ID   A0A3B4TV96_SERDU        Unreviewed;      1332 AA.
AC   A0A3B4TV96;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Ubiquitination factor E4B {ECO:0000313|Ensembl:ENSSDUP00000009928.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000009928.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000009928.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   STRING; 41447.ENSSDUP00000009928; -.
DR   Ensembl; ENSSDUT00000010120.1; ENSSDUP00000009928.1; ENSSDUG00000007227.1.
DR   GeneTree; ENSGT00390000009300; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261420; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   CDD; cd16658; RING-Ubox_UBE4B; 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:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT   DOMAIN          1268..1332
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..400
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1332 AA;  149240 MW;  B27B067D49CFE922 CRC64;
     MEELSADEIR RRRLVRLAGG QTSQPSTPLS TPLTSPQRET PPGPLHGHSG ATPQPLPPAA
     SQSLGLIVHS GTPATSPMGN SGVAYGSQSS EGVSSLSSSP SNSLETQSQS LSRSQSMDID
     TASCEKSMSQ VDVDSGIENM EVEDSDRREK RNLTEKETSA NSDVSEEQAL QLICKILRVS
     WKEQDRDVIF LPSLAAEFHQ NSKDAYSDFK DLIGQILMEV LMMSTQSRVH NPFASLTATS
     QPIAAAKSPD HRLTLVQPSS LGGSPMGPSA GSFGASSLSS LYGCGSPHPM ALDAAKRTSP
     SLPTPTTSSV PSTPSTPQFI VPPSPSVTTT PRHSLNPPSA PMPISQRYRP YSVNSPWGVP
     SPSSSGQRGF SFIGPSPNPA GPSVPPNTPV PVPPPSPQSL SLSSPWARNL PSSTPPAMVP
     PSPRSNTQQT AFGSRIPPSS LGACGGGMSC DSASDRFTIE ACKETEMLNY LIERFDSVGM
     EERKAPKMCS QPNVSQLLSN IRSQCISHVA LVLQGTLTQP RNPLQQSLLV PYMLCRNLPY
     GFIQELARIT HQEEEVFRQI FIPILHGLAL AVKECSFDSD NFKFPLMALA ELCEIKFGKT
     HPVCSLATSL PLWCPKPLSP GCGREIQRLS YLGAFFSLSV FAEDDTKVGD KYFSGPAITM
     ENTRVVSQSL QHYLESARGD LFKVLHNILL NGETRELALN YMAALVNYNV KKAQMQTDDK
     LVSTDGFMLN FLWVLQQLSM KIKLETVDPY YIFHPRCRLA VSLEETRLKA TMEELKSWLT
     ELHEDPTKFS EPKFPTECFF LTLHTHHLSI LPGCRRYIRR LRAIRELNRT VEELKNSESQ
     WKDSPLASRH REMLKRCKTQ LKKLVRAKAC ADVGLLDENL LRRCLQFYST VIQLILRIVD
     PAYPNITLPL NPEIPKSFAA LPEFYIEDVA EFLLFVVQYS PQVLYEPCVQ DIVTFLVVFI
     CSQNYIRNPY LIAKLVEVLF VTNPAVQPRT QRFSEMMENH PLSVKQLVPA LMKFYTDVEH
     TGATSEFYDK FTIRYHISTI FKSLWQNIAH HGTFMEEFNS GKQFVRYINM LINDTTFLLD
     ESLESLKRIH EVQEEMKNKE QWEQLPREQQ QSRQSQLTQD ERVSRSYLAL ATETVEMFHI
     LTKQVQKPFL RPELGPRLAA MLNFNLQQLC GPKCRDLKVE NPEKYGFEPK KLLDQLTDIY
     LQLDCARFAK AIADDQRSYS RELFEEVISK MRKAGIKSSI AIEKFKLLSE KVEEIVAKNS
     QSEMDYSDAP DEFKDPLMDT LMTDPVMLPS GNIMDRSIIL RHLLTESMLE SVPELKERIH
     AWMREKQGGR PV
//