ID A0A0S7DRB5_9EURO Unreviewed; 1139 AA.
AC A0A0S7DRB5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=ALT_008300 {ECO:0000313|EMBL:GIM39816.1}, CNMCM8060_000438
GN {ECO:0000313|EMBL:KAF4180963.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:KAF4180963.1, ECO:0000313|Proteomes:UP000713487};
RN [1] {ECO:0000313|EMBL:GIM39816.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM39816.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4180963.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4180963.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4180963.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4180963.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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:KAF4180963.1}.
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DR EMBL; BCLY01000009; GIM39816.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000010; KAF4180963.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DRB5; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_5439; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000713487; 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; 2.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..120
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 194..433
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 880..1051
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 121..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 124631 MW; 0957F909B8A517B4 CRC64;
MVGLASAAGL VGFLSEPDPE LRVFALKTLD SQIDLLWTEV VDAVPQIEAL YEDESFPERE
LAALVAAKVY YHLQEYNESM VFALGAGKLF KLENCGEFEE TIIAKCVDTF ISLSAAQRPA
AGDSSANLNN SFPTSGEGAT STSASLTSPI TPFSQSTLPS KSLLSRQEVP GLDAAHPGGE
DVSVKHDETS LVLKRGVQGQ LQAVIERLFE QCFVQKRYRQ VIGIAIEAKN LDVLRRTIVR
ASEDEKKHGG SRRSEELMEY VLDICMGIVQ ERAFRNEILK LILELLNEIP APDYFSIAKC
VVFLNEHSMA SVILRQLVEK GDARSLAVAY QISFDLYDNS TQEFLKKVRE EIAELVPEAQ
QADSSKTESQ EEPKESDPLL QDQSSSEQSR SLGSNDAQAE LSDEARTAFK NILEILDGIK
SIQLNLEFLY RNNKADIAIL NKVRDSLEAR NSIFHTAVTL SNAFMHAGTT HDKFFRDNLE
WLGKAVNWSK FTATAALGVI HRGNLSQGQK LLQPYLPREH IAGVGGSGSV YSQGGSLYAF
GLIYANHGGM AVDMIRDHFK KATEEVVQHG GALGLGVAGM ATGDDGIYED LRNVLYTDSA
LNGEAVGLAM GLVMLGTGNM RALEDMIQYA HDTQHEKIVR GLAMGMALIM YGRQEAADEL
INGLLGDPDP TLRYGGIMTI ALAYCGTGSN KAVRRLLHVA VSDVNDDVRR VAVLSLGFIL
FRKYQSVPRM VELLSESYNP HVRYGAAMAL GISCAGTGLD EAIDLLEPML KDSTDFVRQG
ALIALAMVLV QQNEAMNPRV SSLRKAMMKM IGDRHEDAMA KFGCAVALGI IDAGGRNCTI
SLQTQTGNLN MPGIVGAAVF IQYWYWFPLT HFLSLSFTPT AVIGVDQKLE VPFFKFHSNT
RPSLFDYPPE QQVKAEEAPE KVKTAVLSTT AQAKRRAQRR EKQQRRESMD VDQTPTTPKV
SDQLPEKMET DEGVEKPEEE AKEGEKGAGE GPKKKAEREK VGYELENMSR VLPAQLKYLT
FPDPRYEPVK RPTGGVVVVL DKNPDEPRET IEMKASKEVR QPAATAESLQ DRLQAAIGAA
ALQTPQRDAG RMPLGADPTA AAGAAAAAGV LTAVDEDEEG GEEAPVPEEF EYESEGMEE
//
