ID   A0A3B3XGN9_9TELE        Unreviewed;       776 AA.
AC   A0A3B3XGN9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000014145.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000014145.1}
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   ---------------------------------------------------------------------------
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   RefSeq; XP_014837416.1; XM_014981930.1.
DR   AlphaFoldDB; A0A3B3XGN9; -.
DR   Ensembl; ENSPMET00000022061.1; ENSPMEP00000014145.1; ENSPMEG00000016527.1.
DR   GeneID; 106914840; -.
DR   CTD; 64844; -.
DR   OrthoDB; 1342875at2759; -.
DR   Proteomes; UP000261480; Unplaced.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16812; RING_CH-C4HC3_MARCH7; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR14471:SF1; E3 UBIQUITIN-PROTEIN LIGASE MARCHF7; 1.
DR   PANTHER; PTHR14471; MARCH7/10 E3 UBIQUITIN PROTEIN LIGASE FAMILY MEMBER; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          622..692
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   REGION          21..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..548
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   776 AA;  84799 MW;  284FDF9BBC3589A1 CRC64;
     MDSRSRRLPF CLSSSRSSYT FTPAVSSSLG SSRRYSREPV LNNDRFQSAS SPYKADTDKQ
     SSRLLSSSRD YSSSDTRSPS WKLPSLTSSG RSYDRPRVES ALSSRSKASD AEGRSGICSG
     VLSASDDAES KRAKLSYSNR LYSRTANTSL TGSGYSSNVL SSSSRGANDS LDSSWGSYRL
     LSRPTPSSTK PLLSSREQET KTEPGLSSLG ERRARNPGLV SSLYQTDRVT STYAQGARPK
     ETTYSPSSSS SAVRESSLSR HASSFSSQQP TSSRLHDLSS RSAARFTNAP PSLRSTQEQA
     RSAVCSGVFA SHSSSSSSSS SSSSSNTPWQ SSPVRRPEPA LPRPTAEGGE PEGRSSTRRL
     LSRLFSRRSS QDSSSCSSSV RSLDDDSPST SGESVDSDEG AGSSNADPDA GSAATALDSL
     RSLRTDLSTI QESNPGHGGL GRSRTASWRE PSVSSSSSGG GGGRGSSWLS APFRARCPPL
     LSRLRRYARE DGSHSPSGSE QDYSRPQHLL RTWDDLEHKA SQDDDDEEEE EEEEEEEDDD
     DEDEEEEGAF ALAESYADGI EDETLPELEV VFSPRRRLGV LENLSAAVGR GERQPDQKEK
     TLSSKDQEKL RKIKEKLLME DSDEEEGDLC RICQMREESS SNPLIQPCHC TGSLQFVHQE
     CIKRWLHSKI SSGTNLEAIT TCELCKEKLR LNIDNFDIQE LYRTHVQSEY DEFISSGLYL
     VVLLHFCEQR FSDVLGAVDA AGLPMEKAMR KTRTAGRLST SLTWTMTKST DHLTVT
//