ID   A0A3B3TAZ1_9TELE        Unreviewed;       987 AA.
AC   A0A3B3TAZ1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000039598.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000039598.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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       Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
CC   -!- SIMILARITY: Belongs to the Arkadia family.
CC       {ECO:0000256|ARBA:ARBA00007622}.
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   AlphaFoldDB; A0A3B3TAZ1; -.
DR   STRING; 1676925.ENSPKIP00000039598; -.
DR   Ensembl; ENSPKIT00000020607.1; ENSPKIP00000039598.1; ENSPKIG00000016836.1.
DR   GeneTree; ENSGT00940000157691; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16681; RING-H2_RNF111; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR029306; RNF111_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR16200:SF1; E3 UBIQUITIN-PROTEIN LIGASE PLR-1-RELATED; 1.
DR   PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR   Pfam; PF15303; RNF111_N; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          935..976
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..517
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   987 AA;  105918 MW;  BD43B3DFF2D0B2FD CRC64;
     MKSDIPPSAM RQCDPVKGAL AGPEPVEAKD FVGDVELVAK AGSELAPLCT DSRQDAAKAD
     PGRGLGGRKK RRGQQAGPSD CVPIEGQSEE ERPLESSLSD CVSSPSSSPR FGDSDTLSSE
     DEEGLGAPWV GPRAENRRQP QQSKAAPAGG TGRPHAILGR TRGSRTHRWP QPEAEAVLLK
     RPCLTHRKHV AKGAVATGVG GVSPRTPRQK ERLLLQRRKR EVIARRKYAL LHSSSSSSSS
     SSEELTSDDS SSSSPSFTGP EDELYVDVSS SSSHADGAIV AAGPLDEDVV VIEATSTQLV
     QPSEEINVTS TDSEVEIVTV GDGYRPRPSG GHGRMQWGPS CSQGRALEHR SRHRNSTVIQ
     PLRQSAGEVV DLTVDEDDPS MAAASSGSSS QPMRSSSSFL SASTSDPPHD GPGPSCRVAA
     FASLPQSTLG TQAHGGDIAV PPLQDDGRRG SLAVPGEAGS SAMPRLPSCC PQHSPCGGAA
     PGHLPLGHAH SSCQQGPPPS QHSHSHHPHH HHHHRVASPP QPPVVFPEPS CPLERPVGVP
     GSCPTAGGAA SQCHDQTLPV DLSSGALRGS VANGPPGTSF HAASAFDPCC PGSSTRPPLY
     TSQAAPPAGA SQPSTMDTFS SGMVAPAQLS SCRQYVNPPY GPLTRLLHHQ TLSSCPHSHS
     SAPPAAQVDY VIPHPVHPFH APLPPHSHGH TMPPVPPPSL PTEAPLGSSV QRLHQHEVFQ
     RMEVQRRRMM QHPTRAHERP PPHPHRMHPN YGHGHHIHVP QTMSSHPRQP EQRAAWDLGI
     DASVTVTPYP PGHLPPPLPH YHPPPRLHHF PLPFMVRLLL YSLCVPMMGR HAALGYKEIL
     IRGRNAVSDA PLPPQHAGMP DVSYPHIRYI SSRMPGFGRS YEDLLHLEER LGTVNRGASQ
     GTIERCTYPH KYKKRKLHSK QDGDEGMEED TEEKCTICLS ILEEGEDVRR LPCMHLFHQL
     CVDQWLLTNK KCPICRVDIE AQLSAES
//