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Database: UniProt
Entry: A0A182HHM1_ANOAR
LinkDB: A0A182HHM1_ANOAR
Original site: A0A182HHM1_ANOAR 
ID   A0A182HHM1_ANOAR        Unreviewed;      1213 AA.
AC   A0A182HHM1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Anopheles arabiensis (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7173 {ECO:0000313|EnsemblMetazoa:AARA000724-PA.1, ECO:0000313|Proteomes:UP000075840};
RN   [1] {ECO:0000313|Proteomes:UP000075840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dongola {ECO:0000313|Proteomes:UP000075840};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   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 arabiensis DONG5_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AARA000724-PA.1}
RP   IDENTIFICATION.
RC   STRAIN=Dongola {ECO:0000313|EnsemblMetazoa:AARA000724-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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; APCN01002428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182HHM1; -.
DR   EnsemblMetazoa; AARA000724-RA; AARA000724-PA; AARA000724.
DR   VEuPathDB; VectorBase:AARA000724; -.
DR   VEuPathDB; VectorBase:AARA21_012960; -.
DR   OrthoDB; 45541at2759; -.
DR   Proteomes; UP000075840; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd16724; RING-HC_MIB1_rpt1; 1.
DR   CDD; cd16725; RING-HC_MIB1_rpt2; 1.
DR   CDD; cd16727; RING-HC_MIB1_rpt3; 1.
DR   CDD; cd02339; ZZ_Mind_bomb; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR042056; MIB1/2_ZZ.
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   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR24202:SF53; E3 UBIQUITIN-PROTEIN LIGASE MIB1-RELATED; 1.
DR   PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13606; Ank_3; 1.
DR   Pfam; PF06701; MIB_HERC2; 2.
DR   Pfam; PF18346; SH3_15; 2.
DR   Pfam; PF13920; zf-C3HC4_3; 3.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 8.
DR   SMART; SM00184; RING; 3.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 6.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
DR   PROSITE; PS51416; MIB_HERC2; 2.
DR   PROSITE; PS50089; ZF_RING_2; 3.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW   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}.
SQ   SEQUENCE   1213 AA;  130117 MW;  F1D48A892C2552CD CRC64;
     MACASTSSTA SMELVGPAGP TNVAAAARPS RFTMEGVGSR VIRGPDWKWG KQDGGEGHVG
     TVRNFESQEE VVVVWDNGTA ANYRCAGAYD LRILDSAPTG IKHEGTMCDT CRQQPIFGIR
     WKCAECNNYD LCSICYQSDK HHLRHRFHRI TTPGGEKTLL EPRRKSKKIA VRGIFPGARV
     VRGVDWQWED QDGGNGRRGK VNEVQDWSSA SPRSAAYVVW DNGAKNLYRV GFEGMADLKV
     VNDAKGMTVY RDHLPLLGEY GPGRAPNNFQ IGDQVTVDLD IEIVQSLQHG HGGWTDGMFE
     CLSTTGTVVG IDEDHDIVVA YPSSHRWTFN PTVLTIVSSP MMLLADNQPQ QFAVGDFVKI
     CSDLERIKIL QRGHGEWAEA MVPTLGKVGR VQQVYHDNDL KVEVCNTSWT YNPLAVTKVA
     SSSDGATAVT TNGERLSAIL KKLFEPHASG DTTEELVKAA ANGDKAKVEE FLIGSAGGQN
     VAPSSSSAAG AAASLGESQS VVKVDVNGVF AGHTALQAAS QNGHLEVIEV LLRHNADVEI
     EDKDGDRAVH HAAFGDEPGV MGMLAKAGAD LNARNKRRQT ALHIAVNKGH FNVVKTLLEL
     NCHPSLQDSE GDTALHDAIS KEHDNMLALL LDNGADITLT NNNGFNALHH AALKGNPSAM
     KVLLTKTNRL WIVEEKKDDG YTALHLAALN NHVEIAELLV RMGKANMDCQ NVNLQTALHL
     AVERQHVQIV KLLVREGANL NIPDKDGDTP LHEALRHHTL SQLRQLQDVE GFGKILMGLR
     NNTDKKASAS IACFLAANGA DLTIKNRKLQ TPLDLCPDPN LCKTLIKCYN ERKTEDMDSM
     TLGMASHTGG GGGPTMPLRR GGYRPPDEPI ASTSAGNPGT SGLGSGGLNH AQIDANLLMG
     LSKMSIQPNA AGEANTNVSV NHNTASSGGG GGVSVACSVA TTTAGDSSGP LDECLLCSDQ
     KRDTVFKPCG HVVCCENCGP RIKKCLICRE SVLSREKIDE CLVCSDRKAS VFFKPCGHMV
     ACEHCAPIMK KCVQCRTQLE QMVPLSVCSG GQGSVINIQH PVEDGKKDLL HNHNASQQQQ
     QQLLQGTNKA GLGVAMNNTM SPNASALAAG SGSGGVALGN NGQAVGGASS STGSSNTNAS
     LIVSPNNLNL VDDFQKLQQQ LQDIKEQTMC PVCFDRIKNM VFLCGHGTCQ MCGDQIDGCP
     ICRKTVEKRI LLF
//
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