ID A0A8B6G242_MYTGA Unreviewed; 780 AA.
AC A0A8B6G242;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=MGAL_10B034998 {ECO:0000313|EMBL:VDI57610.1};
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:VDI57610.1, ECO:0000313|Proteomes:UP000596742};
RN [1] {ECO:0000313|EMBL:VDI57610.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
CC {ECO:0000256|ARBA:ARBA00061087}.
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:VDI57610.1}.
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DR EMBL; UYJE01007762; VDI57610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8B6G242; -.
DR Proteomes; UP000596742; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20338; BRcat_RBR_RNF19; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000052; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:VDI57610.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000596742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:VDI57610.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
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:PRU00175}.
FT TRANSMEM 334..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..324
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 110..158
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..13
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 85195 MW; 354BCB7BC76AAB6F CRC64;
MYVQMLRSQQ SNIPGVMRKR DSEVTSVSSG NSRGSERRKN RFSLRRLFYV TQGTTANRRT
RSHVSLDSDS GRSDASVLAP PDREILPRQS SSVDTHSLSH KKGSSISREC PLCLNTHPSE
EFPDIMTCHH RSCITCLQTY LQIEITESRI NISCPECTEK YHPNDIQMIL QNDILVKKYE
DFMVRRVLVT DPDARWCPAP DCGYAVIAKE CAGCPRIRCE RPGCDTDFCY HCKQYWHPNK
TCDAARAERA SSNLRSPSVS YSHDNDSQND IKPCPRCGAF IMKMNDGSCN HMACPVCGAE
FCWLCMKEIS DLHYLSPSGC TFWGKKPWSR KKKILWQLGT LVGAPVGITL IAGIAVPAMI
IGIPVWVGRK IHSKYKLSPK HRRNLAITGG VATSILFSPV VAGLAVGIGV PILLAYVYGV
VPISLCRSGG CGVTATNKGG VRFEFDEENE TVGPAGPDTQ SVGTGHNVAN PSIAPSIGDA
SLGMTNSLSA SGSHMDRVGI IRDEISDRDS ASNRAIGGYS LNGSLCGGNY YTQKLEIQAD
VSSNMPDIRD KDTSSVVTAT SAYEVQVDMP SRGRHSSVES STLVSAKQRN VSGQSSPISG
CSAYLSGPES QNTKCKKCKR HNNSNSDKSC EQSSVHFADQ VSLCDDVTTH SISEESDKFL
GYLTSESAHG KCFTSRCSEL KSGIPPCQSR FQDSNASSLP EVEVDRPSLK ESENARKAVS
TSALPLSQFK LSHKSLCKSK SQEDCALSDK SKVGRVRHRS CELAMETGRI SPTEENDNQL
//
