ID A0A7N6A6M8_ANATE Unreviewed; 871 AA.
AC A0A7N6A6M8;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RNF19A {ECO:0000313|Ensembl:ENSATEP00000044203.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000044203.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000044203.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSATEP00000044203.1}
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 AlphaFoldDB; A0A7N6A6M8; -.
DR Ensembl; ENSATET00000048116.2; ENSATEP00000044203.1; ENSATEG00000024849.3.
DR GeneTree; ENSGT00940000158703; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000265040; Chromosome 16.
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; cd20362; BRcat_RBR_RNF19A; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16775; RING-HC_RBR_RNF19A; 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 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:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 TRANSMEM 364..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..354
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 135..183
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..508
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 92891 MW; 973D8536AF090D6D CRC64;
MQLSIEHSLG LGLVIVDLTD RSDCCVPASI LTKVVDLLSE VMGSDRDLQS TASSISLPSV
KKAPKKRRLS LASLFRRRGR ESKSGRQRSR ELQHPGPGGL GGVDGIASIE SIHSDMCNDR
NSAFSVAGTG VLLECPLCLL RHSRESFPDI MTCPHRSCID CLRQYLRIEI SESRVNISCP
ECSERFNPHD ICMILGDRAL MEKYEEFMLR RWLVADPDCR WCPAPDCGYA VIAFGCASCP
KITCGREGCG TEFCYHCKQL WHPNQTCDAA RQQRAQSLRL RTVRSSSLSY SQESGAAADD
IKPCPRCAAY IIKMNDGSCN HMTCAVCGCE FCWLCMKEIS DLHYLSPSGC TFWGKKPWSR
KKKILWQLGT LVGAPVGIAL IAGIAIPAMI IGIPVYVGRK IHNRYEGKDI SNHKRNLVIA
GGVTLSVIVS PVVAAVTVGI GVPIMLAYVY GVVPISLCRS GGCGVSAGNG KGVRIEFDDE
NDMNAGGGAA ATDTTSVADN RNNPSIGEGS VGGLTGSLSA SGSHMDRLEA IKDNLSETAS
TMALAGASIT GSLSGSAMVN YLNRLEVQAD VQKERCSLSG ESGTVSLGTM SDNASTKAMA
GSILNSYVPL DRDGNSMEVQ VDIESKPGKL RHHSGSSSVE DGSHVGRCGL ICPSNGCTSS
EGKGTSAKWA KEASCCSSSG SGGKKSKGKL RKKGCGGTKI NETREEMDAQ LLEQRSTNSL
EFDSPSLSGS LPSVADSHSS HFSEFSCSDL ESMKTSCSHG SGGGDYHTRF ATVSPLPEVE
NDRLETCPTS LSSFPQGQGA VITPHSPTST TSSLGRGAEL SPLCFITEEN VNLVCPTELD
SHSNTGELLK EANNNHQTQQ QPKNSCIQTD I
//
