ID A0A8B6GDW5_MYTGA Unreviewed; 986 AA.
AC A0A8B6GDW5;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=MGAL_10B002988 {ECO:0000313|EMBL:VDI62634.1};
OS Mytilus galloprovincialis (Mediterranean mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=29158 {ECO:0000313|EMBL:VDI62634.1, ECO:0000313|Proteomes:UP000596742};
RN [1] {ECO:0000313|EMBL:VDI62634.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T.;
RL Submitted (NOV-2018) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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:VDI62634.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYJE01008281; VDI62634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8B6GDW5; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000596742; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000596742};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 8..48
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 271..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..655
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 111722 MW; C69A02247C23F0E8 CRC64;
MESRMSSCPV CHEGIDVFAV GCCDHVICYK CSCRMRVLCE QFYCPICRTD LPQVYLIKEA
LKFSEIPRYG YIPNRRNKIF FQNEDIKHSF DNILENRCQI CAHARPERSF KDLQNHLRKQ
HTLFYCNLCV DHLTLLPSER KFYNRQDLAT HRRQGDKDDK SYKGHPNCEF CDERYFDKDE
LYRHLRKDHY FCHFCDPEGC SEFYNDYQSL RNHFGEKHYL CQEGDCAGVE VRLTHAFRSK
IDFQAHTTAE HANNLTKAQA KQLRTIDIDY QLPRRETQRR RDRGGVNTGD YEDVRPVQTQ
VFHNNRGSRG RQRYEEPRGY RRGNFSEEDV QKAIHASLDV MKEKEKVEEQ PEKEEEEEVK
VLRNAKNFPV LGNNDLRVDS PDDSDHKDSD SEALDFSMAQ QIALKNKRSV QVGRLISEEF
PSLSGEPSTK DKTAETLEKK PAIVKTSKPE PIVKSQPVSK SVSKPVSKFT VSKGLVVDDF
PGLPTKSSSI NSALGSAKWV PKQTAKETKQ AAAMPVQVTM NVSANNQKSS KNKTKSSNKA
FQDEKDFPSL GGQPTSTSAS NMNWLQKSAK GKSKPIQERK PIDWFDADND FDFSIENVTK
LSKPILTDDK NSNTSDSKKK KKKKDKSKPS DNDIINDSKP KGGSSLDSIA SSLFSTKGVT
NREPVKVESP KVVRKEESDR SASPENFKIV HKKVKTADIP EDNNKFSILS NETEIKPFVE
SKPRFVPKQN DKNLKLDDFP TLGSSNQSKA PPPGFAKPLP SNSSVPSVKP PGFDNVSSSK
RPPPGFAMPT SSQKNGHSTS EEKSCTFTLK NIMPMMTEMS NFDYVAPENS KVRNQKLIGD
IRLHLGEDIE NFDQFKTVSA SFRQGTTDAT EYYKQCEQLI GKDNFDIIFS ELLVLLPDIN
KQQELLTTYK SIQEKNKSGH VIRISGKSAD APWKQTSNFQ TCPTCRQVLL SSDYTEHTSI
HGSASDFPSL GDGGGGHCLR SWVKGK
//
