ID A0A0N0P6L3_LEPSE Unreviewed; 302 AA.
AC A0A0N0P6L3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=ABL78_3158 {ECO:0000313|EMBL:KPI87749.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI87749.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI87749.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI87749.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI87749.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJSK01000075; KPI87749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0P6L3; -.
DR EnsemblProtists; KPI87749; KPI87749; ABL78_3158.
DR VEuPathDB; TriTrypDB:Lsey_0075_0110; -.
DR OMA; YAPWREW; -.
DR OrthoDB; 276791at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
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 TRANSMEM 182..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..54
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 126..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 32320 MW; 837F8305EE22447F CRC64;
MTSTAAPAPD FSCAICLDTA AEPVVTRCGH LFCWDCLAHW LHSPSGAPEC PVCKGRVDER
ISGDIIPLYG KGKQVANKPA SGPHATASTA ATTAPTAANA AAAATAMDPA QEAFFSRPSA
YSFAPGREAR RESAAATHAA PHAEEEHHPR PTADRAPPRP RPHSAQQHQN VQMHMQNHGM
PLTVGSSVFF FGGGGGMFFS IALIIAWAVY NYAPWREWRG DLTRWYHRLR GDPIPEERRD
GTTANAEASP SSANSNGANQ TAAPGPASGE ETVVLPSQQV MVRNLIFSIL AVFVLFQLLL
FM
//
