ID A0A3Q3LBJ5_9TELE Unreviewed; 927 AA.
AC A0A3Q3LBJ5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 28-JAN-2026, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000007051.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000007051.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMAMP00000007051.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR RefSeq; XP_026181626.1; XM_026325841.1.
DR AlphaFoldDB; A0A3Q3LBJ5; -.
DR FunCoup; A0A3Q3LBJ5; 1175.
DR STRING; 205130.ENSMAMP00000007051; -.
DR Ensembl; ENSMAMT00000007248.2; ENSMAMP00000007051.2; ENSMAMG00000004761.2.
DR GeneID; 113141433; -.
DR GeneTree; ENSGT00390000014178; -.
DR InParanoid; A0A3Q3LBJ5; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 13..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 292..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..305
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..513
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..577
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 103330 MW; F4DE8DC6E8585F4A CRC64;
MDSTTTKETE KNCVLCCQEV DIFALGKCDH PVCYRCSTKM RVLCEQKYCA VCREELDKVV
FVKKLQPFSS LPWQQFPCEK KLDIYFGDEK IHAQYRHLLS SECVRCTEPK VFSRFEELEQ
HMRKQHELFC CKLCMKHLKI FSHERKWYNR KELARHKVHG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYYCHFC DADGSQEYYS DYKYLSEHFR ESHYLCEEGR CAMEQFTHAF
RTEIDYKAHK AGAHSKNRAE ARQNRHIELQ FNYAPRQHRR NEGLVSGEDY EEVRHNRGGR
GRPHGGQKSW RYSREDEDRQ MEAAIRASMV MRRQEERAAV QERSAPKHCR EERTERTEPE
ESRQRTGPIK PTIKPPVRTM KSTNPGEEDD FPALGATAAT SIVKPAPVAV KAAHSALKED
DFPSLSTVAT VSPMTPAYSA QPKKTSSILD EDFPALVSKI RPLKPAAGTN SAWSSNSSVA
KPVANPPLSS RPAPPLSSAS SGPQLLSSTT SSSSRRKKKV GENGKTVFTR SPPSSDDESG
GMTQQEFRSV PTMLDISSLL TVKGSNSKPS AVTSSSSNPP PSTDLPTCKA SKKKKQQKNT
AAPTPSVSGT TATVNTMSVE TAAQKENVPE KTRYKPLSSA VTSTSSLRNH PEKPLLLSKE
AAPVLRPSAD PPLEQEEEFP ALATKKPPPG FKTSFPMKAS APASAPAAAP VSAPAASPAL
PPPPPGLVVS GPKPPPGFTG IPLNSNVLEP APSAGNLPPN TGYLVPEDFQ QRNLELIQSI
RKYLHDDESK FNEFKNYSTQ FRQGVISAAQ YHHNCKDLLG DDFNRIFNEL LVLLPDTSKQ
QELLTAHGDC KALEKQSGAG GGKKNKNKKN AWQTPTTVAH VAAELDCQVC PTCRQVLAPK
DFNFHKTLHT RESDEFPSLQ SISRIIS
//
