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
//