ID A0A165Q6F3_EXIGL Unreviewed; 265 AA.
AC A0A165Q6F3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|PIRNR:PIRNR001213};
GN ORFNames=EXIGLDRAFT_636302 {ECO:0000313|EMBL:KZW03151.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03151.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW03151.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03151.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- FUNCTION: Non-catalytic component of the proteasome.
CC {ECO:0000256|PIRNR:PIRNR001213}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR001213}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR001213}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC {ECO:0000256|PIRNR:PIRNR001213}.
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DR EMBL; KV425884; KZW03151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165Q6F3; -.
DR STRING; 1314781.A0A165Q6F3; -.
DR InParanoid; A0A165Q6F3; -.
DR OrthoDB; 116867at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR CDD; cd03760; proteasome_beta_type_4; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR016295; Proteasome_beta4.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR PANTHER; PTHR32194:SF6; PROTEASOME SUBUNIT BETA; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF001213; Psome_endopept_beta; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR001213};
KW Nucleus {ECO:0000256|PIRNR:PIRNR001213};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PIRNR:PIRNR001213};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
SQ SEQUENCE 265 AA; 29416 MW; 7011421E0E893768 CRC64;
MDHFPTNWGR PRSEAVDLYN TYPLHNRPGP KADAFTEGVQ RTQAPIVTGT SVLAFRFKDG
IIMAADNLAS YGSLARFKDV QRLIPVGAYT VIGGGGDMSD LQHINHLLEG LIIEELCEED
GHALGPAEIY EYLSQVLYAR RSKMDPLWNS LLVGGFKDGK SFLGYVDLLG TTYTASTLAT
GYGSMIAQPL LRKYVEGREE TLTEDEGKKI IEECMKVLFY RDARSINKYQ IATITEKGIS
ISESLSAHTE WSFAEKIRGY GAQTQ
//
