ID S0DSD7_GIBF5 Unreviewed; 1154 AA.
AC S0DSD7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=FFUJ_02417 {ECO:0000313|EMBL:CCT65474.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT65474.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
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; HF679025; CCT65474.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DSD7; -.
DR STRING; 1279085.S0DSD7; -.
DR EnsemblFungi; CCT65474; CCT65474; FFUJ_02417.
DR VEuPathDB; FungiDB:FFUJ_02417; -.
DR HOGENOM; CLU_002323_0_1_1; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000016800; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProtKB-UniRule.
DR GO; GO:0034515; C:proteasome storage granule; IEA:EnsemblFungi.
DR GO; GO:0004175; F:endopeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:EnsemblFungi.
DR GO; GO:0043248; P:proteasome assembly; IEA:EnsemblFungi.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
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:UP000016800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..133
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 192..423
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 867..1036
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 360..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 126143 MW; 67B4E2376F53987C CRC64;
MPGIVSATGV LAFLTDEEPE LKVFALQTLN DDIDTVWTEV AAVLTQIEAL YEDESFPERQ
LAALVLAKVY YHLQAYNDSM VFALAAGDLF KLDSPGEFEE TIISKCVDQY IAVNAAKKAA
PQASKSTDLP ELATTFASGA EGAVMSPTTP FSQTTLPPKS LLSRDSIDNT MVEATFQPAF
KQGRSGSIAE LPDQATSSLQ RVVERLFESC LEQGRYRQVV GIAVEAKKLD VLRSVIKRAS
DDEKKAKSNP LENSPGPAED LMEYTLSICM DIVQERAFRT EILRLILDLL NDIPNPDYFA
IAKCVVYLNS DEEASRMLRS LVEKGDRSSI ANAYQIAFDL YDNGTQEFLG KVLASLPASK
PVKKETDENG EQSNESESLL QNKQEDPEDE LPEPVSKAYS NIREILDGSK TIRLNLEFLY
RNNRTDLSIL NKVRDSLEGR NSIFHTAVTF CNAFMNQGTT NDKFFRDNLE WLGKAVNWSK
FTATAALGVI HRGNLSQSRK LLEPYLPRQG GLSSGSIFSQ GGALYAYGLI HANHGADALD
YLKEQFGQAE EEVVQHGGAL GLGIAGMATG DWEIFEKLRE ILFQDSALNG EAVGLAMGLI
MLGTGNVKAL EDMITYAHET THEKIVRGLA IGMALIMFGR QEGADVLIEG LLNDPDPTLR
YGGIMTVALA YCGTGSNKAI RKLLHIAVSD VNDDVRRIAV MSLGFILFRK PGSVPRMVEL
LSESYNPHVR YGSAMALGIS CAGTGLDEAI DLLEPMMKDP TDFVRQGALI SLAMILVQQN
EVMNPKVSSI RKTLKKVVGD RHEDAMTKFG AALALGIIDA GGRNCTIGLQ TQTGNLNMAG
IVGMAVFTQY WYWFPFTHFL SLSFSPTSII GLDHDLEIPN FKFHCATRPS LFDYPPEQEV
KTEEGPALIA TAILSTTAQA KRRAQKKERA QRRESMEIDT APSKSGGDKM DVDEDKKVDE
AKDKKEEQEK EPAASTDTKK KPEKEKVGYE IENMTRVLPG QLKYVSFPAG RYKPVKKPTG
GPLLLLDSEP EEEKSLLEEK LKKVTTERAP VAGQQTGRGG RGGAQRAVLD SLAESRGGAN
SAMLGQLLRN QGRSPFGLLD AEPQTPGGNA SGAAAAAGVL TAVDEDSDDD EEAPVPKEFE
YFTDAGEDDD EDDE
//
