ID A0A7L1LRR3_BOMGA Unreviewed; 820 AA.
AC A0A7L1LRR3;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE Flags: Fragment;
GN Name=Rnf19a_0 {ECO:0000313|EMBL:NXN77742.1};
GN ORFNames=BOMGAR_R01773 {ECO:0000313|EMBL:NXN77742.1};
OS Bombycilla garrulus (Bohemian waxwing) (Lanius garrulus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Bombycillidae; Bombycilla.
OX NCBI_TaxID=125297 {ECO:0000313|EMBL:NXN77742.1, ECO:0000313|Proteomes:UP000532545};
RN [1] {ECO:0000313|EMBL:NXN77742.1, ECO:0000313|Proteomes:UP000532545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-23 {ECO:0000313|EMBL:NXN77742.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXN77742.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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:NXN77742.1}.
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DR EMBL; VXBU01001123; NXN77742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L1LRR3; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000532545; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; 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 Ligase {ECO:0000313|EMBL:NXN77742.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000532545};
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 345..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..335
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 116..164
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..41
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..636
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..665
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..698
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXN77742.1"
FT NON_TER 820
FT /evidence="ECO:0000313|EMBL:NXN77742.1"
SQ SEQUENCE 820 AA; 88173 MW; D90D9A8583CDDA29 CRC64;
GLYMKFNTFL MSDLDMSLHR QMGSDRDLQS SASSVSLPSV KKAPKKRRIS LGSLFRRKKD
TKRKSRDLNG GVDGIASIES IHSEMCTDKN SIFSTCTSSD NGTTSSSKPS GDFMECPLCL
LRHSKDRFPE IMTCHHRSCV DCLRQYLRIE ISESRVNISC PECSERFNPH DIRLILNDDI
LMEKYEEFML RRWLVADPDC RWCPAPDCGY AVIAFGCASC PKLTCGREGC GTEFCYHCKQ
IWHPNQTCDA ARQERAQSLR LRTIRSSSIS YSQESGAAAD DIKPCPRCAA YIIKMNDGSC
NHMTCAVCGC EFCWLCMKEI SDLHYLSPSG CTFWGKKPWS RKKKILWQLG TLVGAPVGIA
LIAGIAIPAM IIGIPVYVGR KIHNRYEGKD ISKHKRNLAI AGGVTLSVIV SPVVAAVTVG
IGVPIMLAYV YGVVPISLCR SGGCGVSAGN GKGVRIEFDD ENDINVGGTN AAVDTTSVAE
ARHNPSIGEG SVGGLTGSLS ASGSHMDRIG AIRDNLSETA STMALAGASI TGSLSGSAMV
NCFNRLEVQA DVQKERYSLS GESGTVSLGT VSDNASTKAM AGSILNSYIP LDREGNSLEV
QVDIESKPAK FRHHSGSSSV EEGGAVGRGS AGGSGPPEGK AGATKWAKDS AAGKKCKGKL
RKKSSMKINE TREDMDAQLL EQQSTNSSEF DSPSLSDSIP SVADSHSSHF SEFSCSDMES
MKTSCSHGSS DYHTRFTTVS VLPEVENDRL ENSPQPSGIP VPVPAAPSTD VPQLSYIAEE
SINHGSSADV DLAVGETLKE TNNNHSQQAV ELSTAVQTEM
//
