ID A0A6G0IAS5_LARCR Unreviewed; 867 AA.
AC A0A6G0IAS5;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, 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};
GN ORFNames=D5F01_LYC12272 {ECO:0000313|EMBL:KAE8288403.1};
OS Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Larimichthys.
OX NCBI_TaxID=215358 {ECO:0000313|EMBL:KAE8288403.1, ECO:0000313|Proteomes:UP000424527};
RN [1] {ECO:0000313|EMBL:KAE8288403.1, ECO:0000313|Proteomes:UP000424527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMULYC20181020 {ECO:0000313|EMBL:KAE8288403.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAE8288403.1};
RA Xiao S.;
RT "Chromosome genome assembly for large yellow croaker.";
RL Submitted (JUL-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:KAE8288403.1}.
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DR EMBL; REGW02000012; KAE8288403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G0IAS5; -.
DR Proteomes; UP000424527; 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; 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:UP000424527};
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 395..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..385
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 166..214
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..531
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..725
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 91209 MW; 3B8283A7AA1F0CF8 CRC64;
MSLQKHQQLG GGIGGVMGSD RDLQSTASSI SLPSVKKAPK KRRLSLAALF RRRGREAKSG
RQRSRELQHS GPGGLGGVDG IASIESIHSE MCNDKNSAFY SVAGTGAASA AAAAAAAAAA
TAAAAAAAAA AAAAAASTSS ASGPSSSTSS SSSKVGAGVG TELLECPLCL LRHSRESFPD
IMTCHHRSCI DCLRQYLRIE ISESRVNISC PECSERFNPH DIRMILGDRA LMDKYEEFML
RRWLVADPDC RWCPAPDCGY AVIAFGCASC PKITCGREGC GTEFCYHCKQ LWHPNQTCDA
ARQQRAQSLR LRTVRSSSLS YSQESGAAAD DIKPCPRCAA YIIKMNDGSC NHMTCAVCGC
EFCWLCMKEI SDLHYLSPSG CTFWGKKPWS RKKKILWQLG TLVGAPVGIA LIAGIAIPAM
IIGIPVYVGR KIHNRYEGKD ISNHKRNLVI AGGVTLSVIV SPVVAAVTVG IGVPIMLAYV
YGVVPISLCR SGGCGVSAGN GKGVRIEFDD ENDMNVGSGA AATDTTSVAD TRNNPSIGEG
SVGGMTGSLS ASGSHMDRLG AIRDNLSETA STMALAGASI TGSLSGSAMV NYLNRLEVQA
DVQKERCSLS GESGTVSLGT ISDNASTKAM AGSILNAYMP LDRDGNSMEV QVDIESKPGK
LRHHSGSSSV DDGSHVGRCG WTCPSNGCTS SEGKGTSTKW AKEASCSSSS SSGGKKSKGK
LRKKGGGGTK INETREDMDA QLLEQRSTNS SEFDSPSLSG SLPSVADSHS SHFSEFSCSD
LESMKTSCSH GSSGGDYHTR FATVSPPTRG GERPPGDLPR FLIFLPGTWS CDHTPLPHLH
HLLPGPRCRA LPSLLHHRGE RQPGVPR
//
