ID A0A0M4EQ83_DROBS Unreviewed; 359 AA.
AC A0A0M4EQ83;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=Dbus_chr3Rg1864 {ECO:0000313|EMBL:ALC47114.1};
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:ALC47114.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC47114.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC47114.1};
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 -!- 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};
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DR EMBL; CP012526; ALC47114.1; -; Genomic_DNA.
DR RefSeq; XP_017845439.1; XM_017989950.1.
DR RefSeq; XP_017845440.1; XM_017989951.1.
DR AlphaFoldDB; A0A0M4EQ83; -.
DR STRING; 30019.A0A0M4EQ83; -.
DR GeneID; 108601964; -.
DR OMA; DERSADN; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000494163; Chromosome 3r sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR CDD; cd16667; RING-H2_RNF126-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710:SF4; E3 UBIQUITIN-PROTEIN LIGASE IRUKA; 1.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 236..277
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 305..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 38408 MW; 1939FF7A50E2EDF7 CRC64;
MAEAMVVEER TATPKRFFCH MCNVEINIPN TDYTCPLCSN GFVEELPANA PELSASTSNS
ASISDAGNIG TSFSPGGSGI LNVESLRNDI VSLLSMRNVP NLEITIEPNR RHVLGLGSGG
GAATPGSNIG GGRVRPANLD RLDNVLYDFL QSLPLSGATA EIVAGPGGSV GTGNSHMFFM
GNPGDYAWGR EGLDTIVTQM LNQMETSGPP PLSTQRINEI PNVKISAEEV ERKMQCSVCW
DDFKLDESVR KLPCSHLYHE NCIVPWLNLH STCPICRKSL ANDDDTEGTD EDYVWLNNMV
ETANRSRAQS AQSNTSSQTT TTTTAAAAAP AAASQSATAA APNQLNNVFT FDEDNMNLD
//
