ID A0A267FHC6_9PLAT Unreviewed; 1027 AA.
AC A0A267FHC6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=BOX15_Mlig033066g2 {ECO:0000313|EMBL:PAA73171.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA73171.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA73171.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA73171.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA73171.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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 -!- 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:PAA73171.1}.
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DR EMBL; NIVC01001028; PAA73171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267FHC6; -.
DR STRING; 282301.A0A267FHC6; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000215902; 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 CDD; cd16520; RING-HC_MIBs-like; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
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; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF06701; MIB_HERC2; 3.
DR Pfam; PF18346; SH3_15; 1.
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 SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 3.
DR SUPFAM; SSF57850; RING/U-box; 2.
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; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000215902};
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..120
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 160..212
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 223..301
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 556..588
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 589..621
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 622..654
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 725..757
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 758..790
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 894..929
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 983..1016
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 68..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 957..984
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1027 AA; 110485 MW; BDBA27605FD61D9D CRC64;
MLLLQIGLRV VRGPNWKWQD QDGGEGSVGT VVEIGKSVSS TAVAASADLA ATASRLTGSS
KSATSAAASN SASSSSVNHS SSYNSSGPEK TVFVQWDNGS RTNYRVGYQG AYDLRVFDSA
PVGIRHTVSC SECNRRSLAS AGGSLSASSG GRSSVGAVGR SPHHQQQQQQ PVIQGIRWTC
AECDNYSLCS ACYHGDAHNL DHEFYRFDYN KSARVSVGKR RGCVKMDARG IFAGARVVRG
PDWDWGRQDG GDGRPGRVLD IRGWENESGR SVANVRWDNG LSNVYRVGHK GKVDLKLLQA
PASWGLYYRD HLPVLGERLD SVGGGCPYRV GERVRVARSE AQLRVMQEGH GGWNEKMSEL
VSQCGHVHRI TERGDVRVQF DSGQAQRWTL NPDALERVAS LRAGQLVRVL DDETELRRCL
VDSWQDWHRS LAGSLVKVHS VHSDSSALVV TSENRTARLD PSVLVRLQQS AETAANNRMA
SHDIGAPLNV LVQKLIELTS STDAGAASTS TAGGSAASSS SLGACRSFLA EVSQGNLETV
RQMLASRATP VDGSINGKTG LMVACHQGHL EVVKLLLSHK ASVSAIDEER DTPLHYAAFG
NQPAAIKLLA AAGAPMDAQN NTGCTALHVA VNKQHKDCVQ ALLQLGASPN CQDGYGDTAL
HDAIGRASTD ILNLLVQHQQ LKPHSRNKRG FEPLHQAALK GNAGAAAALL ARFGPEDCGN
RRKDDGFAPL HLAALNGHVS VARALLDAGC NAEIRNQRGQ TPFLLAVCQA KLAVASLLAD
RGADVNAADE DQDRACHFAA MRSGPYSKLP EFRLHAAPIL APTVALLDWN SKAPMPAKLV
LTAWMLQLGA DLGAVNRKGQ TAVSLLGNEP DIVTCLNLFH RKLSLERADA DSLCQVCQDD
LSSVTFEPCG HRISCDHCSA KMRLCLRCKQ PIERKLRDQD LIPAVAAAAA AEAGTSGGRQ
QNNLFEMQEE LQRLREKVAN EECSICMDNP RTVAFLCGHQ ACTDCAQALV QCHMCRKPIQ
ARIQLYK
//
