GenomeNet

Database: UniProt
Entry: J9GD52_9SPIT
LinkDB: J9GD52_9SPIT
Original site: J9GD52_9SPIT 
ID   J9GD52_9SPIT            Unreviewed;       550 AA.
AC   J9GD52;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   13-SEP-2023, entry version 39.
DE   SubName: Full=IBR domain containing protein {ECO:0000313|EMBL:EJY88256.1};
GN   ORFNames=OXYTRI_17765 {ECO:0000313|EMBL:EJY88256.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY88256.1};
RN   [1] {ECO:0000313|EMBL:EJY88256.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY88256.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY88256.1}.
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DR   EMBL; AMCR01000492; EJY88256.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9GD52; -.
DR   EnsemblProtists; EJY88256; EJY88256; OXYTRI_17765.
DR   OrthoDB; 180516at2759; -.
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; cd20335; BRcat_RBR; 1.
DR   CDD; cd20336; Rcat_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; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00647; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 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   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        416..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        465..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          200..407
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          204..250
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          524..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  63253 MW;  023D724A064E59B3 CRC64;
     MKNQSDVSIN QNTDDVFFDE LYLRKYQSTV VHKNQQNKKI INGQRLSQNS QGQKSNSVQG
     IDINYVLIVR QLIEMGFPIS QVKRLLCIHK ISDLNEAAQL LTKDENGKYT HYFTPRQSTN
     NNDDQNTQCY ICNEQASEHH QNNPFVFMRR VSYTKIIQES FAGDKKKQSI ISQLQPKVLD
     QSFAPDQHET QEISLQNNEV QIYCNICYDS MGQSEFLDID NCHHKFCKNC VIAYLDQLIS
     TRQITKLICP EYGCGKALQF KLLEKLLSTE QLDKYKEFKQ DLEVMIDSKR GYCPNPACNK
     ITRFNKKKQK DYKCEHCKFE FCGKCQISWA RHVGKKCEDV LAEELGDWFK NSDFQNCPKC
     RVRVEKTSGC NHMTCAQCQN KWCWLCGSNC GYGHYLPFNP FGCPGMLFTP KGRCTILVFM
     IINFLLLPLT MTLTTMFFIG VALFMGQFKL NESFCGISAS RFKRANIAVK LLIILLNIVE
     AGITLPLVVG ISVALVGLVI VPAYIFQFYK IVKIILLWSC KTNDKKGPKS QQTSQIQEQL
     IEKEDQSNQV
//
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