CSN5_KLULA
ID CSN5_KLULA Reviewed; 373 AA.
AC Q6CRJ8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE EC=3.4.-.-;
GN Name=RRI1; Synonyms=CSN5; OrderedLocusNames=KLLA0D08503g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 CNS complex is involved in the
CC regulation of the mating pheromone response. {ECO:0000250}.
CC -!- SUBUNIT: Component of the COP9 signalosome (CSN) complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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}.
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DR EMBL; CR382124; CAH00537.1; -; Genomic_DNA.
DR RefSeq; XP_453441.1; XM_453441.1.
DR AlphaFoldDB; Q6CRJ8; -.
DR SMR; Q6CRJ8; -.
DR STRING; 28985.XP_453441.1; -.
DR MEROPS; M67.A01; -.
DR EnsemblFungi; CAH00537; CAH00537; KLLA0_D08503g.
DR GeneID; 2892990; -.
DR KEGG; kla:KLLA0_D08503g; -.
DR eggNOG; KOG1554; Eukaryota.
DR HOGENOM; CLU_031199_1_0_1; -.
DR InParanoid; Q6CRJ8; -.
DR Proteomes; UP000000598; Chromosome D.
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:EnsemblFungi.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0070452; P:positive regulation of ergosterol biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0000338; P:protein deneddylation; IEA:EnsemblFungi.
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 Reference proteome; Signalosome; Zinc.
FT CHAIN 1..373
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194854"
FT DOMAIN 66..201
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 289..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 147..160
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 291..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 373 AA; 42457 MW; B08003C30F10A34E CRC64;
MSSIKFHEKS LKEVTRWIQA NEDINTETSL SSSSDSSTTI PVIDHLPARI PYATDLKRNP
CHFQKCLISR LATTKMLSHA VDGGDIEVMG MLVGYTSNDM IVVKDCYSLP VQGTETRVNA
HMESYEYMVQ YLDAFVTKED KIVGWYHSHP GYGCWLSNID IQTQSLNQNY QDPYLAIVVD
PKKSLSGNTL DIGAFRTLPS KDNNEHVDYY PLNIQLYQNS LDVNISKLKL KFKVDPAIQN
NPNEPELMKE LHECVENWFH AKKVMKSTVG FNAIGSTVVN ETEIGNEDFT HERSNSISST
SSLTTRHTTD VEMDDQESAQ SSLDIPANVI PGMQFQEAEI KHEYELKKKK LLLLKVKQYQ
KLRTYRQLFN ASE
