ID   A0A671LVX9_9TELE        Unreviewed;      1076 AA.
AC   A0A671LVX9;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 25.
DE   RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000256|ARBA:ARBA00040077};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC107690452 {ECO:0000313|Ensembl:ENSSANP00000022558.1};
OS   Sinocyclocheilus anshuiensis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Sinocyclocheilus.
OX   NCBI_TaxID=1608454 {ECO:0000313|Ensembl:ENSSANP00000022558.1, ECO:0000313|Proteomes:UP000472260};
RN   [1] {ECO:0000313|Ensembl:ENSSANP00000022558.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSANP00000022558.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC       ligase in conjunction with specific E1 and E2 ligases. May also
CC       function as an E4 ligase mediating the assembly of polyubiquitin chains
CC       on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates
CC       'Lys-48'-linked polyubiquitination of substrates.
CC       {ECO:0000256|ARBA:ARBA00037624}.
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 ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
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DR   RefSeq; XP_016344287.1; XM_016488801.1.
DR   RefSeq; XP_016344288.1; XM_016488802.1.
DR   AlphaFoldDB; A0A671LVX9; -.
DR   Ensembl; ENSSANT00000024044.1; ENSSANP00000022558.1; ENSSANG00000011639.1.
DR   GeneID; 107690452; -.
DR   KEGG; sanh:107690452; -.
DR   OrthoDB; 20295at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000472260; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0036503; P:ERAD pathway; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:TreeGrafter.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd16657; RING-Ubox_UBE4A; 1.
DR   FunFam; 3.30.40.10:FF:000055; Ubiquitin conjugation factor e4 a; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13931:SF16; UBIQUITIN CONJUGATION FACTOR E4 A; 1.
DR   PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472260};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          994..1068
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          29..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1076 AA;  122940 MW;  FC5103593C0A63F4 CRC64;
     MTDQGNNNQN ISQNPFAALF SSLADAKQFA SGQKQRRHAD QQSVDSGESQ SESDNSVSDS
     IEDNDDSVAE ISRSFRSRQE LCEQLNVNHM IQRIFLITLD NSDPSLRGGN GIPPCCVYLE
     EMAADLDGQD WLNMDTIEQA LFSRLLLQEP GNHLIYMTSC SAVNLSADRD AGEKRVVPYL
     YACYRRAKEE ITKVPEKLLS YAVQCKNLTV SNARTVLLTP EIYISQNVYE QLLDLLLESV
     RGAQFEEVVE FLEDVIASLL ADQEVRTFGE VMVPVFDIFQ GRVKDLDLCQ LLLYSYLEIL
     LYFSRQKDIS KVLMEYIQPK DPNSGIQYQK TLLGTILNIS CLLRTPGVVE NHGFFLNPSR
     SSPQEMKVQE SDIYQFMEQF HDKLYQILKN LLQQSSETRH LLLSWLGGCL QANMGRAKIW
     ANQMPEIFLQ MYASDAFFLN LGAALLKLCQ PFSRPYSPKL LTFNPTYCLL KELSEEERRN
     RNVHARGLDK ETCLIPVPPQ QTVEFAQSYS LLTENLIFTQ LTMYLGFHRL HDQMVKMNQS
     LHRLQGMWRD TQLSGGPAAA ELREQFERLM TVYLSTKAAT TQPAMLQNCL NLQASCAALL
     VQLSLGNQGP EHIPLTFPLP ALENSLLCFV PEFFAENMGD FFIFLRRFAD EVLESSAESL
     EHVLTFITVF MGNVDRMKNP HLRAKLAEVL EAVMPHMETL SPGAAQPIMF QRQRVFSTYR
     HAPQLAEALI TVFVDIEFTG DPHQFEQKFN YRRPMYAILK YMWGEESYRE SIKRLADYAS
     ENLEAMNPPL FLRFLNLLMN DAVFLLDEAI QYLSKIKILQ LERDRGEWDS LAPDARREKE
     SSLQMLGQLG RFHNIMSNET IGTLAFLTSE IKGLFVHPFL AERIISMLNY FLQHLVGPKM
     GALKVKDFSE FDFKPQQLVS DICTIYLNLG DEENFCATVP KDGRSYSPTL FCQTVRVLKK
     INKPDDMIVS FSILADKIKS LADRHQQEEE TYSDAPDEFL DPIMSTLMLD PVLLPSSNVT
     VDRSTIARHL LSDQTDPFNR SPLTMDQIRP NEELRQQIMK WLADHKQSNQ QMGPSG
//