ID   CSN5_YEAS7              Reviewed;         440 AA.
AC   A6ZXB7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=COP9 signalosome complex subunit 5;
DE            EC=3.4.-.-;
GN   Name=RRI1; ORFNames=SCY_0705;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Catalytic component of the COP9 signalosome (CSN) complex
CC       that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by
CC       mediating the deneddylation of the cullin subunit of SCF-type E3
CC       ubiquitin-protein ligase complexes. The CSN complex is involved in the
CC       regulation of the mating pheromone response. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Component of a COP9 signalosome-like (CSN) complex, composed
CC       of at least RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1.
CC       Within this complex it probably interacts directly with CSN12. Also
CC       interacts with RPN5 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Nuclear localization requires the formation of the CSN complex.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The JAMM motif is essential for the protease activity of the
CC       CSN complex resulting in deneddylation of cullins. It constitutes the
CC       catalytic center of the complex (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN60147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFW02000145; EDN60147.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZXB7; -.
DR   SMR; A6ZXB7; -.
DR   EnsemblFungi; EDN60147; EDN60147; SCY_0705.
DR   HOGENOM; CLU_031199_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0008180; C:COP9 signalosome; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR037740; CSN5.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   PANTHER; PTHR10410:SF6; PTHR10410:SF6; 1.
DR   Pfam; PF01398; JAB; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease;
KW   Signalosome; Zinc.
FT   CHAIN           1..440
FT                   /note="COP9 signalosome complex subunit 5"
FT                   /id="PRO_0000377628"
FT   DOMAIN          71..218
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          319..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           164..177
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   COMPBIAS        319..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   440 AA;  50784 MW;  DE814AD214DDE20A CRC64;
     MSLSNKTVKE LRQLLKERYT VEDELTESIA LSSMRFKPSQ EPEFHALSQS SLLKTKLKQQ
     SSTDIPSYTH VLISKLSCEK ITHYAVRGGN IEIMGILMGF TLKDNIVVMD CFNLPVVGTE
     TRVNAQLESY EYMVQYIDEM YNHNDGGDGR DYKGAKLNVV GWFHSHPGYD CWLSNIDIQT
     QDLNQRFQDP YVAIVVDPLK SLEDKILRMG AFRTIESKSD DNSATSYYEL ETIIFDSELN
     RALFETKLNL HCVIEDDESE QISLNRLIDS MKQYSYLMDS KNVRTRIKLA TTSERVSNEN
     KKNIDYQNRS TRSQFCLNTQ RGDSTETSSF GSMFSGDNTS DVDMEDRNLT EFDSTDTSLC
     INGEPSIHVN RVERSSRSTD NFHNSKKRMN SNQEKCHDEG NDMLQRNVLE TDYARAKNRI
     LASKIKQYER LRFYKDTFTL