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Database: UniProt
Entry: A0A0L0BN55_LUCCU
LinkDB: A0A0L0BN55_LUCCU
Original site: A0A0L0BN55_LUCCU 
ID   A0A0L0BN55_LUCCU        Unreviewed;       431 AA.
AC   A0A0L0BN55;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=FF38_12572 {ECO:0000313|EMBL:KNC21363.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC21363.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC21363.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC21363.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC21363.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNC21363.1}.
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DR   EMBL; JRES01001623; KNC21363.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0BN55; -.
DR   STRING; 7375.A0A0L0BN55; -.
DR   EnsemblMetazoa; KNC21363; KNC21363; FF38_12572.
DR   OMA; ANQFTVL; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd17086; RAWUL_RING1_like; 1.
DR   CDD; cd16739; RING-HC_RING1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR032443; RAWUL.
DR   InterPro; IPR043540; RING1/RING2.
DR   InterPro; IPR042741; RING1_RING-HC.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46076:SF3; E3 UBIQUITIN-PROTEIN LIGASE RING1; 1.
DR   PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR   Pfam; PF16207; RAWUL; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          46..86
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          143..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  47101 MW;  A76306AC39F3E9DB CRC64;
     MASLEPAQNK TWDLSLYELQ RKPQEIITDN TEIAVSPRSL HSELMCPICL DMLKKTMTTK
     ECLHRFCQDC IITALRSGNK ECPTCRKKLV SKRSLRPDPN FDLLISKIYP SREEYEAIQE
     KVMAKFNQTQ SQQALVNSIN EGIKLQSQNR PQRFRTKGSG GGGGAAGGGG RAAGANHNSN
     NAHNVSNESN TNGNESDTNT RESTTTAPLA ATVAINAPTT TATTHSNTTI AAAVSSVTGS
     IAASTSSTRM DDGGSNPPSV RSTPSPVPSN SSSSKPKRAM SVLTSERSEE SESDSQMDCR
     TEGDSNIDTE GEGNGELGIN DEIELVFKPH PTEMAGDNQL MKALKENCIR YIKTTANATV
     DHLSKYLALR LTLDLGSELP EAYRMLNFCI YVAPQPSQLV ILNGNQTLHQ VNEKFWKVNK
     PMEMFYSWKK S
//
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