ID   G1WXN7_ARTOA            Unreviewed;      1043 AA.
AC   G1WXN7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN   ORFNames=AOL_s00004g47 {ECO:0000313|EMBL:EGX54014.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX54014.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX54014.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       {ECO:0000256|PIRNR:PIRNR015947}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S1 family.
CC       {ECO:0000256|ARBA:ARBA00006308, ECO:0000256|PIRNR:PIRNR015947}.
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:EGX54014.1}.
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DR   EMBL; ADOT01000005; EGX54014.1; -; Genomic_DNA.
DR   RefSeq; XP_011116999.1; XM_011118697.1.
DR   AlphaFoldDB; G1WXN7; -.
DR   STRING; 756982.G1WXN7; -.
DR   GeneID; 22888348; -.
DR   eggNOG; KOG2062; Eukaryota.
DR   HOGENOM; CLU_002323_0_1_1; -.
DR   InParanoid; G1WXN7; -.
DR   OMA; IMFGRQE; -.
DR   OrthoDB; 151732at2759; -.
DR   Proteomes; UP000008784; Unassembled WGS sequence.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR016642; 26S_Psome_Rpn2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR   InterPro; IPR048570; PSMD1_RPN2_N.
DR   InterPro; IPR040623; RPN2_C.
DR   PANTHER; PTHR10943; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10943:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1; 1.
DR   Pfam; PF13646; HEAT_2; 1.
DR   Pfam; PF01851; PC_rep; 3.
DR   Pfam; PF18004; RPN2_C; 1.
DR   Pfam; PF21505; RPN2_N; 1.
DR   PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PIRNR:PIRNR015947};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          7..371
FT                   /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21505"
FT   DOMAIN          814..979
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   REGION          864..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          987..1043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..929
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1004
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1043 AA;  113783 MW;  E914AF0BF6BFC9A0 CRC64;
     MLGPVHNAAG LLGLLEEDDI HLQSSALEQL DILVDEFWSE IADSISKIES LYEDPKFPHR
     QLAALVASKV YYHLGAFEDS MMYALGAGDL FDISGKSEFI DTIISKCIDK YISINNPPPP
     PKDLPPSLPE KADPRLTEVV ERMFQKCYDK EDYKPALGIA IESQRLDIVE QGVRLAGERQ
     RGSKAKQAAN GDAVDKSAEL MEFVFELAMN TVQEIDLREK LLRLLVDLHL EQPSPDYFSV
     SKCVVQLNDY GLAAKLLRDL VSKGDNGSLL IAYQIAFDLD SSATQEFLKH VTSNLPDGEI
     PVGEKTETPE DDDDDIVEET AKLLPRTSSE LISKAAAEMN EKSSKHYKSI RTILKGTKTI
     ELNLEFLFRN NHTEMSILNK IRDCLEARTS LLHNALTFAN GFMNAGTLAD GFLRANLDWL
     GKAVNWSKFT ATAALGVIHR GNLSQGMKLL QPYLPNPSSG TGSPYSQGGS LYGLGLIYAN
     HGEDVLPYLL SQFKDTQDEI VQHGGALGLG VAGMATGKTE IYQELRTVLW TESAISGEAV
     GLAMGLIMLG TANPQAIEEM RSYAHETQRE KVKRGLALGM ALVYYSKQEL ADELIDNLLA
     DMDPILRYGG VLTIALAYCG TGSNSAIRKV LHVAVSDVND DVRRVAVFSL GFILFRKYES
     VPRMVELLAE SYNPHVRYGS ALALGIACAG TGLDEALDLL QPMLKDTVEF VKQGALISIG
     MILVQHNEAM NPKVAEFRKT FERILSDKTE DVLSKFGAAV ALGLLDAGGR NCTIGLQTAT
     GSIDMAAVVG MACFTQYWYW FPLAHFLSLG FRPTGIIGLN VDLEVPDFQM WSKTKPSQFD
     YPPKAEESAE KTVEKIATAV LSTTAKARQR AKRTEKERRE REGSVTDSMI IDPPPETPIA
     TTAGEANGEG KEEETGKKKS TKKSQPKETV GYKIDNMSRV LPAQLKHIDF LEGKYQPVKK
     VTGGVLLLVD TQPEEPAKLL EYKSVKPTVP SGAAGTSTSA QAPSEPVGGG GAAAAAAVLT
     QEDDEEDAPV PSAFDYYSDG EGQ
//