ID A0A0M9VXN0_9HYPO Unreviewed; 1174 AA.
AC A0A0M9VXN0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=ESCO_006612 {ECO:0000313|EMBL:KOS23332.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS23332.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS23332.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-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}.
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:KOS23332.1}.
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DR EMBL; LGSR01000001; KOS23332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9VXN0; -.
DR STRING; 150374.A0A0M9VXN0; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000053831; 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; 3.
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:UP000053831};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 6..132
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 194..423
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 868..1048
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 362..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1174
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 127785 MW; 0BA9ACA8FCA9F1C7 CRC64;
MPGLVSATGV LAFLADEEPE LKVFALQTLN DDIDTVWTEV AGALSQIEAL YEDESFPERQ
LAALVLAKVY YHLQAYNDSM VFALAAGDLF KLDAPSEFEE TIISKCVDQY IAITAAKHAP
PALVSNTDLP ELSTTFSSAA DGAAVLSPTT PFSQTTLPPK SLLSRASLDN TILGTDYQPV
AKDGRSGSIA QLPDKATEAS LQRVIDRLFE SCLAQGRYRQ VVGIAVEAKN LEILRRVIKR
ASEDEKASKV KVQEGQQGPA EELMEYTLSV CMDIVQERAF RTEILRLILD LLNDIPHPDY
FAIARCVVYL NADEEASQML RTLIAKADRT SIANAYQIAF DLYDNGTQEF LGKVLGSLPS
GEVKKEDATE GADKENEPLL QNEQAAPEAE LPEDVAKVYR NVRQILDGSK TVRLNLEFLY
RNNHTDLSIL NRVRDSLEGR SSIFHTAVTF SNAFMNQGTT NDKFFRDNLE WLGKAVNWSK
FTATAALGVI HRGNILQARR LLEPYLPRQG GSIGSGSIFS QGGALYALGL IHANHGAGAL
EYLKTQFSQA EEEVVQHGGA LGLGIAGMGT GDLDIFEKLK ETLFQDSALN GEAVGLAMGL
VMLGTGHVKA LEDMITYAHE TTHEKIVRGV ALGMALIMYG RQEGADVLID GLLNDPDPTL
RYGGIMTVAL AYCGTGSNKA VRKLLHIAVS DVNDDVRRIA VMSLGFILFR KPGSVPRMVE
LLSESYNPHV RYGSAMALGI SCAGTGLDEA IDLLEPMMKD PTDFVRQGAL IALAMIMVQQ
NEVMNPKVAS IRKTLKKVVG DRHEDAMTKF GAAIALGIID AGGRNCTIGL QTQTGNLNMT
GIVGMAVFTQ YWYWFPLTHF LSLSFSPTSV IGLDSDLEIP DFKFHCATRQ SLFDYPPEQE
VKAEEGPALI ATAILSTTAQ ARRRAQKKER AQRRESMDID PAPAKGGDKM DVDEEKATTT
TTTTTTTTKE DPKDKKEMDE KDATPSNESK KKPEKEKVGY EIENMSRVLP GQLKYISFPA
GRYKPVKKPT GGPLLLDDTQ PEEAKNLVEE KLKKVITERA PTTGQQTRNG GRAGGRSLLD
DFADPSNVGV GNSVMSQLLR GNGRHGFGLM DPQTPGGNNG GMGSGAAAAA GVLTAVDEDE
EGDEEASCPR PFDYFTDEED EDEDEDEEDA EDAE
//
