CSN5_DEBHA
ID CSN5_DEBHA Reviewed; 469 AA.
AC Q6BMQ3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE EC=3.4.-.-;
GN Name=RRI1; Synonyms=CSN5; OrderedLocusNames=DEHA2F03498g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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 CSN 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; CR382138; CAG88831.2; -; Genomic_DNA.
DR RefSeq; XP_460518.2; XM_460518.1.
DR AlphaFoldDB; Q6BMQ3; -.
DR SMR; Q6BMQ3; -.
DR STRING; 4959.XP_460518.2; -.
DR MEROPS; M67.A01; -.
DR EnsemblFungi; CAG88831; CAG88831; DEHA2F03498g.
DR GeneID; 2903422; -.
DR KEGG; dha:DEHA2F03498g; -.
DR VEuPathDB; FungiDB:DEHA2F03498g; -.
DR eggNOG; KOG1554; Eukaryota.
DR HOGENOM; CLU_031199_0_0_1; -.
DR InParanoid; Q6BMQ3; -.
DR OMA; RCIHELA; -.
DR OrthoDB; 1031881at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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 Reference proteome; Signalosome; Zinc.
FT CHAIN 1..469
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194851"
FT DOMAIN 63..200
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..159
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 203..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 469 AA; 53126 MW; E8E398D0920C5C87 CRC64;
MRCIHELADV FINDSDERIL TQSLDATEID KHADYESFFS INSDESIMKA RPWKSNAKYF
KKTYISSLAL CKMSVHAKSG GAIEVMGMMT GKIIKNSIIV MDVYPLPVEG TETRVNAQAE
GYEYMVQYLE NSKQVGRDEN IVGWYHSHPG YGCWLSGIDV ATQSLNQNFQ DPYLAIVIDP
MKTEDQGKVE IGAFRTFPDN YKSPDSAAPT NNTRGVPPSK QKDFGVHSDK YYSLDIQIFK
SNLDTEILNI ISNKSWIGKL IKSVNTANHQ EQNMIENVFK LINKLQKKEV NQLNRFEISF
IKKFDLIFED IISKKLMNDN RFYSTISQSS YDSFSGHGNS SSNDEMDDES DLDDRDKSSA
PLDISDTGND DVMSMESSVN VYTDKRGDDN DDDDDNDGYD KRPMYTNYRS RANLTKPRKS
GSSPEEHVKL SNNVNKTITN ISNHSKDIGL TELQDLIALK TKESIFLGK
