ID A0A3B0K644_DROGU Unreviewed; 1331 AA.
AC A0A3B0K644;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=DGUA_6G018403 {ECO:0000313|EMBL:SPP83540.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP83540.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) 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; OUUW01000007; SPP83540.1; -; Genomic_DNA.
DR STRING; 7266.A0A3B0K644; -.
DR OrthoDB; 3145419at2759; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd16541; RING-HC_RNF123; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363:SF5; E3 UBIQUITIN-PROTEIN LIGASE RNF123; 1.
DR PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 74..253
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 1264..1302
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1331 AA; 151251 MW; 2A900ACF36DEFEDB CRC64;
MSISKLFVKV FNENIFDQLD QENPYSDLDD DLEGANCSTL PESKPLKIDE LSVSKQMTIV
KTWLDDKFQQ IQTDSNEEIR RLYAETESRI GPDLTIFDVD YTTTVRVSSD RLALRSQGSF
NTVRTNCCVY GGRWMYEVQL HTKGVMQMGW ASSLCQFNEN SGVGDTKLSY GYDGSKQQIW
HISTKKYGDK WQIGDIIGVT LDVDKELIEY YRNGRSMGVA FNKLEKGPGI AFYAAISLGY
TQGIQANFGN RPFVYPVPGF QPLMARPILK LRRANLLMNY LTNLAGIFAK YNAQYKASAN
QSEARVSTKK TVYCIFATML IERFTNEIFD SYIIEDVLLA RISSMTSLTA EKENPHSVLQ
GLLSLFWNFM EGDEIKFVLR KMVNALLSTF THTVQGLDYE KHRQALAMLH CLCLNEQTRK
FLLEGKLFKK HCIAFFLYIH PLEFYIMEEL LPDYMAWTEG IDGPKEKYLG IVEKVRKVTE
PLYAAQKDFL STLMINRDGT PTSPSSRTLF LAKMRRYVID LSMEQRPFHA FFFMQSSIQH
PLDAPVALAF VCILIDQSRN MFREELPGKN VEVNADYFFD GTFDYMHFDR VGGVLSHLRK
VHRSDIDARL GSVRTQQIYD EDRSNSRTNE MDTTLYLLGE NVHNVAVIGH TQGTNNTTFT
HFLNPRTNQG GEATPGNADA EASLCELLDL CIIFYYSAGH KYIVKIASVR DEIAALNDVL
KETKYYREDV ERKLLALEQH ANVCMNDGHQ HVMGELRAKF SQRQNVFATR SISLSRKQIW
LRGVALNNQR RSLLIWMLER MIRTLTNASN TGPLFAFVPE VYVNTLPILL DAVMDFSHHD
MKAQFEATDS ECAVTSAAEF LGVHSADPRI VLASCKDSLL QALGTLTCHK AGVRALERSS
RKSQVALVRA LLRPYENRAW GQSNWLLLRF WMGEGYAYKD SRQPCVWQGG SLPLHMGLCR
SRSKNETHTG LLHNVAPANP SKHFQRLIGS KLIEDEPFAT SFLNSVLSQL NWAFSEFILL
LQEIQNTAQR QENTLFEPKQ LKICSMCFEL TVSLMRCLEM IITVAPEIVT DPSRPNSDLL
LNRICQLISQ VLSRVTVPPG CFQFVVDMCS ADLNAVTHFP IITAALGILL ALMRSEMDVD
ITPQKVTRLS RAFLTDPSFQ FATLEFALGE IRTPLLEQKD IPRGNFDPSA RPHIDPLTND
LRVPFPTNSK RIRADPPIIK FALTDFPTHV NSEEIDNIRR LIDGLRMKQT LLSDITLPSE
DSLCPICCAK PITAVFTPCK HQSCSDCIMQ HMMNSKVCFY CKTTIHTIET LDGTLIYSNE
DVMQTPMNER A
//