ID A0A162Y1J8_DIDRA Unreviewed; 1045 AA.
AC A0A162Y1J8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=ST47_g9286 {ECO:0000313|EMBL:KZM19785.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM19785.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM19785.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM19785.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM19785.1}.
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DR EMBL; JYNV01000290; KZM19785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162Y1J8; -.
DR STRING; 5454.A0A162Y1J8; -.
DR Proteomes; UP000076837; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 5..121
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 200..373
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 809..978
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 368..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1045
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 112977 MW; 94DC00C2A42C9821 CRC64;
MVGLTSAAGV VGFLSEPDPA LRSFALHQLN DQIDLLWPEV AGSVSQIEAL YEDESFPERE
LAALVAAKVY YQLQEYNESM VFALGAGKLL DIHKAGEFEE TILAKCVDTY IAMSAMHNPP
TPVSKASQAT PQLSISFTGG STGAASTSAS LTSPITPFSQ SALPSKSLLS REDSNTFDPT
IPGGGNAGVV GAHPTPMMLQ RNVQKNLQAT IRRIFESCYE SGDYKQVVGI AIEARNLDVL
RASIVRASQD EKKKAGKKPA TGASTKSEEL MDYVLDICMN VVQERGLRNE ILRLILDLLN
DNEIPNPDYF SIAKCVTYLD QHSLASKLVR QLVEQGDDKS LATAYQISFD LYENGTQEFL
AKVMADLPES EGDDDESKPS ANGDASEAKE SDSLLADADT SNVSDLPPRT NKSSSDDHNK
AFSSSVLNKI RDSLEARSSI FHSSVTFANA FMNAGTTNDT FFRENLDWLG KAGQKLLDPY
LPKDSVSTGS HYEQGGSLYA LGLIYANHGS NVLDYLVKQF QNASEEVIQH GGALGVGVAG
MATGSEEIFD AFKSVLYTDS AINGEAVGLS MGLVMLGTGS IKALEDMIQY AHDTQHEKIE
AADELINGLL EDPDPTLRYG GIMTIALAYC GTGSNKAVRR LLHVAVSDVS DDPGSVPRMV
ELLSESYNPH VRYGATMALG IACAGTGLPE AVDLLEPMMK DSTDFVRQGA LIALAMIMVQ
QNEATNPKVA SIRKQLTKII GDRHEDAMAK MGCALALGII DAGGRNCTIG LQTPTGNLNM
AAIVGMAVFT QYWYWFPLTH FLSLSFTPTA IIGVDQDLQI PSFKFHSNTR PSMFDYPPET
EVKAEEAPEK IKTAVLSTTA QDKRRRMVKE RQRRRESMDV DQTPTTPKPA DDDKMDVDDE
KKDDEKKEDE KAEGASTESP KKKAEKEKVG YELENMSRVL PAQVKHITFP GDRFIPVKKP
TLGVILLTDT KPSEPKTLLE LKVKKAAPAP APGASGSSGE QAAEGAAEAE SSGPTTDNLV
DEGDEEASLP GDFEYESDTN PNDSE
//
