ID W5JBU7_ANODA Unreviewed; 443 AA.
AC W5JBU7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=AND_008124 {ECO:0000313|EMBL:ETN60264.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN60264.1};
RN [1] {ECO:0000313|EMBL:ETN60264.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN60264.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN60264.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC008124-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; ADMH02001961; ETN60264.1; -; Genomic_DNA.
DR AlphaFoldDB; W5JBU7; -.
DR STRING; 43151.W5JBU7; -.
DR EnsemblMetazoa; ADAC008124-RA; ADAC008124-PA; ADAC008124.
DR VEuPathDB; VectorBase:ADAC008124; -.
DR VEuPathDB; VectorBase:ADAR2_003651; -.
DR eggNOG; KOG0311; Eukaryota.
DR HOGENOM; CLU_056557_1_1_1; -.
DR OMA; FCIYIAQ; -.
DR OrthoDB; 460116at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000673; 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:UP000000673};
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..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 47606 MW; 58875BD9940543DC CRC64;
MASVEQMQSK SWDLSLYELH RAPQEAITDN TEIAVSPRSL HSELMCPICL DMLKKTMTTK
ECLHRFCSDC IITALRSGNK ECPTCRKKLV SKRSLRPDPN FDLLISKIYP SRDEYEAHQE
RVLAKFNSSH SQQALVHSIN EGIKLQSQNR PNRKQKGENE LCPSNASSSS NSTTVQSTAP
AAGNASNGAN EPTSKEGTPG SAGAGGSGSG SATASTSGTT STAPSTVSSG TGAASSSSTV
AVGGGAGSSS GAASTTAGEQ SRQSSNPPSV RSTPSPAPSN ISSASKAKRP RSVMTSERSE
ESESNSEMDG RTEENDSNLD TEGDGNSEVG SDEIELVFKP HPTEMTGDNP LLKALKENSI
RYIKTTSNAT IDHLSKYLAM RLTLDLDQEL PESYRLVNFC IYIAQQTDQL VVLSGNQTLQ
QVNEKFWKVV NKPLEMYYSW KKS
//
