ID A0A9W7TRI3_TRIRA Unreviewed; 904 AA.
AC A0A9W7TRI3;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=IRJ41_014151 {ECO:0000313|EMBL:KAI7803968.1};
OS Triplophysa rosa (Cave loach).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=992332 {ECO:0000313|EMBL:KAI7803968.1, ECO:0000313|Proteomes:UP001059041};
RN [1] {ECO:0000313|EMBL:KAI7803968.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Muscle {ECO:0000313|EMBL:KAI7803968.1};
RA Peng Z.;
RT "Comparative genomics reveals that relaxation of natural selection precedes
RT convergent phenotypic evolution of cavefish.";
RL Submitted (FEB-2021) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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:KAI7803968.1}.
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DR EMBL; JAFHDT010000011; KAI7803968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W7TRI3; -.
DR Proteomes; UP001059041; Linkage Group LG11.
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:UP001059041};
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 295..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..501
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 101864 MW; 2CF8BA814880356E CRC64;
MESIPKKDTE STCVLCCQDI DIFAVGKCDH PVCYRCSTKM RVLCEQSYCA VCREQLDKVV
FIKKLVPFTA LNIHQYQCEK KYDIHFGDGK IYAQFRKILS HECPQCPESK VFSKFEELEQ
HLRKQHELFC CKLCAKHLKI FSYERKWYNR KDLARHRTQG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DADGAQEYYS DYQYLSEHFR ESHYLCEEGR CSSEQFTHAF
RTEIDYKAHK AAAHSKSRAE ARQNRQIDIQ FTYASRQQRR NEGLVGVEDY EEVDRFNRQR
PGRGRAPGGP QNVRSWRYNR EEEDREVATA LRASLATRSQ EERSHVQDRN NKPRKEEKME
SDELRSTRSV AKPPNEMQAR SMKSTSSLAG VDFPLLGAAA PLAASAIKPT PVSLKEDDFP
SLSGMLVSAP MTPAYTGQPR KHSSFQEEDF PALVSKIKPL KPQSSTASAW SQAGSKPTPN
KPVVLPTKQT SAVSSSILSA SDPPPSGRVP QTLTNSSSRR KKKLTPAETN KAPPKLRCPS
SSDEEDSMNS KTAQEIRAVP TMLDISTLLT VKVGSSQPNP KTSKKKQANS SSSFCTPLHT
PESVSKNAHK ENVPETKPPD ISLTKGPTTS KTNSFMNGHT EKPTEAQSCT SFPENTPSPI
KQPVTDQVPP PMEEDFPALT SKKPPPGFKS AFPLKSTPSV LPPPPGLVPV VSKPPPGFTG
IALNSNVVEP TVSAVNRSTP AIGSYLIPEN FQQRNMDLIQ SIKNVLQNDE TKFNEFKNYS
GQFRQGILPA VQYYKSCQEL LGENFNRVFN ELLVLLPDTR KQQELLTAHG DFKALEKQQQ
SWKPKKNKKK AWQTDNTSIS LELDCQVCPT CKQVLALKDF NTHKTLHNGD DDFPSLQAIS
KIIS
//
