ID A0A087XPQ6_POEFO Unreviewed; 960 AA.
AC A0A087XPQ6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 28-JAN-2026, entry version 49.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000007759.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000007759.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPFOP00000007759.2}
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 EMBL; AYCK01010980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007565794.1; XM_007565732.2.
DR AlphaFoldDB; A0A087XPQ6; -.
DR STRING; 48698.ENSPFOP00000007759; -.
DR Ensembl; ENSPFOT00000007771.2; ENSPFOP00000007759.2; ENSPFOG00000007766.2.
DR GeneID; 103147412; -.
DR KEGG; pfor:103147412; -.
DR CTD; 90850; -.
DR eggNOG; KOG2231; Eukaryota.
DR GeneTree; ENSGT00390000014178; -.
DR OMA; CEKKYDI; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000028760; 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:UP000028760};
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 290..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..461
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..521
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..619
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..657
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 107386 MW; 256084C5DAB3D526 CRC64;
MNSTTVKESE KTCVLCCQDI DIFALGKCDH PVCYRCSTKM RVLCDQKYCA VCREELDKVV
FVKKLKTFQA LPYQQFPFEK RYNIYFVDEM THSQYRRLLL SECVRCPEPK VFSRFEELEQ
HMRKQHELFC CKLCSKHLKI FSYERKWYNR KELARHRAHG DPDDTSHRGH PLCKFCDERY
LDNDELLKHL RRDHYFCHFC DADGSQEYYS DYQYLSEHFR ESHYLCEEGR CATEQFTHAF
RSEIDYKAHK AAAHSKNRAE ARQNRHIDLQ FNYAPRQQRR NDGMVGGEDY EETRHNRGGR
GRLQMGQKSW RYSREREEED RQVEAALRAS MAMQRQTERA AMLRQMERPM TQKQTERPVT
QRQTERPVTQ RQTERPVTQR QTERPAMQER NTSKHCRDER IERIELEEPR HMTGPIKPSN
KPPVKTMKSS NPGDEDDFPA LGASAVAPIA KPGPAAPAAA ALKEEEFPSL SSTAVSSPMT
PAYSGQPKKN SSFQEEDFPA LVPKVRLPKP AASANSAWSN STPVAKPNPQ LPPSSRAPPP
LSAAPSGPQL LSSSNSSSSR KKKKVGEREK ATPPSLSDDD DGGGGMTQEE FCSVPTMLDI
SSLLTINGAN NKPSTTPSSA NPPPNLDLPF SKAGKKKKQK NSAASSASAP AISDTAAPVN
AISVETAAQK ENVPEKTWSK SLSSAVTATS MSASGPTDAT SAVCRDSPRV ITPPVVVPAP
EPEEEFPALM TKKPPPGFKT SFPVKTTAPS PPPVMPPPGL GSSATKPPPG FTGIPLNSNV
VEPAVSLPQK MPTNGYLVPD DFQQRNLELI KSIKKYLHHD ESSFNQFKNY SAQFRQSVIS
AAQYHRSCKD LLGDNFNSIF NELLVLLPDT GKQQELLTAH ADCKALEKQS GASGGKKNKN
KKNAWQTPAT PANTAAELDC QVCPTCRQVL APKDFNSHKT LHITESEEFP SLQSISRIIS
//
