ID A0A182GMC4_AEDAL Unreviewed; 1382 AA.
AC A0A182GMC4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=RP20_CCG012419 {ECO:0000313|EMBL:KXJ75047.1};
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160 {ECO:0000313|EnsemblMetazoa:AALF012419-PA.1, ECO:0000313|Proteomes:UP000069940};
RN [1] {ECO:0000313|EMBL:KXJ75047.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ75047.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ75047.1};
RX PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA Yan G., Tu Z.J., Fang X., James A.A.;
RT "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT insights into its biology, genetics, and evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN [2] {ECO:0000313|EMBL:KXJ75047.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ75047.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ75047.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:AALF012419-PA.1}
RP IDENTIFICATION.
RC STRAIN=Foshan {ECO:0000313|EnsemblMetazoa:AALF012419-PA.1};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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; JXUM01074492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JXUM01074493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KQ562832; KXJ75047.1; -; Genomic_DNA.
DR STRING; 7160.A0A182GMC4; -.
DR EnsemblMetazoa; AALF012419-RA; AALF012419-PA; AALF012419.
DR VEuPathDB; VectorBase:AALC636_004070; -.
DR VEuPathDB; VectorBase:AALF012419; -.
DR VEuPathDB; VectorBase:AALFPA_065019; -.
DR Proteomes; UP000069940; Unplaced.
DR Proteomes; UP000249989; 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 CDD; cd12882; SPRY_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; IPR035773; SPRY_RNF123.
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; SM00184; RING; 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 Reference proteome {ECO:0000313|Proteomes:UP000249989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 50..229
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 1292..1330
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 648..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1382 AA; 154271 MW; EBAC862BB7338FC2 CRC64;
MDFSSVLSSV FGGECPIKVD TRDKDDSSSL LSGYLVAIGQ WLEEKLQSHL FPEDDEDSET
AIAGRLGPRR TVFDATEDGS ILVSKDKLTL QSQNAFSTVK ANCCVYSGRW MYEVQLRSKG
VMQIGWCSAH CKFTQDTGVG DTRYSYGLDG SKQRIWHVYT QKYGPFWRSG DVFGVCVDMD
EGRIEYYRNG AALGEAFKDI ERGPGLALYP AVSLAFNDSL TANFGGSPLK HPVEGYRCLQ
DAPNVLLFQA ECLLKYIVNL SGAISRHTRN DQDSPTSDTA FPSFESIYML IASMLIEKIA
PLLANSYVVE DKVFKYMKGM CVLRSNTNNE SPIQPGSPES TLGMFLTLLW TYLEPEEIKL
FLKKLLNFLA NTYKETPVDL EYEKQRKIIV ILTCICQHPQ TRKYLLEYKF FKKNCLPLFL
YTKPPDESTL EQLLPDDAIW TEGLGGSKQV YLAACEKLKA HTGVLYTLQK NLIHILLNNR
DGDEEESGTP SSRRIFMTKL RKFVMDNNAE MRGLYSSSTQ PAIGLSFLCT LLDVARTLWD
EEISTASTSS TASQRPYIDY RYFYDGTFRY SNIDRIGGVL SYLKKHFRQQ LIEKLGDDHT
SLAAVDQQSD LRNEIAAFNA FLDSAIFLVS GGPNSTYSLI SRAASNTGSE LHHQEGDTSL
GSGRPGGNSG PIKAGNMDER QSICELLDCA VIFYYSVAHK YVVMIADLRD NICHLSDILL
ETKTNCDDVV HNLEELKRSS AVGFSKAHEE LMQELDTRFG QRKSIFAKRS MELARKQAWY
RSVALGSHRR SLLCWLMGIV FETLKRFSEE DVLFSFLPET YINVIPVLLD TILDFSYHDT
GIQHDLSADS ELIGWAADFL ALHLADTRVI LASCKDALIQ ALGSLTCHQA GISALEQASP
KSQQAFVRAL LRPYENRAWG QSNWLLLRFW LGDGFGYRES RPPCVWQGGK EAGRSLGLYR
SRAKNGSHTG LLHLVAPACP SKHFQRMISE ILSKDEPYCT TFLNSVLSQL NWAFSEFIHI
LQDIQNVSQR DEQQVIETKQ LKICSMCFEL TVSLMRALEM ILTITPGLLQ DASRANSEII
LGRICQLAIQ VLSRVTIPPG CFQHVMDLCL PDLSNVTHFA IISAAIGILL ALMKNELLED
DTTIASSSSS SSASTIGTSN GTVIGITKIP RISKHLLTDT SFHITSLEFA LGEIKTPIAA
SSHQAPRGNF DPKMRAHIDP LTNEVRVPSP FRAIIGVKEI VPDPPIIKFN MADYPSHVTK
DELNKVRRLI EILQLRQTLL SEITVLSEDS LCPICYAKQN SAVFDPCQHQ SCENCIIQHL
MNNKQCFYCK LAISKVVRTD GAVIYENSVP LKISLTTTGS SQTDDISQAV DEGDGPSGSP
RL
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