ID A0A671K1P2_9TELE Unreviewed; 849 AA.
AC A0A671K1P2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC107698652 {ECO:0000313|Ensembl:ENSSANP00000000368.1};
OS Sinocyclocheilus anshuiensis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=1608454 {ECO:0000313|Ensembl:ENSSANP00000000368.1, ECO:0000313|Proteomes:UP000472260};
RN [1] {ECO:0000313|Ensembl:ENSSANP00000000368.1}
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; A0A671K1P2; -.
DR Ensembl; ENSSANT00000000425.1; ENSSANP00000000368.1; ENSSANG00000000223.1.
DR Proteomes; UP000472260; 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:UP000472260};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..849
FT /note="RBR-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025686650"
FT TRANSMEM 365..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..355
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 136..184
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 30..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..54
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..692
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..729
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 90836 MW; A4E7C1D9EDD53771 CRC64;
LSSTVRCVLC LTQPCLCFFT DQVEIQPGDS KLTRQQGSER DLPSAASSVS LPSVRKTPKK
RRISLRSLFR RRCGDPKSRK SRALTAGGDG IASVESMQSE MCQQQDHASA LSAPGVASTS
SSSSSSSAST SELLECPLCL LRHTRDRFPD IMTCHHRSCA DCLRQYLRIE ISESRVNISC
PECSERFNPH DIRMILNDRV LMEKYEEFML RRWLVADPDC RWCPAPDCGY AVIAFGCASC
PKITCGREGC GTEFCYHCKQ LWHPNQTCDA ARQQRAQSLR LRPFRSSSLS YSQESGAAAD
DIKPCPRCAA YIIKMNDGSC NHMTCAVCGC EFCWLCMKEI SDLHYLSPSG CTFWGKKPWS
RKKKILWQLG TLVGAPVGIA LIAGIAVPAM IIGIPVYVGR KIHNRYEGKD ISKHKRNLVI
AGGVTLSVIV SPVVAAVTVG IGVPIMLAYV YGVVPISLCR SGGCGVSAGN GKGVRIEFDD
ENDMNVGTGA AVTDTTSVAE TRHNPSIGEG SVGGLTGSLS ASGSHMERIG AMRDNLSENA
STMALAGASI TGSLSGSAMV NCFNRLEVQA DVQKERCSLS GESGTVSLGT ISDNASTKAM
AGSILNAYLP LDRDGNSMEV QVDVESKRGK LRHHSGSSSM DDGSSGGHGA DVCPSGCPHE
GKCVTSRWAK EPSSTSSSSG KKSKGKLRKK SGGTKINETC EDMDAQLLER RSTNSSELDS
PSLSGSLPSV ADSHSSHFSE FSCSDLDACR PPCYESHVRH PNTGGAVSPL PEVENDRLEN
CPTSGTLPQA AAAPLTPDGP AERPLCYIAE ENVSLICGAD AGQSSPKERN NNLPQPTSPV
RNACIQTEI
//
