ID A0A8C5RG45_LATLA Unreviewed; 532 AA.
AC A0A8C5RG45;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS Laticauda laticaudata (Blue-ringed sea krait) (Blue-lipped sea krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX NCBI_TaxID=8630 {ECO:0000313|Ensembl:ENSLLTP00000002223.1, ECO:0000313|Proteomes:UP000694406};
RN [1] {ECO:0000313|Ensembl:ENSLLTP00000002223.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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}.
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DR Ensembl; ENSLLTT00000002316.1; ENSLLTP00000002223.1; ENSLLTG00000001725.1.
DR GeneTree; ENSGT00940000165084; -.
DR Proteomes; UP000694406; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd20338; BRcat_RBR_RNF19; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR FunFam; 1.20.120.1750:FF:000017; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000424; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR051628; LUBAC_E3_Ligases.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000694406};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {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 297..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..287
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 67..114
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 58192 MW; 7F635E5CF35B5B1A CRC64;
MKRPRVGPAS LGVLSLFGRK PQAMSEPLGE PERPPLDRAE ETRVALMLPE EEEEEEEEKE
QEDLVECPLC LLAQPAAAFP ALSSCAHLSC LACLQQYLRI EISESRVQLA CPHCPALLQP
AEIHQLLPEA GLRDKYEEYL LRRLLVADPG TRWCPAPDCS YAVIAYGCAE CPRLVCGRQD
CKTEFCYHCR QPWHPNSSCE QAWREWKQQS PLGVVELSTQ LIWKEEAAHN PDTIKVCPRC
GAFIMKINDG SCNRMNCTVC GCLFCWLCMQ EITDVHFLSP SGCTFWGKKP WSRTRKLLWQ
LGMVLGAPMV ISIVAGIAVP VITLGIPIYT GKKVLNHGRK SKLSGCQQCL SVASSIFLSL
FVSPVITAVT VGVGVPLMLT YVYGVVVLSL CRNRWGCGSS RKEAGELSTV ELENLAKLNE
LLAVLPTPMV PEKGASASIP HSSNSQHEEP CQKDWKSESA STVALAGSML SEAQETSHRD
GLNMVEVEVE IETQPQAAGE HSLCSAASGH SFSADSLAYT SDGCSLAGVM TE
//
