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Database: UniProt
Entry: G3NH61_GASAC
LinkDB: G3NH61_GASAC
Original site: G3NH61_GASAC 
ID   G3NH61_GASAC            Unreviewed;       785 AA.
AC   G3NH61;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000004669.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000004669.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000004669.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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};
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DR   AlphaFoldDB; G3NH61; -.
DR   STRING; 69293.ENSGACP00000004669; -.
DR   Ensembl; ENSGACT00000004683.1; ENSGACP00000004669.1; ENSGACG00000003557.1.
DR   eggNOG; KOG1815; Eukaryota.
DR   GeneTree; ENSGT00940000158703; -.
DR   InParanoid; G3NH61; -.
DR   OMA; HQCSISL; -.
DR   TreeFam; TF324777; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000003557; Expressed in testis and 13 other cell types or tissues.
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:InterPro.
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   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:SF111; E3 UBIQUITIN-PROTEIN LIGASE RNF19A; 1.
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   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {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        353..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        406..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..343
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          124..172
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..702
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  83251 MW;  E3D6E7F360932EE5 CRC64;
     GSDRDLQSTA SSISLPSVKK APKKRRLSLA SFFRRRGRES KSARPRSREL QLPGPLGLVG
     VDGIAIIESI HSEMCNDKNS AFFSVAGNGA ASAAAVVSTS SASGPSSSSS SRLGVVAVGE
     LLECPLCLLR HSRESFPDIM TCHHRSCIDC LRQYLRIEIS ESRVNISCPE CSERYNPHDI
     RMILGERALM DKYEEFMLRR WLVADPDCRW CPAPDCGYAV IAFGCASCPK LMCGREGCDT
     EFCYHCKQLW HPNQTCDAAR QQRAQSLRLR TVRSSSLSYS QESSAAADDI KPCPRCAAYI
     IKMNDGSCNH MTCAVCGCEF CWLCMKEISD LHYLSPSGCT FWGKKPWSRK KKILWQLGTL
     VGAPVGIALI AGIAIPAMII GIPVYVGRKI HNRYEGKDIS NHKRNLVIAG GVTLSVIVSP
     VVAAVTVGVG VPIMLAYVYG VVPISLCRSG GCGVSAGNGK GVRIEFDDEN NMNVGSGAAA
     TDTTSVADAR NNPSICEGSV GGLTGSLSAS GSHMDRLGAI RDNLSETAST TALAGASITG
     SLSGSAMVNY LNRLEVQADV QKERCSLSGE SGTVSLGTIS DNASTKAMAG SILNAYMPLD
     RDGNSMEVQV DIESKPGKLR HHSGSSSMDD GAHAARCGWT CPSAGCTSTS EGKGLAAKWA
     KEASCSSSCS SGGKKSIGKL RKKGAAGGTK INETREDMDA QLLEQRSTNS SEFDSPSLSG
     SLPSVADSHS SHFSEFSCSD LESMKTSCSH GSGGGDYHTR FATVSPLPEV ENDRLESCPA
     SSSSS
//
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