ID A0A1J1HJ46_9DIPT Unreviewed; 2079 AA.
AC A0A1J1HJ46;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CLUMA_CG001833 {ECO:0000313|EMBL:CRK88047.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK88047.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK88047.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CVRI01000006; CRK88047.1; -; Genomic_DNA.
DR STRING; 568069.A0A1J1HJ46; -.
DR OrthoDB; 45541at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-UniPathway.
DR CDD; cd16724; RING-HC_MIB1_rpt1; 1.
DR CDD; cd16725; RING-HC_MIB1_rpt2; 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; 2.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
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; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR004299; MBOAT_fam.
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; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF03062; MBOAT; 1.
DR Pfam; PF06701; MIB_HERC2; 1.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00184; RING; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
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:PRU00228}.
FT TRANSMEM 47..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 857..927
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 933..985
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 996..1074
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 1353..1385
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1386..1418
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1419..1451
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1485..1509
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1519..1551
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1683..1718
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1730..1765
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1304..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1834..1886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2079 AA; 233303 MW; FB454618A2EE3848 CRC64;
MAYKSSLYYD EFDYENYQEA LDYESYEDHI TNFNDALSCS FAVSKQIALQ LLILLFVNFI
YRMIRYANIA EFIKHLSSSL LGYFSTFIFF TTGNFYVCFL VFISYGFLKF LQLIGVKKQG
FLVIAFQIVL IFTCEILELD GNVWQHVRGS ALIISMKAIS VAFDVSSTKI PKLPPIYEYV
GYVLCPANTV LGPFTTFASY KNCNRNKFSL NLFSQIIVNS SISIFFIILS SCFLNYLISD
NNLKYLLMYR DALNFRSSHY FISFMSSAVL LMSGIDSKMT SNIFGYQVTR PLDIELPRSL
IPVVISWNIP IHLWVKSYVF HNLKHFGKFK AIILTYLISS SLHGLNVQLA AVLLSIGIFT
FVEYRLRNTL AEILDACVAA NKCNLDSTKS CTSKGHKNNT TLYWVKMINF AFGVSTVVLL
AYLDMLQSFN RCTVLNKVDY GIISSMRQFS RQMEDQKRKQ NHNEQKMYNN VNEGNANKLR
KWISVTPEPR QPGLTFTVLD YNILSQQLLE QHSYLYQGHS KHALRWNQRF FTLIGEILYN
NPDILCCQEV QNTHLSDIQS RLRSLNYDVI YKKRTGDKPD GCAIFYKRHL FHLIEDHKIE
FEQPGIEVDN NNNMTFQWHQ NVLNIYNLQL LDRENVAVVC KLSLKTDPSV HFVVATTHLL
YNPRRQDIRL AQVQILLAEL DRIAKVSNNE EEQKYLPIIL SGDFNLQPHS APYNLIVNGM
VNYANLTRRT LSTSGKGTNN QTNGRLLLPI KLGITDECQH VNHEIKLYHS ENNKTRTDHD
IELTKEIVNL FQTGILKHNF KFSSAYKDSD DYVSTYQDRW ILVDYIFYSD AINTQTNGSS
LKLLSYLTLP SSEGCRNIGL QIPNTYQGSD HLLLAARFFL EFDGGEGHVG TVRNFESAEE
VVVVWDGGTA ANYRCAGSYD LRILDSAPTG IKHDGTMCDT CRQQPIYGIR WKCAECNNYD
LCSICYHSDK HHLRHRFYRI TVPGGDRILM DPRRKSKKIA VRGIFQGARV VRGVDWQWED
QDGGNGRRGK VIEIQDWAAT SPRSAAYITW DNGAKNLYRV GYEGMADLKV VNDAKGATVY
RDHLPLLGEN TATKSHNGFQ IGDSVIVDLE LEVVQSFQHG HGGWTDGMFE CLNNPGKVVG
IDEDHDIVVS YPSGNRWTFN PAVLTKMASN ATDDSANQFA VGDFVKICSD LERIKILQRG
HGEWAEAMIP TLGKVGRVQQ IYYDKDLKVE VGNTSWTYNP LAVTKVASSS DGSVSAVAAN
GERLSAILKK LFEPQVSSDI TEELVKAAAN GDSAKCEMFL NPNGQVQAPI DHQPTGSPLG
DQQEQTNQQS LPSTSSGPTV STVNQANVNG VFAGHTSLQA ASQNGHLDVI KVLLKYNADV
EIEDKDGDRA VHHAAFGDEP AVIKLLAQAG ADLNARNKRR QTALHIAVNK GHNNVVKTLL
ELRCHPSLQD SEAIHHAALK GNPTAMKILL SKINRPWIVE EKKDDGYTAL HLAALNNHVD
IADLLINMGK ANLDRQNVNL QTALHLAVER QHVQIVKLLV RKGANLNIPD KDGDTPLHEA
LRHHTLSQLR QLQDVEGFGK ILMGLRNNTD KKASASIACF LAANGADLTV KNRKLQTPLD
LCPDPNLCKI LIKCYNEKHT EDIETTTMDD KHLSNGMNNE NNNQQQTQQT KQVESSDINV
DECLLCSEQK RNTVFKPCGH VVSCEACGSR IKKCLICRET VSSREKIDEC LVCSDRKASV
FFKPCGHMVA CDHCAPIMKK CVQCRTAIDQ MVPFKVCCGS TGTIAKVVQS IDDHKKDAHI
LQGTNHNGHN INMNNCNSIN NKFSVVATSS SSSSAQSTYN NLSSTSGMHN HNNNSNNNNN
LMHSSNLNQA TNSTNLASNN APTTSTITKA DQESNVNLFD DMQKLQQQLQ DIKEQTMCPK
RQSQGAKQEM KHGRMFKKNT ATSIKKQTLA LRSRDGSIDN PDLLHLVGIY LNEILSLYGK
PIVRQPNWIL TPAYSNGLIA MGTRFEDDFP QINLGISLGV QDSWVPEGAT AISAIIVDEE
DNMITMSSGV QIKNGGKLIS QNPKNKLTNL SFVKLAFHQ
//
