ID A0A3P8SND8_AMPPE Unreviewed; 965 AA.
AC A0A3P8SND8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000013486.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000013486.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000013486.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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; A0A3P8SND8; -.
DR STRING; 161767.ENSAPEP00000013486; -.
DR Ensembl; ENSAPET00000013844.1; ENSAPEP00000013486.1; ENSAPEG00000009595.1.
DR GeneTree; ENSGT00940000158097; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265080; Chromosome 8.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16726; RING-HC_MIB2_rpt1; 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; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; 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; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
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; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 62..142
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 148..200
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 211..289
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 526..558
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 559..591
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 592..624
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 693..717
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 727..759
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 31..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 106013 MW; 16AF95A078196DD9 CRC64;
MFKSGLKIMG ITPDLFPETP LVPSLQAISS VRAGSAPQKP RRRSSCSGSD SVARPRPLPS
ACRPGPERGS MEVGMRVVRG LDWKWGNQDD GEGHVGTVVE IGRQGSTTTP DKTVVVQWDS
GTRTNYRTGY QGAYDLLLYD NAQIGVRHSN IICDSCKKHG IMGMRWKCKV CFDYDLCTQC
YMNNKHDLSH AFERYETAHS QPVSLAPRQN LPRIILKGIF QGVKVVRGPD WDWGNQDGGE
GKVGKVVDIR GWDTESGRSV ASVTWSNGTT NVYRMGHKGK VDLKYVSDGQ GGFYYKDHLP
KLGEHAELQR QESADGHSFQ QGDKVKCLLE VDILRQMQEG HGGWNPKMAE YICRIGTVHR
ITDRGDVRVQ YSNNIRWTFH PGALTKVNTF GVGELVRVLE DMESVKRLQA GHGEWTDSMT
PVLGQAGKVL KVYADGDLRV AFGGQTWTFN PACLSAQPVE VDANLMTAEN PSESGSTVIS
VLEKLLSQST EQDNPSRLVI EAAHGSANKV RELVQKYPDK VDIKNQGKTA LQVAAHQGHM
EVVKALLQAN SSIEVKDEDG DTALHYTAFG NQAEIARLLL SKGANVNLLN NSMCTALHIA
VNKGFTDVVR VLTEHSADVN LQDSYGDTPL HDAIAKDFRN IIEILVVVPN IDFTQQNHRG
FNLLHHAALK GNKLATEKIL ARARQLVDVK KEDGFSALHL AALNNHRDVA EILIKEGRCD
INIRNNRNQT PLQLAVTQGH TDLVQLLVAE GADVNMEDED GDTAMHVALL RPQLANVVLN
PSVGTSSTEE TSEGCSSTSL YCRLNSSGLL GSTELNVGTA IACFLAHEGA DINYANHKGK
SPLDLVADST MVQLIKSFSE KHRLQRLQAI TCGQGLSSAN LRRVHTTPNT MTNLVLPTPP
GPSECLICSE LALLVLFCPC QHSVACEECA HRMKKCIKCQ VTITKKIRQG KKNPLIPVVW
YVFIN
//
