ID A0A0D1XWJ3_9PEZI Unreviewed; 1140 AA.
AC A0A0D1XWJ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=26S proteasome regulatory subunit RPN2 {ECO:0000256|PIRNR:PIRNR015947};
GN ORFNames=PV09_02016 {ECO:0000313|EMBL:KIW07146.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW07146.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW07146.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW07146.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-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}.
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DR EMBL; KN847533; KIW07146.1; -; Genomic_DNA.
DR RefSeq; XP_016217015.1; XM_016354999.1.
DR AlphaFoldDB; A0A0D1XWJ3; -.
DR STRING; 253628.A0A0D1XWJ3; -.
DR GeneID; 27309989; -.
DR VEuPathDB; FungiDB:PV09_02016; -.
DR HOGENOM; CLU_002323_0_1_1; -.
DR InParanoid; A0A0D1XWJ3; -.
DR OrthoDB; 151732at2759; -.
DR Proteomes; UP000053259; 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:UP000053259};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 5..133
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 199..368
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 897..1066
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 122..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 124449 MW; B86FE24E3DD84209 CRC64;
MVGLTSAAGL VGFLAEPDPA LQSFALHRLN ENVDLLWPEV AVSLGQIEAL YEDDSFPERE
LAALVASKVY YQLQEYDESM RFALGAGKLF NIDQPGEFEN TIIMKCIDTY IALSVLHNPP
TPASSTDKRD LQLSTSFSGN SEGASTSAGI TSPTTPFSQS ALPSKSLLSR QDSSTYDASI
PGGGNAGIIG AHASPMVLKR TVQKNLQGIV RRIFESCYAS GDYRQVVGIA IEARNLEVLR
EAILEAAKAG KGKKAAVSGA AQKGEELMEY VLDICMNVVQ ERGLRNDILR LILDLLNDIP
NPDYFAIAKC VVYLGQHSMA SNMLKHLVER GDGKSLAIAY QISFDLYDNG TQEFLGNVID
ELPETEEAKE EGSAPHANGS IPHPASANSE SGAEPKETDQ LLTEVEQQEA KTMVSRTKQK
PASDEEKKAF TLIRHILRGT KSIELNLEFL YRNNHTDKTV LNKIRDSLEA RNSIFHTGVT
FANAFMNSGT TNDSFFRENL EWLGKAVNWS KFTATAALGV IHRGNITQGQ KLLEPYLPRE
QSMSNSVYSQ GGSLFALGLI YTNHGTNVLE YLRTNFNRAN EEVVQHGGAL GLGLAGMATG
SKQIYEDLKQ VLYTDSAING EAVGLSMGLV NLGTGNIAAL EDMIQYAHDT QHEKIVRGLA
LGMALVMYAR QEAADELING LLEDPDPTLR YGGIMTIALA YCGTGSNKAV RKLLHVAVSD
VSDDVRRVAV MSLGFVLFRK PGSVPRMVEL LAESYNPHVR YGATMALGIA CAGTGLDEAI
DLLEPMMKDS VDFVRQGALI ALAMILVQQN EAMNPKVGTI RKQLAKVIAD RHEDAMAKFG
CALALGIIDA GGRNCTIGLQ TQTGNLNMTA IVGMAVFTQY WYWFPLTHFL SLAFIPTSII
GVDQDLEIPS FKFHSNTRPS MFDYPPEQEV KTEEAPEKVK TAVLSTTAQA RRRRQAKERQ
ARRESMSMSM DIEQTPTTPK VSTDDDKMDT DEKEDKKGEE DAIVETSKKK TEKEKVGYDL
ENMSRVLPAQ LKYISFPAGR YVPVKKPTGG VILLHDTQPD QPKTLVELKV KKTTVQPAPT
RDNAAAVAPQ TPVQRSASRN APGSLAAMLT LAAVDEDNDE GEEAEVPGSF EYETDDEGED
//
