ID A0A8X7WSG8_POLSE Unreviewed; 903 AA.
AC A0A8X7WSG8;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN Name=Znf598 {ECO:0000313|EMBL:KAG2455883.1};
GN ORFNames=GTO96_0007788 {ECO:0000313|EMBL:KAG2455883.1};
OS Polypterus senegalus (Senegal bichir).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Polypteriformes; Polypteridae; Polypterus.
OX NCBI_TaxID=55291 {ECO:0000313|EMBL:KAG2455883.1, ECO:0000313|Proteomes:UP000886611};
RN [1] {ECO:0000313|EMBL:KAG2455883.1, ECO:0000313|Proteomes:UP000886611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bchr_013 {ECO:0000313|EMBL:KAG2455883.1};
RX PubMed=33545088;
RA Bi X., Wang K., Yang L., Pan H., Jiang H., Wei Q., Fang M., Yu H., Zhu C.,
RA Cai Y., He Y., Gan X., Zeng H., Yu D., Zhu Y., Jiang H., Qiu Q., Yang H.,
RA Zhang Y.E., Wang W., Zhu M., He S., Zhang G.;
RT "Tracing the genetic footprints of vertebrate landing in non-teleost ray-
RT finned fishes.";
RL Cell 0:0-0(2021).
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:KAG2455883.1}.
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DR EMBL; JAATIS010009265; KAG2455883.1; -; Genomic_DNA.
DR RefSeq; XP_039630403.1; XM_039774469.1.
DR AlphaFoldDB; A0A8X7WSG8; -.
DR GeneID; 120542193; -.
DR Proteomes; UP000886611; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:KAG2455883.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000886611};
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 345..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..487
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAG2455883.1"
FT NON_TER 903
FT /evidence="ECO:0000313|EMBL:KAG2455883.1"
SQ SEQUENCE 903 AA; 102540 MW; 8935176BD6261DCB CRC64;
MASKLGKESE RSCVLCCQEI DIYALGKCDH PVCFRCSTKM RVLCEQKYCA VCREELDKVI
FVKKPDQFST ITTQNFQCEK KYDIYFSDLQ FCAQFRRILQ HECPQCKELK IFNKFEDLEQ
HMRKQHELFC CKLCAKHLKI FTHERKWYSR KELARHRMQG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DSDGGQEYYS DYDYLREHFR EKHFLCEEGR CNTEQFTHAF
RTEIDYKAHK AAAHSKNRAE ARQNRHIDLQ FTYAPRHQRR NEGVVGGEDY EEVERFNRNL
RGARGGGRGG QQNLRGSWRY NREEEDREIA AAVRASVAAR RREEKRQAQE RELIKPKKEE
TVENEDFKNS RSLPKQTSDI PGKDIPAKTV NNNGPLRGED FPALGSATPC TNKLAEVKLK
EDDFPSLSST VVSGPMTPAY TAATRKQSAF QEDDFPALVS KIKPQKSLGN TSSAWVSSSN
KNVSNISRPA SSNSPISVFP TKTSTTAVST SSLSQQKKKT ASSKGNNRQN DREKSIPSSD
EDDGQVGKTT QEIRSVPTML DISSLLTEKS SVQSISKIGK RKKVGGEKQN SSALLTSVET
VKKVSQKENV PETKSQPLHF PQPINSTLVN EDNLIIEHLD NSIENKNPPI TREPPGLKKT
FSLAPNLLPD EDFPALLPKQ PPPGFSAAFP LKNGPANISP PPGYLAPASK PPPGFTGVPL
NINTSENANS IVGKSASTTG MYTVPDNFQQ RNMELIQTIR NFLQNEESKF NEFKTYSRQF
RQGQMSATHY HKSCQELLGD NFKLVFNELL VLLPDTSKQQ ELLSAHRDIC LQENQGCNKP
KKNKTHAWQS NSTSSNKNSL ELDCQVCPHC LQVLAEKDFV AHKIIHREDD DFPSLQAISK
IIS
//
