ID A0A7L2I5Q6_9PICI Unreviewed; 819 AA.
AC A0A7L2I5Q6;
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:NXR05985.1};
GN ORFNames=SEMFRA_R02279 {ECO:0000313|EMBL:NXR05985.1};
OS Semnornis frantzii.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Coraciimorphae;
OC Piciformes; Ramphastidae; Semnornis.
OX NCBI_TaxID=91796 {ECO:0000313|EMBL:NXR05985.1, ECO:0000313|Proteomes:UP000536381};
RN [1] {ECO:0000313|EMBL:NXR05985.1, ECO:0000313|Proteomes:UP000536381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-42 {ECO:0000313|EMBL:NXR05985.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXR05985.1};
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:NXR05985.1}.
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DR EMBL; VWYK01005583; NXR05985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L2I5Q6; -.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000536381; 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:NXR05985.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000536381};
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 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..706
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 623..633
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..664
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..697
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXR05985.1"
FT NON_TER 819
FT /evidence="ECO:0000313|EMBL:NXR05985.1"
SQ SEQUENCE 819 AA; 87791 MW; C34F6E2015C1409F CRC64;
GLPMKSDPFL VSGLAMSLHR QMGSDRDLQS SASSVSLPSV KKAPKKRRIS LGSLFRKKKD
TKRKSRELNG GVDGIASIES IHSEMCTDKN SIFSTCTSSD NGTVSSSKPS GDFLECPLCL
LRHAKDRFPE IMTCHHRSCV DCLRQYLRIE ISESRVNISC PECSERFNPH DIRLILSDDV
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
ARRNPSIGEG SVGGLTGSLS ASGSHMDRIG AIRDNLSETA STMALAGASI TGSLSGSAMV
NCFNRLEVQA DVQKERYSLS GESGTVSLGT VSDNASTKAM AGSILNSYIP LDREGNSMEV
QVDIESKPAK FRHHSGSSSV EDGSAAGRGS AGSCLPEGKS SATKWSKETT AGKKCKGKLR
KKSSMKINET REDMDAQLLE QQSTNSSEFD SPSLSDSIPS VADSHSSHFS EFSCSDMESM
KTSCSHGSSD YHARFAAVSA LPEVENDRLE NSPQPSGGPV PVPTALSADV PQLSYIAEES
INHASSTDVD LGAGETVKET NNNHSQHAME LSAAVQTEI
//
