ID   CSN5_YARLI              Reviewed;         354 AA.
AC   Q6C703;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=COP9 signalosome complex subunit 5;
DE            EC=3.4.-.-;
GN   Name=RRI1; Synonyms=CSN5; OrderedLocusNames=YALI0E04829g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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. {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; CR382131; CAG79140.1; -; Genomic_DNA.
DR   RefSeq; XP_503559.1; XM_503559.1.
DR   AlphaFoldDB; Q6C703; -.
DR   SMR; Q6C703; -.
DR   STRING; 4952.CAG79140; -.
DR   MEROPS; M67.A13; -.
DR   EnsemblFungi; CAG79140; CAG79140; YALI0_E04829g.
DR   GeneID; 2912215; -.
DR   KEGG; yli:YALI0E04829g; -.
DR   VEuPathDB; FungiDB:YALI0_E04829g; -.
DR   HOGENOM; CLU_053034_0_2_1; -.
DR   InParanoid; Q6C703; -.
DR   OMA; ALWNKYW; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019784; F:deNEDDylase activity; IBA:GO_Central.
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:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR   GO; GO:0000338; P:protein deneddylation; IBA:GO_Central.
DR   InterPro; IPR037740; CSN5.
DR   InterPro; IPR040961; CSN5_C.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   PANTHER; PTHR10410:SF6; PTHR10410:SF6; 1.
DR   Pfam; PF18323; CSN5_C; 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..354
FT                   /note="COP9 signalosome complex subunit 5"
FT                   /id="PRO_0000194858"
FT   DOMAIN          56..193
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          193..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           139..152
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   354 AA;  39933 MW;  88D2A901F9852427 CRC64;
     MASLATFQVE NDIVDVDSTP QQGFDRDDLY KYDDVEQKAI LAAHPWRTDP SYFRNVLVSS
     IALVKMAMHA RSGGAIEVMG MMTGKILPNT FVVMDCYPLP VEGTETRVNA QQEGIEFMVE
     YLQGLKDVGR RENIVGWYHS HPGYGCWLSG IDVDTQFQNQ QFQEPFLAVV VDPNRTISAG
     KVEIGAFRTY PKDYKPPKKA TKQNQDQSVP LSKAKDYGAH SERYYELDVS FFKSSLDENL
     LQLLWNKNWA ATLSQSTIQL NHDYTSKLML DLSEKNAQLA IGLGEKTPQS QGRGFREAMS
     KADNEPHTNL LNYSTKGQWE AVNRSVKDGV QIGSDELQGL MSLEIQRRLF GRAK