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CSN5_ASPFU
ID   CSN5_ASPFU              Reviewed;         334 AA.
AC   Q4WZP2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=COP9 signalosome complex subunit 5;
DE            EC=3.4.-.-;
GN   Name=csn5; ORFNames=AFUA_2G16250;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000001; EAL93923.2; -; Genomic_DNA.
DR   RefSeq; XP_755961.2; XM_750868.2.
DR   AlphaFoldDB; Q4WZP2; -.
DR   SMR; Q4WZP2; -.
DR   STRING; 746128.CADAFUBP00003130; -.
DR   EnsemblFungi; EAL93923; EAL93923; AFUA_2G16250.
DR   GeneID; 3512817; -.
DR   KEGG; afm:AFUA_2G16250; -.
DR   VEuPathDB; FungiDB:Afu2g16250; -.
DR   eggNOG; KOG1554; Eukaryota.
DR   HOGENOM; CLU_053034_0_2_1; -.
DR   InParanoid; Q4WZP2; -.
DR   OMA; ALWNKYW; -.
DR   OrthoDB; 1031881at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
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..334
FT                   /note="COP9 signalosome complex subunit 5"
FT                   /id="PRO_0000194847"
FT   DOMAIN          51..187
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          273..294
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   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   334 AA;  37356 MW;  EE9B42676313AEFB CRC64;
     MQAAQQSWEL ENTISLIDPQ RDALYRYDEE THKALSAARP WAKDPHYFKS IRISAVALIK
     MTMHARSGGS LEVMGLMQGY ILPETFVVTD AFRLPVEGTE TRVNAQEEAN EYMVSYLQSC
     RDAGRMENAV GWYHSHPGYG CWLSGIDVTT QDMQQLGGPF VAVVIDPERT ISAGKVDIGA
     FRTFPKDYTP PKEGNEDEDY QTIPLSKAED FGAYAHQYYS LEVSFFKSSL DTELLSQLWN
     KYWVATLSQS PLFTTRDYGS RQMMDLSQKV RRAARGIESS GSRGGATTPK DQQLEKIVRD
     GQRIVSEEVK GLLAAEVKMK LFQGIGEGTQ TGAS
 
 
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