CSN5_EMENI
ID CSN5_EMENI Reviewed; 335 AA.
AC Q5BBF1; C8VM14; Q4L2Q0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=COP9 signalosome complex subunit 5;
DE EC=3.4.-.-;
GN Name=rri1; Synonyms=csn5, csnE; ORFNames=AN2129;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IDENTIFICATION IN THE CSN
RP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF HIS-134;
RP HIS-136 AND ASP-147.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=17470786; DOI=10.1073/pnas.0702108104;
RA Busch S., Schwier E.U., Nahlik K., Bayram O., Helmstaedt K., Draht O.W.,
RA Krappmann S., Valerius O., Lipscomb W.N., Braus G.H.;
RT "An eight-subunit COP9 signalosome with an intact JAMM motif is required
RT for fungal fruit body formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8089-8094(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 (By similarity). The CSN complex
CC seems to link protein degradation to sexual development. Required for
CC fruit body formation. {ECO:0000250, ECO:0000269|PubMed:17470786}.
CC -!- SUBUNIT: Component of the COP9 signalosome (CSN) complex.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q5BBF1; Q5BB47: csnF; NbExp=3; IntAct=EBI-15634720, EBI-15634741;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA64961.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY126455; AAM95164.1; -; Genomic_DNA.
DR EMBL; AACD01000032; EAA64961.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF86237.1; -; Genomic_DNA.
DR RefSeq; XP_659733.1; XM_654641.1.
DR AlphaFoldDB; Q5BBF1; -.
DR SMR; Q5BBF1; -.
DR DIP; DIP-60929N; -.
DR IntAct; Q5BBF1; 7.
DR STRING; 162425.CADANIAP00008806; -.
DR MEROPS; M67.A02; -.
DR EnsemblFungi; CBF86237; CBF86237; ANIA_02129.
DR EnsemblFungi; EAA64961; EAA64961; AN2129.2.
DR GeneID; 2875469; -.
DR KEGG; ani:AN2129.2; -.
DR VEuPathDB; FungiDB:AN2129; -.
DR eggNOG; KOG1554; Eukaryota.
DR HOGENOM; CLU_053034_0_2_1; -.
DR InParanoid; Q5BBF1; -.
DR OMA; ALWNKYW; -.
DR OrthoDB; 1031881at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0008180; C:COP9 signalosome; IDA:AspGD.
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; TAS:AspGD.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0070791; P:cleistothecium development; IMP:AspGD.
DR GO; GO:0030448; P:hyphal growth; IMP:AspGD.
DR GO; GO:0000338; P:protein deneddylation; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IMP:AspGD.
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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease;
KW Reference proteome; Signalosome; Zinc.
FT CHAIN 1..335
FT /note="COP9 signalosome complex subunit 5"
FT /id="PRO_0000194852"
FT DOMAIN 51..187
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
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"
FT MUTAGEN 134
FT /note="H->A: Inhibits fruit body formation; when associated
FT with A-136 and A-147."
FT /evidence="ECO:0000269|PubMed:17470786"
FT MUTAGEN 136
FT /note="H->A: Inhibits fruit body formation; when associated
FT with A-134 and A-147."
FT /evidence="ECO:0000269|PubMed:17470786"
FT MUTAGEN 147
FT /note="D->A: Inhibits fruit body formation."
FT /evidence="ECO:0000269|PubMed:17470786"
FT MUTAGEN 147
FT /note="D->A: Inhibits fruit body formation; when associated
FT with A-134 and A-136."
FT /evidence="ECO:0000269|PubMed:17470786"
SQ SEQUENCE 335 AA; 37808 MW; 9556E0A5B812FD9E CRC64;
MQAAQLSWEL ENAVTLIDPQ RDSLYRYDEE THKYLSDTRP WTKDPHYFKS VRISAVALLK
MVMHARSGGS LEVMGLMQGY ILPNTFVVTD AFRLPVEGTE TRVNAQDEAN EYMVSYLQSC
REAGRMENAV GWYHSHPGYG CWLSGIDVST QDMQQMSGPF VAVVIDPERT ISAGKVDIGA
FRTFPKDYTP PKEEQEEDEY QTVPLNKAED FGAHASHYYS LEVSLFKSAL DTEILSLLWN
KYWVATLSQS PLFTTRDYGS KQMLDLSQKT RRVARGIESN PPRGGAPTQV RDQQLERVVK
DGQRIVSEEV KGLLAAEVKM QLFQGIGGKQ TVEST
