ID A0A094BJY8_9PEZI Unreviewed; 1118 AA.
AC A0A094BJY8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=V494_05751 {ECO:0000313|EMBL:KFY35630.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY35630.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY35630.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY35630.1}.
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DR EMBL; JPJW01001940; KFY35630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BJY8; -.
DR STRING; 1420907.A0A094BJY8; -.
DR HOGENOM; CLU_002323_0_1_1; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000029288; 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; IPR004155; PBS_lyase_HEAT.
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; 4.
DR Pfam; PF18004; RPN2_C; 1.
DR Pfam; PF21505; RPN2_N; 2.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SMART; SM00567; EZ_HEAT; 2.
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:UP000029288};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..119
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 192..418
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 861..1034
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 360..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 121838 MW; 6AFC4C72A92DF4E7 CRC64;
MPGLVSATGV LGFLSDEEPE LKIFALQTLN DDIDTLWTEV AGSVGQIEAL YEDDTFPERR
LAALVLAKVY YHLQEYNESM AFALGAGDLF KLDNGGEFEE TIISKCVDQY IALSASHRPR
ASDAGTSGIP TLATSFANTA GDSNVSGALS SPTTPFSQST LPSKSLLSRQ STDISADYPT
ISTGSLSLSV ADRKTQVALE NVIERLFESC LREGRYRQVV GIAIEARNLE VLRRVIKRAS
DDEKKAGKSA DNGSGPTEEL MEYVLNICMD VVQERALRTE ILKMILDLLN DIPTPDFFAI
AKCVVYLNLD GEASSMLRKL VEKGDDSSRA VAYQIAFDLY DNGTQEFLAN VQKALPVEKK
AEEPVAEGES EPLLGENKDT SNTDNFSPEQ IQIFTNIRSI LDGSKSIKLN LEFLYRNNHT
DISILNKVRD SLEGRNSIFH TAVTFCNAFM NQGTTNDQFF RDNLEWLGKA VNWSKFSATA
ALGVIHKGNL SQCRKLLEPY LPRPSSVGGS IFSQGGALYA YGLIYANHGA EALDYLRQSF
NDTQEEVVQH GGALGLGLAG MATGSEEIYE NLKSILYTDS ALNGEAVGLA MGLIMLGTGN
IKALEDMIQY AHDTQHEKIV RGVAMGMALI MFGRQEGADE LIEGLLNEAD PTLRYGGIMT
VAMAYCGTGS NKAVRKLLHV AVSDVNDDVR RIAVMSLGFI LFRKPSSVPR MVELLSESYN
PHVRYGAAMA LGISCAGTGL DEAVDLLEPM MKDPTDFVRQ GALIALAMIM VQQNEAMNPK
VAAIRKTLKK IVGDRHEDAM TKFGCSLALG IIDAGGRNCT IGLQTQSGNL NMPGIVGMAV
FTQYWYWFPF THFLSLSFTP TSMIGLDHDL EIPNFKFHSA TRPSLFDYPP EQEVKTDEAP
TLIATAVLST TAQARRRAQK KERAQRHESM DIDQTPTTPK VSAPDAEKME VDEESKEGGK
KEGEEDKEAG AQGTPKKKAE KEKVGYDIEN MSRVLPAQLK FISFPAGRYK PVKKPTGGVI
MLLDSQPEEP KSLIEEKMKK ASVERAAALP TLEDLRQESF SLRRLADAQG EAAGALSGAG
AAAGAGVLTA VDEDGEGGEE AAVPNEFEYF SDEEEEEN
//
