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Database: UniProt
Entry: A0A2G8LQX5_STIJA
LinkDB: A0A2G8LQX5_STIJA
Original site: A0A2G8LQX5_STIJA 
ID   A0A2G8LQX5_STIJA        Unreviewed;       722 AA.
AC   A0A2G8LQX5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   02-APR-2025, entry version 28.
DE   SubName: Full=Putative E3 ubiquitin-protein ligase RNF31 isoform 3 {ECO:0000313|EMBL:PIK62635.1};
GN   ORFNames=BSL78_00427 {ECO:0000313|EMBL:PIK62635.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK62635.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK62635.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK62635.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK62635.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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:PIK62635.1}.
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DR   EMBL; MRZV01000008; PIK62635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8LQX5; -.
DR   STRING; 307972.A0A2G8LQX5; -.
DR   OrthoDB; 9978677at2759; -.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
DR   GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR   GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR   GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR   GO; GO:1990450; F:linear polyubiquitin binding; IEA:TreeGrafter.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR   CDD; cd20337; BRcat_RBR_HOIP; 1.
DR   CDD; cd20351; Rcat_RBR_HOIP; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   InterPro; IPR047540; BRcat_RBR_RNF31-like.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047542; Rcat_RBR_RNF31-like.
DR   InterPro; IPR026254; RNF31-like.
DR   InterPro; IPR041031; RNF31_C.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE LUBEL; 1.
DR   PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR   Pfam; PF18091; E3_UbLigase_RBR; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230750};
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          341..578
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   722 AA;  82970 MW;  E018235B6C2360B0 CRC64;
     MDLFRRAAHQ EQNPVRGDHR APPRQIPGVK PRPAEQNAPQ VQHGPPVVVK RWRCEHCTYL
     NEASDGNICT MCSRTTTSPQ MEEHVTEYPV TIIRAEEVMT QSGPPHGLER PLPRTMNALE
     KRPEHEQPRY ETKEEENARR TREEEQRKRD EEEVESQQKQ ENLTLRLLIM YRNQGNFNAN
     KEERYSLEEV ATAWAVLERE GIMNMQPVEW LDKHLKKQLE LFGGDVLREF CRRYNLNPKD
     YHQWIPNEYV HPAWLKNDGV REKTAAECLA LLQEKVKDIC AENPDVDYEE HAAKLLLEGG
     FDSENLSWGL QLSAAEEKQD EIDGWLGKMW DVAYSVEGAI EKIENSMLNE ADKKELIGIP
     SCQCHICTEC FTQNFTLLAQ NTPCVYKFAC PSCNEPKLEE ISEDEFHRYF TYLGMVLKQH
     LNPADFELYQ QKLVTWGLIK DENFRWCANG CSNGFINERD DVKIQCTNCK KFQCFDCQKP
     WQEQHEGISC EEFEQWKKDN DPEFQAQGLA AHLKENGINC PNCKMRYELA KGGCMHFKCA
     QCMHEFCCGC NLPFLKYPNC RKFPSCQGKG LHAHHPRDCL YHLRDQECET LQKLLQDNGV
     EYNRANAAAN LPEEDGCPVK EQREDPDGLV DVNCGKELIA AAGLCLTHYK EYLVSLINQS
     KIDPADILTA GELGAALKRD GQNVPVIQAG EANEAYQERL RQLLKAQIPL HEGGEAVAAN
     RL
//
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