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Database: UniProt
Entry: A0A2G5SRG4_9PELO
LinkDB: A0A2G5SRG4_9PELO
Original site: A0A2G5SRG4_9PELO 
ID   A0A2G5SRG4_9PELO        Unreviewed;      1167 AA.
AC   A0A2G5SRG4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   02-APR-2025, entry version 29.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
GN   Name=Cnig_chr_X.g23679 {ECO:0000313|EMBL:PIC17441.1};
GN   ORFNames=B9Z55_023679 {ECO:0000313|EMBL:PIC17441.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC17441.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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:PIC17441.1}.
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DR   EMBL; PDUG01000006; PIC17441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5SRG4; -.
DR   STRING; 1611254.A0A2G5SRG4; -.
DR   OrthoDB; 61092at2759; -.
DR   Proteomes; UP000230233; Chromosome x.
DR   GO; GO:0071797; C:LUBAC complex; IEA:TreeGrafter.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:TreeGrafter.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR   GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR   CDD; cd20335; BRcat_RBR; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR051628; LUBAC_E3_Ligases.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22770:SF13; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          820..1047
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1098..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1167 AA;  135489 MW;  47D43BB59D858F02 CRC64;
     MAGRTRRGEM DVPTHHLNYV VDAPSSSNDW HAVQPNDMNR ADLYPTDQIR ALFHQRQRYR
     RGFPTRTSLH LKFPEQWPCG LQQVHITGRD LKIKKIDKLQ EVRINQTGAI IGRAERNPRR
     IDPEWFDQTV NEVKQRIHSM ESEPWIRSAV FYPLGPKNIL QALGGCFFAR KYCLVVNPNN
     ALAYLVMESF GNSEDDTEAI ENFLKLSSTR LESEMVSTPN AGYSMIYSYG EQPKLVSTLS
     NSTVALVFDL EYLKEKRHNS RATHLTPEKF YQYHFGCPVR FSRRLSDPEK AWLEKKVEMY
     NFRDHPLRML QFYTVEDRNA AVQQSRFEFL DVLFCDSMFN YKDPTEQLHL YVTYSEESKQ
     DEMVQVTLSA ERDKIIAENA FRAHNLRCRY FNDKKVEDRM LRYDRSHKKI ILSGFPKHLT
     TFEGKRWLVE RITSSNNIRL ISIEPFTENV YDAEQKLSRA KNKKLNDCIE KEIYRIGHCH
     NIYRPISWEW IWDLQRALEA GNLLEMVKQR EDVPWKIFRN NRGPMQYLET YTVHFPTVPT
     GLRFVEHILE EASNTSLFSA DESDKNGPMI VPCFRKSITI SRALRYALRQ TIRSFDRYIR
     QFFSALSQNE DVMMESPEAT YYGARLCEEW NEDRETGVLE IQGWNAVSVG FFMRNLLRAM
     DPLELVSIPA CPPDENAQLF FGVGENYVRS LPKKYDGNVV VDIDQFSQKI RLWGLAAEEA
     LEDLRSYSTN KSDIVIEVAI PVHFPHFNDR LRDFLDRKVI DHFRRSLDIK KLEEGNAGSF
     LRFEGTIEAY EKLIEGLTEL SAAVFNREID GNKDLEESQR EYQCTCTVPG FARINDFYRL
     HCGHVFCRTC LSSCINSSIG DAKLLIECPN DACKKFITPK ELMDLVLGDG RRLKDIDSEK
     LSILVNKTKD AIIAADPEIK NCNTADCIGI NTKEKGDIKE LKKCTACRRP YCRRCLCEAH
     GERTCEEALR LQNPDEALKM WIEEAGDRVG HCPVKECNWM MEKGEGCNHM QCPKCSIHFC
     WTCGFTSDES GPIYAHMTSD HEENELEDYV VDDDERDMQE QLVGLFMAGN MDNEAPDGNG
     IGEGEFDGQF AELLQNQALN RRRNPTPPPP PPRRPRRLER LPDVVLDRHP NLTEEDEEVY
     LNFLNAAATR EDQDERIREL AEDIPNR
//
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