ID W8BH84_CERCA Unreviewed; 1074 AA.
AC W8BH84;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=MIB2 {ECO:0000313|EMBL:JAB89004.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB89004.1};
RN [1] {ECO:0000313|EMBL:JAB89004.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB89004.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
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; GAMC01017552; JAB89003.1; -; mRNA.
DR EMBL; GAMC01017551; JAB89004.1; -; mRNA.
DR EMBL; GAMC01017550; JAB89005.1; -; mRNA.
DR AlphaFoldDB; W8BH84; -.
DR UniPathway; UPA00143; -.
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:UniProtKB-UniPathway.
DR CDD; cd16726; RING-HC_MIB2_rpt1; 1.
DR CDD; cd16520; RING-HC_MIBs-like; 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); 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 InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 2.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00184; RING; 2.
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; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 1..76
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 82..134
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 145..223
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 463..495
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 496..528
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 REPEAT 630..663
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 664..696
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1031..1064
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 904..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 118755 MW; 719711A0836BBB5B CRC64;
MRSAIQPGIR VVRGPNWIWQ NQDDGEGHVG TVCEIGRSGS THSPENTVVV NWDSGHRTNY
RVGYQNQYDL IIVDNAQVGV RHSNVVCDGC SKPGIAGIVF KCAQCSNYHL CAYCYGADLH
DTEHIFIRYT TPTSLGVRVP PRKNSKRIQL KGIFIGAKVV RGPDWEWGQQ DGGEGKTGRV
MEIRGWDNES CRSVANVSWV TGSTNVYRLG HKGNVDLKCT FPSIGGYYYK DHMPVLGQTE
EQQPVVPTVK PMFSVGDRVK VCLDVDALMK LQQGHGGWNP RMVEQLPKWG TVHRITDKGD
IRVQYDNCPN RWTFHPAALV KVISFRVGDL VTIINDANKV QQLQKGHGEW IDLMRYALGK
HCKVIKVYSD GDLRIQQLDD GFEWTLNPKC VRLERSPLAT AAERSNSMMD LSHRRTDHVM
TPLSGLSGTS VADKLVREAA QGHLDFVKQY LDAHSEQVNV MSGGKACIQV AAHQGYVDLV
KYLITKGANV NVVDKEGDSA LHYAAFGNQP ETMRVLLQNG ADINFLNSSH CSALHICAHK
KTPHCVRELL QFGADVNIQD SYGDTALHDA IGKENTEVVE LLCNAPNLDF LIKNNRGFNV
LHHASLKGNV VAAKRILQLA RQLVNVKKDD GFAALHLAAL NGHARVVETL IVEGLAEIDI
RNNRRQTPFL LAVSQGHASV IERLVTLGCD IMARDEDGDN AMHLCVIKKT NLQQATEPSG
EDSPKIRSIF DNLAHILDDR LMYTILCYLS SCGCRVEQNN KGTNIFGWIT NKDMKELILK
YQPTPSPSST NEASNSNPAV EVENNIQNLN LNTDNEGETA GAAAVSNSGD TDIVTDDISQ
PNNFTQMSTS HCSTPTHHVD SSTVEPGVKK LNSDRQTPAV NASVAGNGGN VLDTQYMHMT
AIPSTSGVTQ STSNRKMTRK PEGVPAPKAS PKATPPPPPP THATFHIGPQ ECIVCDEKLQ
LIKFEPCQHQ ISCEECGLRM KKCLRCGVQI ERRIAAGGRV IVSSDQTRVP SADRLRYLEN
KIQEYEETHY CSICMERTRD VAFLCGHGAC SRCAETLRTC HMCRKTILRK INLY
//
