ID A0A8C6QJ89_NANGA Unreviewed; 831 AA.
AC A0A8C6QJ89;
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};
GN Name=Rnf19a {ECO:0000313|Ensembl:ENSNGAP00000004861.1};
OS Nannospalax galili (Northern Israeli blind subterranean mole rat) (Spalax
OS galili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Spalacidae; Spalacinae; Nannospalax.
OX NCBI_TaxID=1026970 {ECO:0000313|Ensembl:ENSNGAP00000004861.1, ECO:0000313|Proteomes:UP000694381};
RN [1] {ECO:0000313|Ensembl:ENSNGAP00000004861.1}
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}.
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 Ensembl; ENSNGAT00000008149.1; ENSNGAP00000004861.1; ENSNGAG00000006667.1.
DR GeneTree; ENSGT00940000158703; -.
DR OMA; HQCSISL; -.
DR Proteomes; UP000694381; 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; 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 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:UP000694381};
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 354..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..344
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 125..173
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 615..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..676
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 89845 MW; 4E5D35429B9AE529 CRC64;
YIFRYNEGLC MNTDPDSILM SILDMSLHRQ MGSDRDLQSS ASSVSLPSVK KAPKKRRISI
GSLFRRKKDN KRKSRELNGG VDGIASIESI HSEMCTDKNS IFSTNTSSDN GLASISKQIG
DSIECPLCLL RHSKDRFPDI MTCHHRSCVD CLRQYLRIEI SESRVNISCP ECTERFNPHD
IRLILSDDIL MEKYEEFMLR RWLVADPDCR WCPAPDCGYA VIAFGCASCP KLTCGREGCG
TEFCYHCKQI WHPNQTCDAA RQERAQSLRL RTIRSSSISY SQESGAAADD IKPCPRCAAY
IIKMNDGSCN HMTCAVCGCE FCWLCMKEIS DLHYLSPSGC TFWGKKPWSR KKKILWQLGT
LVGAPVGIAL IAGIAIPAMI IGIPVYVGRK IHNRYEGKDV SKHKRNLAIA GGVTLSVIVS
PVVAAVTVGI GVPIMLAYVY GVVPISLCRS GGCGVSAGNG KGVRIEFDDE NDINVGGTNT
AIDTTSVAEA RHNPSIGEGS VGGLTGSLSA SGSHMDRIGA IRDNLSETAS TMALAGASIT
GSLSGSAMVN CFNRLEVQAD VQKERYSLSG ESGTVSLGTV SDNASTKAMA GSILNSYMPL
DKEGNSMEVQ VDIESKPSKF RHNSGSSSVD DGSATRSHAG GSASGLPEGK SSATKWSREA
TAGKKSKGGK LRKKGNMKIN ETREDMDAQL LEQQSTNSSE FEAPSLSDSM PSVADSHSSH
FSEFSCSDLE SMKTSCSHGS SDYHARFATV NILPEVENDR LENSPHQCSI SLLSKTASCS
EVPQPSHSAE DHGNSGVKPS VDLYFGDGLK ETNNNHSHQM MDLKVAIQTE I
//
