ID A0A182TLS6_9DIPT Unreviewed; 1009 AA.
AC A0A182TLS6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Anopheles melas.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC004652-PA, ECO:0000313|Proteomes:UP000075902};
RN [1] {ECO:0000313|Proteomes:UP000075902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEC004652-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC004652-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR AlphaFoldDB; A0A182TLS6; -.
DR STRING; 34690.A0A182TLS6; -.
DR EnsemblMetazoa; AMEC004652-RA; AMEC004652-PA; AMEC004652.
DR VEuPathDB; VectorBase:AMEC004652; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000075902; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16726; RING-HC_MIB2_rpt1; 1.
DR CDD; cd16520; RING-HC_MIBs-like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF06701; MIB_HERC2; 1.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 9..87
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 328..360
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 361..393
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 394..426
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 495..519
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 529..561
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 966..999
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 742..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 108703 MW; 6E3A4177791560AA CRC64;
IRLPPRKGAA KIQLKGIFVG ARVTRGPDWE WNNQDGGPGK TGRVMEIRGW DNESCRSVAS
VAWASGSTNV YRLGHKGNVD LRYVQPAVGG YYYKDHMPVL GQPEEQQPVS PPVRSHFYVG
DRVQVAIAED RLKMLQQGHG GWNPRMAEYL TKVGIVHRIT DKGDIRVQYE GCANRWTFHP
AALVKIYSFN VGDMVTFISD PAKMQHLQKG HGEWIETMHN VLGKPGKVIK IYGDGDLRVQ
QLDDDMAWTV NPKCVKLASS CHAAATERSN SMADLSNQRN QEHHMAPLAG LTGGTAADKL
VREAAQGNLD YVQSQLSMTP EAVNYVSGGK TCLQVAAHQG HVELVKYLIL MGANVNVVDK
EGDSTLHYAA FGNQPEVMRV LLQHNASIDE LNSSHCSALH ISAHKKPPHC VKVLLEFGAN
VNMQDAYGDT ALHDAIGKEN TEVVELLCSC PTLDLTIRNH RGFNALHHAS LKGNVHAARH
IIRLARQLVN VRKDDGFAAL HLTALNGHTR VIEVLVQEGQ ADINIRNNRS QTPFLLAVSQ
GHTAAIEKLV DLGADVRARD EDGDNAMHLC IIKKGNLVHD VSPTDAPKIH DIYQSLAGIV
IEHRLMYALL CFLASEGCPL DVNRKGARVL DWIGSPQIKE IIVEYERTRL AREAAAAAAP
NGPVISTSYP VAHGLGAAAA GSCSRNLPNA EEDTQQLLCN FEGMSIAPAG STTAAPSIEA
VTGGSGRVEK LADAAGSGSL ALENGLAGGS GLQHASPPPP PSSSSSTLSP AMGDSPASTT
GAPIPPNHGM FAKPMMKPCR GGSSHLSGMF GTTTNAAAKH NSPRQFVQDK SVPQPPTPAA
PASAGAASSA SPTPPPVPPP LPTTPAHQLH QLLHQPPLPP TDAPRECIVC NETLALIVFE
PCQHQIACAE CGVRMKKCLT CGLHIERRTT AAGCPLEGSK DGRLLSADRL RYLESKIMEI
EETHCCSICM ERRRNVAFLC GHSSCSKCAE TLKICHMCRK PITKKINLY
//
