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Database: UniProt
Entry: N1P670_YEASC
LinkDB: N1P670_YEASC
Original site: N1P670_YEASC 
ID   N1P670_YEASC            Unreviewed;       464 AA.
AC   N1P670;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Itt1p {ECO:0000313|EMBL:EIW08615.1};
GN   ORFNames=CENPK1137D_385 {ECO:0000313|EMBL:EIW08615.1};
OS   Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW08615.1};
RN   [1] {ECO:0000313|EMBL:EIW08615.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW08615.1};
RA   Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA   Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA   Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA   Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT   "De novo sequencing, assembly and analysis of the genome of the laboratory
RT   strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT   biotechnology.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CM001534; EIW08615.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1P670; -.
DR   HOGENOM; CLU_021364_2_2_1; -.
DR   Proteomes; UP000013192; Chromosome XIII.
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; cd20354; Rcat_RBR_RNF14; 1.
DR   CDD; cd23134; RING-HC_ITT1-like; 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; IPR047548; Rcat_RBR_RNF14.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:PRU00175}.
FT   DOMAIN          176..455
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          180..233
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   464 AA;  54052 MW;  F759B515388A0020 CRC64;
     MALTQFENDL EILRDMYPEL EMKSVKVEEE GEFPQRINGK LLFKISLLTD VNIEFGDQHM
     LLSNLSNECV EFTIYSCHYP DIRRCVVMDI KSLWISTDEK KMLIEKALRL VEETVDMSIE
     FADSFTSILI LIFGFLIDDT AILLFPNGIR KCLTQDQYDL FKQIGEEATL QKVSRSNYHC
     CICMEMEKGV RMIKLPCGNA NVEHYLCRGC AKSYFTAMIQ ENRISSVRCP QCEYKELKLE
     DFKSYKKMLK ALFTPLIPVS FLKEVIDTEL CERYEKMFYN QAATRLSKYC PYACVTCRRC
     DSWCTKEDID DAMIQCQKCH FVFCFDCLHA WHGYNNKCGK KVSLSTDIIE EYLDDTVTSY
     ERKRKLEAKY GRRVLELEVN DYLAEKMLDL AIKKEGSNLQ RCPRCKVVVE RSEGCNKMKC
     EVCGTLFCFI CGVLLYPEDP YEHFREAYSG CYGRLFEGMP GTET
//
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