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Database: UniProt
Entry: A0A0V0R759_PSEPJ
LinkDB: A0A0V0R759_PSEPJ
Original site: A0A0V0R759_PSEPJ 
ID   A0A0V0R759_PSEPJ        Unreviewed;      1094 AA.
AC   A0A0V0R759;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
GN   ORFNames=PPERSA_03647 {ECO:0000313|EMBL:KRX10340.1};
OS   Pseudocohnilembus persalinus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC   Pseudocohnilembus.
OX   NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX10340.1, ECO:0000313|Proteomes:UP000054937};
RN   [1] {ECO:0000313|EMBL:KRX10340.1, ECO:0000313|Proteomes:UP000054937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36N120E {ECO:0000313|EMBL:KRX10340.1};
RX   PubMed=26486372; DOI=10.1038/srep15470;
RA   Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA   Miao W.;
RT   "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT   persalinus provides insight into its virulence through horizontal gene
RT   transfer.";
RL   Sci. Rep. 5:15470-15470(2015).
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:KRX10340.1}.
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DR   EMBL; LDAU01000030; KRX10340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0R759; -.
DR   EnsemblProtists; KRX10340; KRX10340; PPERSA_03647.
DR   InParanoid; A0A0V0R759; -.
DR   OrthoDB; 180558at2759; -.
DR   Proteomes; UP000054937; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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; cd20335; BRcat_RBR; 1.
DR   CDD; cd20336; Rcat_RBR; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 2.
DR   Pfam; PF00149; Metallophos; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054937};
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          646..849
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1067..1094
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1094 AA;  128886 MW;  3608C0404A3B0CE3 CRC64;
     MRDICICVYN EENGFQFMEQ EYQISTNFLR YFFMPHGKVC KDGEIYHTYF TLGEDSATQT
     YIGIHSGSDI EYLDLQYCKL NELYECVEDL GNINYQIKIK GEKLKQVEHR AERNIFKQKI
     ENLTPNTLYS FKLINPAINQ TLYQTNYQTL SENDSIKLIE GGDSGVTQRA RNLIKQIKNI
     DPHALIIGGD IAYDDGIRGC YYSWDTFLKM WEQELFLPLN KTIPFIFTLG NHDVGYNAVE
     NVVVKEKPLY FDFFTFSDDN QNYHAHKLGN ILLLCLDSGY MAHPSQQKDF IDFYSNKYKN
     QQKFAVYHVP IYPVCLETDT IWHVDLHSME AMEENWVKLF EKNKFIGAFE NHYHLFKRTY
     PIKQRQIDHE NGVIYFGDGS FGLNPPYTCI EENKRDKTFP IFEKFQYSES DHIWVLESHS
     DHLKIDSING YGDDKSTNLQ EQEQEQDQSY SIDLDEKITD INRENPINIQ KPRVNDYDIN
     NNQCTISIQE QNDTIDYEKQ FNIQWAQVCL NRLGYEGDYI DWLDEIYKIE MKKEQLVEIA
     VELIREMEDL QEIPCENLQI RTHLFKNKKI PQKFLHENSI QSISVNNINE QQPQKKLNPS
     QSITSINSNE EIKEQKLSSK KMNFEINQNI DQQINIIDNF NQSQKQIFQC EICLEDNLKS
     SQIFKMVGCQ HYCCKVCSIE YLKQLINTSQ VMSIKCIQDG CKNIIQQQTV QKVVDEQTYT
     KYLKFKNRIK HSNDPNVKFC IQPDCEEVVK LGPNNLCQCI CGMKFCGRCN GIWHPQKTCE
     QTIDQEFKEY AKSNIVQNCP KCKSKIEKKS GCNHITCAMC KYEWCWLCRS KYKRGHFQKN
     NIFGCPGFYS NKKDWPISKI YCYRITNLLK QYRAPRIPGP RITFIQMRQF QEISNLIERG
     IRGDVDYPEF EPQNLNINNN LRFIPDRQSQ SEQINRFHAK FSLRLQQMAI NHLGLQNGNN
     PNQNQFIQNF PQNFQRKNYP TIQFDSPLSS LDKFSEDVEI EMDQDNNLEN IKQNEKQISQ
     SQKDIQQDQN FASDIKNIEI KSNLNKFNEN NGKNSQILQQ KSYGSNKYTQ NYNQNNLNDK
     NRNQQSSQIN KLPI
//
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