ID H3B381_LATCH Unreviewed; 767 AA.
AC H3B381;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000016352.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000016352.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AFYH01075747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01075752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3B381; -.
DR STRING; 7897.ENSLACP00000016352; -.
DR Ensembl; ENSLACT00000016466.1; ENSLACP00000016352.1; ENSLACG00000014407.1.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00940000158097; -.
DR HOGENOM; CLU_007287_2_0_1; -.
DR InParanoid; H3B381; -.
DR OMA; NIRINMM; -.
DR TreeFam; TF324147; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008672; 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: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 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; 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; 2.
DR Pfam; PF18346; SH3_15; 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; 4.
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:UP000008672};
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 1..71
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 77..129
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 140..218
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT REPEAT 442..474
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 475..507
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 508..540
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 609..633
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 643..675
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 767 AA; 84796 MW; 2EBAB825C4B92FCB CRC64;
MSLIGVRVVR GPSWKWQDQD GGEGHLGTIT DISEQGSAHG KAAIVQWDCG ECRKYRIGVS
NNYDLLLYDN ASTGVHHVHV TCDGCNHIGI WGIRWKCVQC HNFDLCSICY MSDKHNIGHS
FHRILTPSSQ GVAVPPRQNS KKIQAKGIFV DATVRRGKDW KWGNQDQAKG NPGKVAAVRG
WNSTAINNAA TVIWSNRYRN NYRLGFGGMV DLKCTNPATG GFYYKDHLPK LGETAVIAKS
TFKKGDKVKC KIFQTQQMHL GLLSELLTPI GQVKSVTTEG DIVVQYGNSN EVQYKPENII
RFYEVGDYVK IIEDLETVKK LQSGHGGWAE GMRQTLGHIG QVIKVLPKGD LKVSIGGSTW
TYNPACVYTA DPSEVQKEMN TNSDENDEAS GGTFVFVKTK TFNFDVDHDD PVQLVIAAAK
GNMDEVKELV HKFPSKVDIK HKGKTALHVA SHQGHTEIVK ILLEAKTDMK IKDDNEDTAL
HFAAYGNEHE VANMLLRNGA LANSVNAANQ TPLHIAAQKG YTSVARVLCD NKCDVNIQDS
DGNTPMHIAV DHDFEEIIDC LSSMKNRNYS LANHSGYNPL HTAAVKGSKL GVQRIIARAA
NLVDEKKEDG FSALHLAAYN GHTDVVKVLI KEGRCNINAL NNRGQTAFML AVSRGHADTA
FLMVRENCNI NVEDEDGNTA LHLLFRNQEL FSEAKYQLEP DSTLLDILND TGLIANKTIY
VGEALAYFLA KEGADLHHSN NRGRKPLDYL KNDIILNTVK SFAKAYR
//
