ID A0A3Q3B2R7_KRYMA Unreviewed; 923 AA.
AC A0A3Q3B2R7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000023250.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000023250.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSKMAP00000023250.1}
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}.
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 RefSeq; XP_017271975.1; XM_017416486.3.
DR AlphaFoldDB; A0A3Q3B2R7; -.
DR STRING; 37003.ENSKMAP00000023250; -.
DR Ensembl; ENSKMAT00000023545.1; ENSKMAP00000023250.1; ENSKMAG00000017253.1.
DR GeneID; 108236056; -.
DR KEGG; kmr:108236056; -.
DR CTD; 90850; -.
DR GeneTree; ENSGT00390000014178; -.
DR OMA; CEKKYDI; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000264800; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
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:UP000264800};
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 276..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..515
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..617
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 102765 MW; C9DD2DB1F5068CC3 CRC64;
MDLTTAKDSE KTCVLCCQDN DIFALGKCDH PVCYRCSTKM RVLCDQKYCA VCREELDKVV
FIKKLKAFQS LPYQQFPCEK KHDIYFGDEM IFSQYRRLLL SECPLCREPK VFSRFEELEQ
HMRKQHEVFC CKLCLKHLKI FSYERKWYNR KELARHRAHG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DADGSQEYYS DYKYLSEHFR ESHYLCEEGR CSSEQFTHAF
RTEIDYKAHK ASAHSKNRAE ARQNRQIDLQ FTYAPRQQRR NDGQVTGEDY EDMRHNRGGR
GRPQMGQKSW RYSREREEED RQMEAALRAS MAMRRQAERA AVQERSTPKH CREERTERVE
AEEPKPPTGH LKTANKPPVK TMKSTNPGDE DDFPVLGATA GAPIVKPAPA VSTAARAALK
EDDFPSLSSA AVTAPMTPAY SGQPKKTSSF QEEDFPALVS KVRPFKPAAG TKSAWSSHTA
APKTNTHQPP PARAPPPVSS VSSGPQLLPS SNSLSLRRKK KVGENGKTAS YPSPPLSDDE
SGGMTQQEFR SVPTMLDISS LLTVKGGNSK PPAVTSTFSS PTPSADHATS KPNKKKKQKN
TTASSASASA MSGAATAVDT SSVETTAQKE NVPEKTWSKP PSSALTAPVL NGVANGRADT
PPAVCRELPI GTPPPSTEPA PEPEEEFPAL ITKKPPPGFK TSFPVKTSAA TTAPAGAPPP
PPPGLGISAP KPPPGFTGIP LNSNVVEPVV NQPPKALSSE YLVPDDFQQR NLELIQSIKK
YLNNDESKFN QFKNYSAQFR QSVIPAAQYH RSCKDLLGDD YNRIFNELLV LLPDTGKQQE
LLAAHGDCKA LEKQSGGGRK NKNKKNAWQT PATAANTAAE LDCQVCPTCR QVLAPKDFNS
HKTLHIRENE EFPSLQSISR IIS
//
