CSN5_CRYNB
ID CSN5_CRYNB Reviewed; 371 AA.
AC P0CQ25; Q55L72; Q5KAB0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE EC=3.4.-.-;
GN Name=RRI1; Synonyms=CSN5; OrderedLocusNames=CNBJ1120;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000049; EAL18470.1; -; Genomic_DNA.
DR RefSeq; XP_773117.1; XM_768024.1.
DR AlphaFoldDB; P0CQ25; -.
DR SMR; P0CQ25; -.
DR MEROPS; M67.A13; -.
DR EnsemblFungi; AAW45929; AAW45929; CNJ02350.
DR EnsemblFungi; EAL18470; EAL18470; CNBJ1120.
DR GeneID; 4938452; -.
DR KEGG; cnb:CNBJ1120; -.
DR VEuPathDB; FungiDB:CNBJ1120; -.
DR HOGENOM; CLU_053034_0_2_1; -.
DR Proteomes; UP000001435; Chromosome 10.
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; 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 Signalosome; Zinc.
FT CHAIN 1..371
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000410222"
FT DOMAIN 51..188
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 278..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..147
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 278..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 371 AA; 41382 MW; C2501D17FCA717C9 CRC64;
MASTARKTFE INNNVQVVDP SAAIFQYSRE EEKLLDDEAP WRTDPHYFHT VKISAVALIK
MVTHARSGGI YEIMGIMYGK VRDGTFWIMD VAALPVQGTE TRVNAGNEAM EYMVNFQTAN
AEAGKGELLR GWYHSHPGYG CWLSGIDVNT QLNNQKFNDP YLAVVIDPNR TVSAGKVEIG
AFRTYPEGYT PPATGNSQYQ SIPMDKIEDF GVHANAYYPL KVEIYKSKLD EKMLDLLWNK
YWVATLSSNS LVSNLEYSTS QVQDLNAKLR AASQSISNSS SKLKLKPTQP TTKGKETTEG
SDKKLKKGEK EFSGVEEEET PLNKVTQESS RITSEAENGI ISQLLKEKLF NTPLTQSVDD
KSAQATVQGR Y
