CSN5_YEAS1
ID CSN5_YEAS1 Reviewed; 440 AA.
AC B3LH96;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE EC=3.4.-.-;
GN Name=RRI1; ORFNames=SCRG_00706;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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=EDV08475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408043; EDV08475.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B3LH96; -.
DR SMR; B3LH96; -.
DR PRIDE; B3LH96; -.
DR EnsemblFungi; EDV08475; EDV08475; SCRG_00706.
DR HOGENOM; CLU_031199_1_0_1; -.
DR Proteomes; UP000008335; 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_0000377627"
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; 50783 MW; DE941EC75589F75E 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 QFDSTDTSLC
INGEPSIHVN RVERSSRSTD NFHNSKKRMN SNQEKCHDEG NDMLQRNVLE TDYARAKNRI
LASKIKQYER LRFYKDTFTL
