ID A0A7L1YCZ2_9PASS Unreviewed; 821 AA.
AC A0A7L1YCZ2;
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:NXP19730.1};
GN ORFNames=SCYSUP_R08503 {ECO:0000313|EMBL:NXP19730.1};
OS Scytalopus superciliaris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Rhinocryptidae; Scytalopus.
OX NCBI_TaxID=312124 {ECO:0000313|EMBL:NXP19730.1, ECO:0000313|Proteomes:UP000580825};
RN [1] {ECO:0000313|EMBL:NXP19730.1, ECO:0000313|Proteomes:UP000580825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-46 {ECO:0000313|EMBL:NXP19730.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXP19730.1};
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:NXP19730.1}.
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DR EMBL; VXBX01002685; NXP19730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L1YCZ2; -.
DR Proteomes; UP000580825; 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:NXP19730.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000580825};
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 609..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..636
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..666
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..699
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXP19730.1"
FT NON_TER 821
FT /evidence="ECO:0000313|EMBL:NXP19730.1"
SQ SEQUENCE 821 AA; 88421 MW; 13B577D774FE25A1 CRC64;
GLYMKFNPFL MSDLDMSLHR QMGSDRDLQS SASSVSLPSV KKAPKKRRIS LGSFFRRKKD
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 LDREGTSLEV
QVDIESKPAK FRHHSGSSSV EDGSAAGRGS AGCSAGPQEG KAGASKWSKD STAGKKCKGK
LRKKSSMKIN ETREDMDAQL LEQQSTNSSE FDSPSLSDSI PSVADSHSSH FSEFSCSDME
SMKTSCSHGS SDYHTRFTTV SVLPEVENDR LENSPQPSGI PVPVPIAPST DVPQLSYIAE
ESIHNGSSTD VDLGVGETLK ETNNNHSQHA VELSTAIQTE I
//
