ID A0A6G1PMP2_9TELE Unreviewed; 931 AA.
AC A0A6G1PMP2;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=EXN66_Car007207 {ECO:0000313|EMBL:KAF3691532.1};
OS Channa argus (northern snakehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Channoidei; Channidae; Channa.
OX NCBI_TaxID=215402 {ECO:0000313|EMBL:KAF3691532.1, ECO:0000313|Proteomes:UP000503349};
RN [1] {ECO:0000313|EMBL:KAF3691532.1, ECO:0000313|Proteomes:UP000503349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OARG1902GOOAL {ECO:0000313|EMBL:KAF3691532.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF3691532.1};
RA Zhou C., Xiao S.;
RT "Opniocepnalus argus genome.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000503349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhou C., Xiao S.;
RT "Opniocepnalus argus Var Kimnra genome.";
RL Submitted (FEB-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}.
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DR EMBL; CM015718; KAF3691532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G1PMP2; -.
DR Proteomes; UP000503349; Chromosome 7.
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; cd20363; BRcat-RBR_RNF19B; 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; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
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:UP000503349};
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 418..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..408
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 189..237
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..83
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..177
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..748
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..922
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 99627 MW; 311F9EBD74594B04 CRC64;
MDTSKMDIEG EENEEPHPIP LLDFPVHVRD RLPNPGSPLA HPSPPSGEMS LQTHLRIEGS
SGEVMGSDRD LQSTSSSISL PSVKKPPKKR RLSLASLFRR RGREPKTGRQ RSRELQHPVS
GGMGGVDCIA SIESIHSEMC NDKNSAFFSV AGTGVASATA ASTSSASGPS SSTSSSKRGG
GAGAELLECP LCLLCHSRES FPDIMTCHHR SCIDCLRQYL RIEISESRVN ISCPECSERF
NPHDIRMILC DRALMEKYEE FMLRRWLVAD PDCRWCPAPD CGYAVIAFGC ASCPKITCGR
EGCDTEFCYH CKQLWHPNQT CDAARQQRAQ SLHLRTVRSS SLSYSQESGY TADDIKPCPR
CAAYIIKMND GSCNHMTCAV CGCEFCWLCM KEISDLHYLS PSGCTFWGKK PWSRKKKILW
QLGTLVGAPV GIALIAGIAI PAMIIGIPVY VGRKIHNRYE GKDISNHKRN LVIAGGVTLS
VIVSPVVAAV TVGIGVPIML AYVYGVVPIS LCRSGGCGVS AGNGKGVRIE FDDENDINVG
SGATATDTTS VADNRNNPSI GEGSVGGLTG SLSASGSHMD RLGTIRDNLS ETASTMALAG
ASITGSLSGS AMVNYLNRLE VQADVQKERC SLSGESGTVS LGTISDNAST KAMAGSIFNS
YMPLDRDGNS MEVQVDIESK PGKLRHHSGS SSVDDGSHVG RSGWICPSNG FTSSEGKGSS
TKWAKEASCC SSSSSTGKKS KGKLRKKGCG GTKINETRED MDAQLLEQRS TNSSEFDSPS
LSGSLPSVAD SHSSHFSEFS CSDLESMKTS CSHGSSGGDY HTRFTTVSPL PEVENDRLET
CPASSTCLTH GQGAVTTPHS PTSTNSSLGY GAELSPLCFI TEENVNLVCP TEPDSQSNTG
ELQKETNNNH QLQHPAQPQQ QPKNFCIQTD I
//
