ID A0A0A2L5N5_PENIT Unreviewed; 488 AA.
AC A0A0A2L5N5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=COP9 signalosome complex subunit 2 {ECO:0000256|ARBA:ARBA00014879};
GN ORFNames=PITC_001430 {ECO:0000313|EMBL:KGO75279.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO75279.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO75279.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO75279.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO75279.1}.
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DR EMBL; JQGA01000480; KGO75279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L5N5; -.
DR STRING; 40296.A0A0A2L5N5; -.
DR HOGENOM; CLU_028981_0_1_1; -.
DR OMA; SEENWKD; -.
DR OrthoDB; 5477605at2759; -.
DR PhylomeDB; A0A0A2L5N5; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.570; -; 1.
DR InterPro; IPR000717; PCI_dom.
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 SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000313|EMBL:KGO75279.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 252..420
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..482
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 449..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 56225 MW; 84D9EE2AEFFC7045 CRC64;
MSDDDDFMQD SGDEDYDFEY EDADDDDSGD IGIENKYYNA KQIKVDNPEE AVDEFLGIAP
MEQDKSDWGF KGLKQAIKLE FKLGRYSDTV VHYRELLTYV KSAVTRNYSE KSINNMLDFI
EKGSDNEEAY QCMEEFYSLT LESFQNTNNE RLWLKTNIKL ARLWLERKQY GQLGKKMREL
HRACQREDGS DDTSKGTYLL ELYALEIQMS AETKNNKRLK ALYQRALRVR SAVPHPKIMG
IIRECGGKMH MSEENWEEAQ SDFFESFRNY DEAGSMQRIQ VLKYLVLTTM LMKSDINPFD
SQETKPYKND PRISAMTDLV DAFQRDDIHA YEDVLSKHPD VLADPFIAEN IDEVSRNMRT
KAVLKLIAPY TRFSLQFISK HIKVSVPEVL DILSFLILDK KLNAKIDQDN GTVVVESASD
VERLRAVGEW SSALRNLWQT TLNGEGLRAN EPSQGSIFQS SLGDEGMRST GPRARKDGRG
KMPAKWLF
//
