHHIS GTVRSCQKFL VEFYTHQIYS NPHANVRTAL
     RRLIQQRAIT TSPPVLLDNF
//

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