ID A0A1V6Q217_9EURO Unreviewed; 977 AA.
AC A0A1V6Q217;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=COP9 signalosome complex subunit 2 {ECO:0000256|ARBA:ARBA00014879};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN ORFNames=PENANT_c017G07847 {ECO:0000313|EMBL:OQD83320.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD83320.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CSN2 family.
CC {ECO:0000256|ARBA:ARBA00009318}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD83320.1}.
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DR EMBL; MDYN01000017; OQD83320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6Q217; -.
DR STRING; 416450.A0A1V6Q217; -.
DR OrthoDB; 5477605at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd22749; Otubain_C65; 1.
DR Gene3D; 1.25.40.570; -; 1.
DR Gene3D; 3.30.200.60; Peptidase C65 Otubain, subdomain 1; 1.
DR Gene3D; 1.20.1300.20; Peptidase C65 Otubain, subdomain 2; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR019400; Peptidase_C65_otubain.
DR InterPro; IPR042468; Peptidase_C65_otubain_sub1.
DR InterPro; IPR042467; Peptidase_C65_otubain_sub2.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10678; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 11/COP9 SIGNALOSOME COMPLEX SUBUNIT 2; 1.
DR PANTHER; PTHR10678:SF3; COP9 SIGNALOSOME COMPLEX SUBUNIT 2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10275; Peptidase_C65; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 252..420
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT DOMAIN 605..808
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 110753 MW; 01645221A0358A6E CRC64;
MSDDDDFMQD SGDEDYDFEY EDADDDDTGD IGIENKYYNA KQTKVDNPEE AIDEFLGIAP
MEQDKSEWGF KGLKQSIKLE FKLGRYSDAV EHYRELLTYV KSAVTRNYSE KSINNMLDYI
EKGSDDAEAY QCMEEFYSLT LQSFQNTNNE RLWLKTNIKL ARLWLERKQY TQLSKKMREL
HRACQHEDGT DDSSKGTYLL ELYALEIQMF AETKNNKRLK ALYQRALRVR SAVPHPKIMG
IIRECGGKMH MSEENWKEAQ SDFFESFRNY DEAGSMQRIQ VLKYLVLTTM LMKSDINPFD
SQETKPYKND PRISAMTDLV DAFQRDDIHA YEAVLSKHPD VLADPFITEN IDEVSRNMRT
KAVLKLIAPY TRFSLQFISK HIKISVSEVL DILSFLILDK KLNAKIDQDS GTVVVESSSD
VERLRAVGEW SSALRTLWQT TLNGEGLRAD DGVGGMFAGS PIRCAGSSVA QRRKCQEHKL
DFTYAMSISK PWNHHFGPHP FPKQNLNLHL YRDALSSSPL SPVALSLPSY SHSRHSRHSP
STMSNLNALS ADEMERFQKL SNSYEPDVQG PLVSRKEPTQ SVALEYANAD PAFSSKTNAL
AITHPEYRIM KGDGNCGWRA VAFGYFETLF ALRDPMRIQR EITRFKSLEM LLKQVGHSEH
LYEIFTDATE DLFTQTINAI QSGAGDESFL VETFNNEFAS SAVITHFRLL TSSWMRLNPH
RYQAFLSVPL EQYCASQIDP LKTEIDEIGL QALVDGVIEG AGFGVEILYL DRSEGDAVTP
HQLSPHNPSG ATIRLLYRPG HYDLLYPADP NVNMEPIVNY QYAMTSDYSN WNEGPLGFDV
DSSLMAIPNL MADPSFAMGT PMSPMPSVSP APTSPFRMSP QQEMYQSPMQ THAPIPSIPV
SSPPPPIPPP SAAPPPMTTL PSRSSDGPQI RLNPLVMKPN LSRSLPVTTP FKNSPYNQAH
FQNSDFEPIH WEPHDRR
//
