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Database: UniProt
Entry: A0A0M4E8T3_DROBS
LinkDB: A0A0M4E8T3_DROBS
Original site: A0A0M4E8T3_DROBS 
ID   A0A0M4E8T3_DROBS        Unreviewed;      1019 AA.
AC   A0A0M4E8T3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000256|ARBA:ARBA00040077};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=Dbus_chr2Lg561 {ECO:0000313|EMBL:ALC38476.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC38476.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC38476.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC38476.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CP012523; ALC38476.1; -; Genomic_DNA.
DR   RefSeq; XP_017855343.1; XM_017999854.1.
DR   AlphaFoldDB; A0A0M4E8T3; -.
DR   SMR; A0A0M4E8T3; -.
DR   STRING; 30019.A0A0M4E8T3; -.
DR   GeneID; 108608467; -.
DR   OMA; WLTEIAM; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000494163; Chromosome 2l sequence.
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; cd16657; RING-Ubox_UBE4A; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT   DOMAIN          939..1013
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   COILED          459..486
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1019 AA;  116226 MW;  4A2643D805C9F081 CRC64;
     MTSVEETENP FAALLNSGPN PNGVSKQLIE KILLFTLNNE LAKDVQSKRN TAILCLAEVI
     VADNSADDTL TEELLAHALF ERLMLSDASK YLISNSQCSA NSQEEAAETR AMQYLYGAFT
     RCEQLQRNCI DQEKEHCKRI LELILNNAST CMRQPELFAP QSFAAQWLEL FEQSDEHDTS
     TQEFLVRVAC KVIEEDEPLE ALGALKAIFY PMLSDLHKQL VKENLITIKK NIFWILGFFV
     RDKRAGMLGE LLIDYTTPNP KAKGGEYMDT LFGQLLCISI MPKWQNAPYE FFREITLVTQ
     QSDPSLWGLL AHHQQSMFAL MKQLLVLSPA TKKKTLQWIA NCLDANVARG HLWSTMNMNL
     EQTVHSTASD AFMTSLSAVL MRLCAPLCAP SLKVMLVDPT YCAVAEASDR QAKGVHMLKA
     YEETCLLPAE EGEQRLTAEK YNFITEIFYM AQKAFELGNR ACIERLNRMM RELQNTQNAY
     QEVATRDPNN DLTKNLFRML QDQMQQVLCI RNGLAEPQND TAILKFFEAS AIWLTEIAML
     PRESYETALD KKDFAPQLLR NLELLSLSPP FVAPYMKSVP ECIIDNIAAY LNFCRSFAGD
     QFIQMYASSH DAFFKMILLF MGSAELVKNP HLRAKLADAL EFLLPNSQAA TNNRKLFHTH
     IFDSHPDRLQ LVRSLLNVFV SIEMTGQSVQ FEQKFNYRRP MYAIMEFLWT KEEHVQSFRQ
     LATEAESNME AIEPPLFLRF INLLINDAIF LLDESLSNLE QIKQLQQAQD AGEWNNLSHS
     ERQQQTTNLH HLGMLARFDN ILGRDTINIL KLLTTEIKSI FCHNSMVDRI AAMLNYFLLH
     LVGPRRERFK VKDKKEFEFD PAQTVLEIAH IYINLSTDNS FCLAVSQDGR SYSDQLFGYA
     ENILIRIGGG QLIGDMSEFA LKVQKMSADY KVEQELLADA PEEYLDPIIS TLMTDPVVLP
     SSNVTVDRST IARHLLSDQT DPFNREPLTM DKVKSNEKLK LEIEQWIEGK RNGATRSKS
//
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