CSN5_CANAL
ID CSN5_CANAL Reviewed; 609 AA.
AC Q59PG6; A0A1D8PLU1; Q59PI9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE EC=3.4.-.-;
GN Name=JAB1; Synonyms=CSN5, RRI1; OrderedLocusNames=CAALFM_C403450CA;
GN ORFNames=CaO19.10880, CaO19.3372;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017626; AOW29103.1; -; Genomic_DNA.
DR RefSeq; XP_711591.2; XM_706499.2.
DR AlphaFoldDB; Q59PG6; -.
DR SMR; Q59PG6; -.
DR STRING; 237561.Q59PG6; -.
DR MEROPS; M67.A01; -.
DR GeneID; 3646811; -.
DR KEGG; cal:CAALFM_C403450CA; -.
DR CGD; CAL0000189891; JAB1.
DR VEuPathDB; FungiDB:C4_03450C_A; -.
DR eggNOG; KOG1554; Eukaryota.
DR HOGENOM; CLU_053034_1_0_1; -.
DR InParanoid; Q59PG6; -.
DR OrthoDB; 1031881at2759; -.
DR Proteomes; UP000000559; Chromosome 4.
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; 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..609
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194848"
FT DOMAIN 75..215
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 210..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..174
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 609 AA; 69519 MW; 245E358C970CE057 CRC64;
MTCLDELAHS LESKSDTTNF KTRNSKIKTI DLYQQNELSG KHPQDQDKFY RLPAIDPIAR
DKKPWKEDIN YFNKCYISSL ALMKMCTHAQ TGGSIEIMGM LVGKISGHSI IVMDTYRLPV
EGTETRVNAQ NEAYTYMVEY LTERQQLSNG KNEENIVGWY HSHPGYGCWL SGIDVSTQSL
NQGFQDPYLA IVVDPVKTLK QGKVEIGAFR TYPEGSQQQP SMTNKTRKDQ NKPHNSGANA
NRKILPKSKQ KDFGSHADKY YSLDIEIFTS SWDDKVIEML KDEDSLTWMK NLLVDSNNND
KILGIRKDEI RSIELIKNYE LISQGNHNAD EGETIFDLIE QLKIQANTPK FMLDKLTTMK
FDSTFESVLY KRLLKKTQKS TTTKKNRKDL STDIDDETML DESDLEKNVG TGGIETSISS
DDDDEEEEGE GEGNSSSRRD NNNNEVEEGP TDEVDSEYAN EELLEEVGAL ENYNFNDLLE
NKSANKFLRS EQKIKHKNRP IHQRMDNSSM ISEWNRLGHQ QQHMPADYPY QWSSNVANLV
KTSKTNRRRE RLHRLQGASI DNKKQFELGL HGSPESKAKS ANLVKLAKSI GLNEVFDLIT
LDAQQKLFG
