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Database: UniProt
Entry: A0A267FTK1_9PLAT
LinkDB: A0A267FTK1_9PLAT
Original site: A0A267FTK1_9PLAT 
ID   A0A267FTK1_9PLAT        Unreviewed;       730 AA.
AC   A0A267FTK1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   02-APR-2025, entry version 28.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=BOX15_Mlig000845g2 {ECO:0000313|EMBL:PAA77150.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA77150.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA77150.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA77150.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA77150.1};
RA   Berezikov E.;
RT   "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT   model organism for stem cell research.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PAA77150.1}.
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DR   EMBL; NIVC01000762; PAA77150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A267FTK1; -.
DR   STRING; 282301.A0A267FTK1; -.
DR   OrthoDB; 9978677at2759; -.
DR   Proteomes; UP000215902; 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   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR026254; RNF31-like.
DR   InterPro; IPR041031; RNF31_C.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR001841; Znf_RING.
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; 2.
DR   SMART; SM00647; IBR; 3.
DR   SMART; SM00184; RING; 3.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215902};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          42..73
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          193..420
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          64..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PAA77150.1"
SQ   SEQUENCE   730 AA;  80758 MW;  2ADE6554B8AC7754 CRC64;
     NPCRLAAPTR MASASENIEW QCQHCTFINS SVCDTSNPKS RIICSVCSKS VSCEELLDLH
     QRQQRAQHLE RAPKPKPRKN QQHRQSFDDE SRASWSLRDA ETDAAAEPLS ISMSQRFSRT
     RMSETSSTLG LRRCIGEERD PGAVEANDIF TRSSKPFYPT HRATEGVLQW DQIRPLRAIS
     IRNSKAAPME TTASKECPVC IDDKKLVEVP LCDCEVCSDC LCQQIEVRLM HDSSVSVLTC
     PVCDKLDDRA LTDTSCEYFP LLQRLLAGQL KPAVMKKLDE RLRDWRLKLT DNFCWCSGCS
     NGFEVSEHHD RQVRCPHCGK ETCRKCGKAW HERHRGVSCQ QFGEWRQQTD LSERGLAQFL
     ESRGSSCPKC GFQFELSRGG CLHLTCRQCK AEFCSDCGSL FVRQECCGGN KGLHCHHGSE
     CVETFRDWPL EKVRQTDLSE RGLAQFLESR GSSCPKCGFQ FELSRGGCLH LTCRQCKAEF
     CSDCGSLFVR QECCGGNKGL HCHHGSECVE TFRDWPLEKV RQAALERGVQ LELVGVAGAV
     GRCSVQEQKE TSGGGLEDGE CGRPVVEAGL CESHLKEALA SAMRGNKKKD RVGAPDFLAG
     PMSSKVGKAQ RPTSAPLVAP SKSLNPGLAQ RPMRLDFFSS NNKPKLNFNR RDLSPTLSEI
     STSVDFACPH CTAVSPTAPS VSNGSRVLCT VCGKTTPSKG GSGADGAFSG SDSMFNSYDV
     DFESCLDIWD
//
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