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Database: UniProt
Entry: A0A0M4EC69_DROBS
LinkDB: A0A0M4EC69_DROBS
Original site: A0A0M4EC69_DROBS 
ID   A0A0M4EC69_DROBS        Unreviewed;       403 AA.
AC   A0A0M4EC69;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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_chr3Lg2357 {ECO:0000313|EMBL:ALC45191.1};
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:ALC45191.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC45191.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC45191.1};
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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; CP012525; ALC45191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4EC69; -.
DR   STRING; 30019.A0A0M4EC69; -.
DR   OMA; LDEVCPY; -.
DR   Proteomes; UP000494163; Chromosome 3l sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR   PANTHER; PTHR11224:SF10; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50103; ZF_C3H1; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          50..77
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          233..286
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          315..344
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         50..77
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         315..344
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          81..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  45951 MW;  C48C695EA0F1CB73 CRC64;
     MHLVYMFIYV CQNEHLVWPE IIFESVCTCD MSSVAVATID EAPISSVTPG RSQALCHYYL
     RGVCRFGDNC RYSHDLTLQQ GQSDEELPGG DSTTTEANAD AKASTSRRNW ANAPVFVPGR
     LYAVDESASS SSAAVQNGIS WAEIVGGPST NDEPVKLAKP QSLEQVCPYE NPCPYRQYCP
     YRIHLELCEM CDQFCMHPTD QAQRKKHKRD CLQQHEQAME LSFAIAQSKD KTCGICFDTI
     MEKVGKEKRF GILPNCNHIF CLECIRTWRQ AKQFEHKITR ACPECRVCSD FVCPSAFWVE
     TKEEKDKLLN DYRAALGAKD CKYFKKGEGK CPFGNKCFYK HALPNGDIVD VGLPKRARKL
     HSQNELIDLL DIYLWEFVDR RDYHWLELLS SDISDSSDYT DEE
//
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