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Database: UniProt
Entry: A0A2G8KK47_STIJA
LinkDB: A0A2G8KK47_STIJA
Original site: A0A2G8KK47_STIJA 
ID   A0A2G8KK47_STIJA        Unreviewed;      1042 AA.
AC   A0A2G8KK47;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=BSL78_14774 {ECO:0000313|EMBL:PIK48373.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK48373.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK48373.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK48373.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK48373.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIK48373.1}.
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DR   EMBL; MRZV01000526; PIK48373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8KK47; -.
DR   STRING; 307972.A0A2G8KK47; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000230750; 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:UniProtKB-UniPathway.
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-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13857; Ank_5; 1.
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; 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; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230750};
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..75
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   DOMAIN          81..133
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          144..222
FT                   /note="MIB/HERC2"
FT                   /evidence="ECO:0000259|PROSITE:PS51416"
FT   REPEAT          481..513
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          514..546
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          648..681
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          682..714
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          861..895
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          912..947
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   1042 AA;  114114 MW;  9352734C2158488A CRC64;
     MESTVVGYRV VRGPDWRWND QDGGEGNLGT VVEVGKKGSS TSPEKTVIVQ WDNGSRTNYR
     MGYHNAYDLL IYDNATVGIQ HVNILCDACN KQGFMGMRYN CTQCQDFDLC ASCYHGDKHD
     LSHHFLLYIT PSSVGVKLPP RSSAIKIGYR GLVPGAKVMR GPDWDWGNQD GGDGKIGRIK
     DIRGWDSESD RSVANVQWSN GNTNVYRVGH KGKVDLRCLD SVKGGTYYKD HLWKLGQKVA
     KNSVSAYGKK WSFVHGEKVK VNLDVAVLKI MQGDHGGWNA KMEEYVGQEG YVHRITEKGD
     IRVQYSDGIK WTFHPGALTK VTTFSVDDNV RITSDIEKLR KLQLGHGEWH EDMKMALGKV
     GRVIKIYKDG DLRVCVNGQS WTYHCECVTA VESSQDVNVT VAAEASSSQQ QQQDPSGNVQ
     RLKDRIRVLR KGEDCLDKLV TAAARGDVSV VGDLVLKRPG WVSYFTSRWI KQSLGLSTDR
     VQKTALQVAA HQGHVDVVKI LVQAGANLSI PDQEGDTALH YAVFGNQPGI VRYLLEHGAE
     VNLVNKGQCS SLHVAVNKSY MQCVEELIKK ECNVNLQDCC GDTALHDAIA KDNTEAIDIL
     TNIADAEFTL ANRRGFNVLQ HAALKGNKRA TEKLVRAARQ LVNRKKDDGF SALHLASLNG
     HRDVVEVLLT TGQADINIRN NRLQTPIHLA VSQGHVPVVE LLVSRGADLL ASDEDGDTCL
     HVALMKPVVS PGGENLPVIR GIQATLGVSI RPGVALACFL IQEGADPSYL NTQSKSALDL
     VKRNEAYPLS SSLWIIEGRN LFFEEIRFYL ALIGTIQPGR RIAVPNDTSS HVIEDANITD
     ESDAIQQPQL VMSTSVSTTT CKLCHKMADC CLKPCKHITC CMECSQLFAL CPVCKGTIES
     REKIETTDQS KCSLCKTNVA DVTLLPCRHR AACADCFQKM SVCAVCSEPI VEVITAGSAK
     AVAGVSANSL SKSLSKDKEK ISKITTSNDK GRQMECAICM ERESSVVFLC GHTTCGTCAK
     PLKYFGVVGG GRGWGVKAVV AD
//
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