ID T2MA48_HYDVU Unreviewed; 956 AA.
AC T2MA48;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN Name=MIB1 {ECO:0000313|EMBL:CDG68999.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG68999.1};
RN [1] {ECO:0000313|EMBL:CDG68999.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG68999.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
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; HAAD01002767; CDG68999.1; -; mRNA.
DR AlphaFoldDB; T2MA48; -.
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; cd16724; RING-HC_MIB1_rpt1; 1.
DR CDD; cd16725; RING-HC_MIB1_rpt2; 1.
DR CDD; cd16727; RING-HC_MIB1_rpt3; 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); 3.
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:SF53; E3 UBIQUITIN-PROTEIN LIGASE MIB1-RELATED; 1.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 3.
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; 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; 3.
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 7..77
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 83..135
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 146..224
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 451..483
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 517..549
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 550..582
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 619..643
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 653..685
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 785..820
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 832..867
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 912..945
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDG68999.1"
SQ SEQUENCE 956 AA; 105638 MW; 56D5736B8EDCFBEB CRC64;
MATAHNISID VCLSSTIGSR IVRGLDWKWG KQDGGEGHVG TIRSFESNEE VVVVWDNGSA
ANYRCSENYD LRILDSGPSG IKHDGTICDG CRCQPIYGMR WVCADCNNYD LCSVCYHADR
HQLRHRFYRI FAPNGNEVLM EPRKKAKKLI SRGIFPGARV TRGVDWHWEA QDGEAGRRGK
VVDIQNWSAT TPRSAAYVAW DTGAKNLYRI GFEGMVDLKC ISDAKGSPFY RDHLPLLGEN
LTTSQSMTKH WKIGDFVRVD LDLDIVQTLQ RGHGGWADGM VEAMGSIGVV FGFDEDRDVI
VSYASGNKWI FNPSVLTCGI SESDGPKKLA VGDIVQILND QEQVSNLQIG HGEWTDVMVA
TLGKIGCVTK VYHDGDLKVE VNGTSWTYNP KCLKRISSRG TNSASKILHF LESHSSKDPA
ELFIKAAAEG NVKNLEELCH FPNFDINVLY AGHTALQLAC QNGKLESIKF LLQLNADVEV
EDIDGDKAVH HATFYDESRT FALLKEANAD LNSRNKRRQT ALHVAVNKGH IGNIKALLDA
GVHVNLQDSE GDTALHDAIS KKRDDIVELL LNSGTDISLS NNNGFNSLHH AALRGNVKAV
QLILEKKDKP WIVNEQKDDG YCALHLASLN NHLEVAKLLI KLGHANVNIQ NTNLQTPLHL
TVQKQHEEIV KLLVSEGANV NVQDKDGDSP LHEALRNHTL LRLKEMQSVK DVSKLLMGFG
SQDFTKTSST SIACFLAEHG AQLACKNNKG QTPLDLCPDP GLCNALRQSY GQSIQKNKKM
LETECVVCSD MPREVIFSPC GHLVACSGCA PRIKKCLICK ELVQSRQRIE ECLVCSDKPA
SVLFQPCGHI PACSACSSLM KKCVQCRGTI LKMVPSIDLC GLKESSSSSL ICNNDILLLE
KQIQEMKEQT TCVVCLDRRK NMIFLCGHGS CQVCGDQLSE CPMCRKLIEK KILLFC
//
