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Database: UniProt
Entry: A0A0D1Y9V7_9EURO
LinkDB: A0A0D1Y9V7_9EURO
Original site: A0A0D1Y9V7_9EURO 
ID   A0A0D1Y9V7_9EURO        Unreviewed;      1133 AA.
AC   A0A0D1Y9V7;
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=PV11_09354 {ECO:0000313|EMBL:KIV77564.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77564.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV77564.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77564.1,
RC   ECO:0000313|Proteomes:UP000053599};
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 Exophiala sideris CBS121828.";
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; KN846954; KIV77564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1Y9V7; -.
DR   STRING; 1016849.A0A0D1Y9V7; -.
DR   HOGENOM; CLU_002323_0_1_1; -.
DR   OrthoDB; 151732at2759; -.
DR   Proteomes; UP000053599; 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   Reference proteome {ECO:0000313|Proteomes:UP000053599};
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          196..441
FT                   /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21505"
FT   DOMAIN          887..1060
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   REGION          364..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1108..1133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..956
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..1000
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1133 AA;  123712 MW;  CEEC72839C92A152 CRC64;
     MVGLVSAAGL VGFLSEPDPE LRSFALKQLD SQVDLLWTEI ANSVGEIEAL YEDDSFPDRE
     LAAIVASKVY YHLQEYNESM AFALGAGKYF NLDNAGEYED TIISKCLDTY IALSASRDPT
     LAAATAGAQP QLDTAFGQGG DGAASISASL TSPVTPFSQS ALPSKSLLSR QNTAVFDPTQ
     AGAEAGQEGT PEAVIQQRNL QKALNRVIES LFEKCFQEKR YRQVVGIALE ARNLDILRRV
     IKRAAEDERK EDGEATKMGE ELMDYVLEIC MSIVQERGLR NEILKLILEL LNEIPSPDYF
     AIAKCVVYLD QHSMASNILR QLVEKGDARS LAVAYQISFD LYDNSTQEFL LKVREELVDL
     LPKEEAKSDA NASETDKMEE DNQEKAEDQL QQELQESAGA PAPSKPKISK PEQQDAVKKI
     RDILDGLTSI HLNIEFLHKS NRVDYSILTK VKDSLEARYS IYHTAVTLSA GFMHAKTATD
     SFFRQNLEWL GKAVNWSKFT ATAVFGVIHQ GNINQVQRLL SPYLPKAGGV SGSHDSPYSQ
     GGSLYAYGLL CANHKGKAVD FLREKFKEAT EEVVQHGGAL GLGVAGMASG DESVFEDLRN
     VLWADSAING EAVGLAMGLV MLGSGNNKVL SDMIQHAHDT QHDKIVRGLA VGMALIMYGR
     QEGADELIQG LLNDTDPTMR YGGILTIAMA YVGTGSNQAV RKLLHVAVSD VSDDVRRIAV
     LSLGFILFRK YSSVPRMVEL LAESYNPHVR YGAAMALGIS CAGTGLADAI DLLEPMLKDP
     TDFVRQGALI ALAMVLVQQN EAMNPKVGAI RKQMLKIIGD RHEDAMCKFG CAMAMGIIDA
     GGRNCTINLQ TQTGNLNMLG IVGVVVFTQY WYWFPLAHFL SLSMTPTAVI AVDQKLEAPV
     FKFHCNTRPS LFDYPPETVT KTDETPEKVK TAVLSTTAQA KRRAAKKEKQ QRRDSMDVDT
     VTPVTPKVDK DDKMDTDESA VKDDEGKKEE GEKKEGEALE VKKKAEKEKV GYDIPNMSRV
     LPAQLKYLTF PDERYQPVKK PTGGVMVVHD TEPEKERETI PLLVSKVEVP AANTGNAVGG
     AAQPPQTPAH QVIGAGAAAA AGVLTAIDED EDEAEDAPVP AEFDYETDGE EDS
//
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