ID   A0A3B3UWP9_9TELE        Unreviewed;       693 AA.
AC   A0A3B3UWP9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000017273.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000017273.1}
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}.
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DR   AlphaFoldDB; A0A3B3UWP9; -.
DR   STRING; 48699.ENSPLAP00000017273; -.
DR   Ensembl; ENSPLAT00000026471.1; ENSPLAP00000017273.1; ENSPLAG00000021621.1.
DR   GeneTree; ENSGT00940000158097; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16726; RING-HC_MIB2_rpt1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR040847; SH3_15.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR   PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13857; Ank_5; 1.
DR   Pfam; PF18346; SH3_15; 2.
DR   Pfam; PF13920; zf-C3HC4_3; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 7.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   REPEAT          190..222
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          223..255
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          256..288
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          357..381
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          391..423
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          649..682
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   693 AA;  75925 MW;  CF027C16511CA08F CRC64;
     MQEGHGGWNP KMAEYICRIG TVHRITDRGD VRVQYSNNIR WTFHPGALTK VNTFGVGELV
     KVLDELENVK RLQAGHGEWT DSMTPVLGQV GKVLKVYADG DLRVAFGGQT WTFNPACLMA
     QPAEVDANLM TAENPNESGS TVISVLEKLL SQSTEQDNPG RLVIEAAHGS ANKVRELVQK
     YPDKVDIKNQ GKTALQVAAH QGHTEVVKTL LQANSSVEVK DEDGDTALHY TAFGNQAEIA
     RLLLSKGANV NVLNNSMCTA LHIAVNKGFT DVVRVLTEHA ADINLQDSYG DTPLHDAIAK
     DFRSIIEILV VVPNIDFTQQ NHRGFNLLHH AALKGNKLAT EKILGRARQL VDVKKEDGFS
     ALHLAALNNH RDVAEVLIKE GRCDVNIRNN RNQSPLQLAV TQGHTDLVQL LVDEGADVNM
     EDEDGDTAMH VALLRPQLAN VMLTPSAGGS STEEGSEGCS STSLYCRLNS SGLLGNTELN
     VAMAIACFLA QEGADISYAN HKGKSPLDLV GDGTMMQLIK NFSEKHRLQR LQAITCGQGL
     SSASLRRVHT TPNTMTNLVF PTPAGPSECL ICSELALLVL FCPCQHSVAC EECAHRMKKC
     IKCQVTITKK IRQDQTEVDC SPGTENSEQH NLLEQLQSRY RQMEERITCP ICIDNHIKLV
     FQCGHASCID CSAALKTCPI CRQTIRERIQ LFV
//