ID A0A8C5LXP3_9ANUR Unreviewed; 660 AA.
AC A0A8C5LXP3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RNF19B {ECO:0000313|Ensembl:ENSLLEP00000005900.1};
OS Leptobrachium leishanense (Leishan spiny toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pelobatoidea; Megophryidae; Leptobrachium.
OX NCBI_TaxID=445787 {ECO:0000313|Ensembl:ENSLLEP00000005900.1, ECO:0000313|Proteomes:UP000694569};
RN [1] {ECO:0000313|Ensembl:ENSLLEP00000005900.1}
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}.
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}.
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DR Ensembl; ENSLLET00000006148.1; ENSLLEP00000005900.1; ENSLLEG00000003720.1.
DR GeneTree; ENSGT00940000158451; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000694569; Unplaced.
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; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16776; RING-HC_RBR_RNF19B; 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: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; 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; 1.
DR Pfam; PF22191; IBR_1; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000694569};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..660
FT /note="RBR-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034941540"
FT TRANSMEM 342..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..332
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 114..161
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 32..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..614
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 71512 MW; 200EA06E658CF134 CRC64;
MLRAKTWAAF TGFICFACAV AFTDAEPLPG SAAPESLAMT EGSAEPPPCP GTRRRRFLLS
LPNVFPGRTR AIAEPSVPSP PPSPPPVAAA DPAVPAPVPP PPSPTAGADS LLECPLCLVR
QPPEELPELL SCRHRSCLRC LRQYLRIEIT ESRVNLRCPE CAERLSPQHV RAILRDPLLT
RKYEEFLLRR CLAADPDCRW CPAPDCGYAV IAYGCASCPR LVCEREGCLT EFCYHCKHVW
HPNQTCDMAR QQRASSFGMR RKHPSGISYG QESGLTDDMK SCPRCSAYII KMNDGSCNHM
TCAVCGCEFC WLCMKEISDL HYLSPSGCTF WGKKPWSRKK KIIWQLGTLI GAPVGISLIA
GIAIPAMVIG IPVYVGRKIH GRLENKKTSK HKKNLAVTGG VILSVIASPV VAAVSVVADA
WRALKNPSIG ESSMEGLTSV LSTSGSPTDG LSVLQGNYSE TASFAALSGG SLTGGMLSGG
RAKYCRLEVQ ADVQKETCQK DTVSLSAVSD SASTRAMAGS IISSYNPQER EVNNLEIQVH
IEAKPSRYQL MSESSTEESL HVAVPLVEGE DDEGCRDQVP PCDITLAQPE SIRSDLESSD
AQSDDVPDLA SEEYDSPHLL PPSPPDPQCE SPTPRMCAQQ EGICAREEVL SKVEFIEVRV
//
