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Database: UniProt
Entry: A0A0C3CWS7_HEBCY
LinkDB: A0A0C3CWS7_HEBCY
Original site: A0A0C3CWS7_HEBCY 
ID   A0A0C3CWS7_HEBCY        Unreviewed;      1029 AA.
AC   A0A0C3CWS7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN   ORFNames=M413DRAFT_418720 {ECO:0000313|EMBL:KIM48301.1};
OS   Hebeloma cylindrosporum h7.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX   NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM48301.1, ECO:0000313|Proteomes:UP000053424};
RN   [1] {ECO:0000313|EMBL:KIM48301.1, ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RA   Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN831769; KIM48301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3CWS7; -.
DR   STRING; 686832.A0A0C3CWS7; -.
DR   HOGENOM; CLU_002323_0_0_1; -.
DR   OrthoDB; 151732at2759; -.
DR   Proteomes; UP000053424; 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; 1.
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:UP000053424};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          7..319
FT                   /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21505"
FT   DOMAIN          765..923
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   REGION          821..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          983..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..859
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1029 AA;  110804 MW;  AEF93164BCE5B373 CRC64;
     MVRPQSSAAG VLALLQEPDP IFKQHALKAL NPLVPQFWAE ISEHIAIIEA LYESDELPKP
     ARDAAALVAS KVYYFLGEYD EALSFALGSG NAFQAETRAY GSEEYVETII SKAIDRYIQA
     RSTEQSGSKE KIDPRLQTTI EGIFGRCISE GEYKQAIGIA LESHRLDVIS SIYLQTKDVS
     LLSYAMEGVL DTGFSLSYRD QVLRFLFPLF PQLTAGDGSP HVHALTRLLV TLSDPSLTIP
     LLASLVSTEQ LLAYQFAFDL VEGGSQDFLE TLRAELPEGD EACPRHPSQK TRPVYDKLRT
     ILTGKESVKL YREFLKRNNQ TDLLILKNTK DALEPRSSIY HTALTLQNAF MHAGTTSDVF
     LRENLEWLGL ASNWSKFSAT AGLGVIHKGY FEQGQTILGP YLPQSGGESN IPGANYSEGG
     ALYALGLINA GCGSDITTYL RDALKAAQGE VVQHGAALGL GVAGMGSKSL EAFEDLKNIL
     FTDSAVAGEG AGYAMGLVML GTAAADPVRE MLQYARETQH EKIIRGLAMG IAFIYYGRQE
     EADETIKLLL TEKDPILRYG GVYAMALAYA GTANNDAVRK LLHIAVSDTS DDVRRAAVTS
     LAFLLFKNPA QVPRVVQLLS ESYNPHVRCG ATLALGIACA GTGLPDAIEI LEPMTKDSVD
     FVRQGAFIAL GMILVEQSEA SSPSIIPTRA KYTKVISDKH EDPMARFGAS IGQGFIDAGG
     RNVTISLQSR AGSTNTSAIV GMVMFCQFWY WYPLAHCACL AFSPTGIIGL NGDLKAPKFD
     YISNAKPSLF AYPLSTKPPK KETATKVATA VLSTTAKVKA REKKKAAAEG DSMDLVKPFD
     TKQEGDADVD MKTDEASPRD GDVSPITQSV SNLPEESKPS TSKAKKAEPS FEQRPNFSRV
     TPAQLAYISF PPDGRYQPVR AVSTKTPLSK AGKAVATSGP SSSVLGLGSE KYAGGGGILL
     LTDLQPNEEA EFIEIETAPP VAPPAAEVVP AGNGSTVAPP PTGRHIALDE NAPESEPPES
     FEYPFDNDT
//
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