ID A0AAD5FND9_SILAS Unreviewed; 914 AA.
AC A0AAD5FND9;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=C0J50_17629 {ECO:0000313|EMBL:KAI5622751.1};
OS Silurus asotus (Amur catfish) (Parasilurus asotus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Siluridae; Silurus.
OX NCBI_TaxID=30991 {ECO:0000313|EMBL:KAI5622751.1, ECO:0000313|Proteomes:UP001205998};
RN [1] {ECO:0000313|EMBL:KAI5622751.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Chongqing {ECO:0000313|EMBL:KAI5622751.1};
RA Zhang Y., Wang D., Peng Z., Zheng S., Shao F., Tao W.;
RT "Comparative genomics of catfishes provides insights into carnivory and
RT benthic adaptation.";
RL Submitted (JUL-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 -!- 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:KAI5622751.1}.
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DR EMBL; MU551610; KAI5622751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD5FND9; -.
DR Proteomes; UP001205998; Unassembled WGS sequence.
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:UP001205998};
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 336..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 102900 MW; DF8E09F71F31B953 CRC64;
MESAMKKEAE NVCVLCCQDF ELFAVGKCDH PVCYRCSTKM RVLCEQKYCA VCRVELDKVI
FVRKLQPFAA LTHHDYQAEK KHGIYFADGK IFAQFRKILQ PECPQCPEPK VFSKFEELEQ
HMRKQHELFC CKLCAKHLKI FSYERKWYNR KELARHRTQG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DADGAQEYYS DYCYLRYHFG ESHFLCEEGR CSTEQFTHAF
RTEIDFKAHK AAAHSKNRAE ARQNRQIDIQ FNYAPRQQRR NDGNLTGLVG ADDYEEVDRF
NRQGRPGRGR PQGLHQNVRS WRYNREEEDK DLAAAIQASQ AARRQAERGQ IHERGGQKPR
KEEIIDGEEL RSSRGPLKPP SEMQGRSVKN SVPLKGEDFP VLGAGVPTLP PPIQSMVKPA
PVSLKEDDFP SLVHSGTMVS GPMTPAYVAQ ARKPSSFQEE DFPALVSKIR PHKPQENTTS
AWSQVGSKSG MLNKPPVVLP TKTVLHSAPV FSASDPPPSS TIPQVQAFHR KKKLISSQCA
KATSKVKSPV SSDDEDPENG KKVQEIRAIP TMLDISSLLT VKTGSSQPSN KNGKKKRPPS
ATPSGNSANN AELVTTAAHK ENVPETKPPD GCVPKGIVAP KSNMFINGYK EKPKENKDNI
TPEEPPAPKK QPILETPSVP EEEDFPALIA KKPPPGFKSS FSMKNVQTVL PPPPPGLVPT
ISKPPPGFTG VPLNSNLAER AVPVFNRPTS SLGTYHMPEN FKQRNMDLIQ SIQNLLQNDE
SKFNEFKNYS GQFRQGLISA AQYHKSCHEL LGENFSRVFN ELLVLLPDTQ KQQELLTAHA
DFKAMEKQQP GSKGKKNKKK AWQSCTSTNT LDLDCQVCPT CKQVLAPKDF SDHKTLHIGE
DDFPSLQAIS KIIS
//
