ID PSB4_NEUCR Reviewed; 203 AA. AC Q9P6U7; Q7RV10; V5IN28; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 19-FEB-2014, sequence version 2. DT 24-JAN-2024, entry version 136. DE RecName: Full=Probable proteasome subunit beta type-4; DE AltName: Full=Proteosome catalytic beta subunit 4; GN Name=pcb-4; ORFNames=15E6.60, NCU01368; OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / OS FGSC 987). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=367110; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX PubMed=12655011; DOI=10.1093/nar/gkg293; RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.; RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora RT genome sequence."; RL Nucleic Acids Res. 31:1944-1954(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; RX PubMed=12712197; DOI=10.1038/nature01554; RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; RT "The genome sequence of the filamentous fungus Neurospora crassa."; RL Nature 422:859-868(2003). CC -!- FUNCTION: Non-catalytic component of the proteasome, a multicatalytic CC proteinase complex which is characterized by its ability to cleave CC peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group CC at neutral or slightly basic pH. The proteasome has an ATP-dependent CC proteolytic activity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two CC 19S regulatory subunits. The 20S proteasome core is composed of 28 CC subunits that are arranged in four stacked rings, resulting in a CC barrel-shaped structure. The two end rings are each formed by seven CC alpha subunits, and the two central rings are each formed by seven beta CC subunits. The catalytic chamber with the active sites is on the inside CC of the barrel (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. CC Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- CC ProRule:PRU00809}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB88637.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL353822; CAB88637.1; ALT_SEQ; Genomic_DNA. DR EMBL; CM002240; ESA42564.1; -; Genomic_DNA. DR EMBL; CM002240; ESA42565.1; -; Genomic_DNA. DR PIR; T48798; T48798. DR RefSeq; XP_011394518.1; XM_011396216.1. DR RefSeq; XP_011394519.1; XM_011396217.1. DR AlphaFoldDB; Q9P6U7; -. DR SMR; Q9P6U7; -. DR STRING; 367110.Q9P6U7; -. DR MEROPS; T01.984; -. DR PaxDb; 5141-EFNCRP00000004093; -. DR EnsemblFungi; ESA42564; ESA42564; NCU01368. DR EnsemblFungi; ESA42565; ESA42565; NCU01368. DR GeneID; 3876867; -. DR KEGG; ncr:NCU01368; -. DR VEuPathDB; FungiDB:NCU01368; -. DR HOGENOM; CLU_035750_12_1_1; -. DR InParanoid; Q9P6U7; -. DR OrthoDB; 158209at2759; -. DR Proteomes; UP000001805; Chromosome 2, Linkage Group V. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:EnsemblFungi. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB. DR GO; GO:0061133; F:endopeptidase activator activity; IEA:EnsemblFungi. DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IEA:EnsemblFungi. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi. DR CDD; cd03758; proteasome_beta_type_2; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR035206; Proteasome_beta2. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1. DR PANTHER; PTHR11599:SF6; PROTEASOME SUBUNIT BETA TYPE-2; 1. DR Pfam; PF00227; Proteasome; 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; Nucleus; Proteasome; Reference proteome. FT CHAIN 1..203 FT /note="Probable proteasome subunit beta type-4" FT /id="PRO_0000148053" SQ SEQUENCE 203 AA; 22418 MW; B4EAEBEFB7B56F99 CRC64; MEVLLGITGK DFTIIAASKA AMRGATILKA SDDKTRSLNK HTLMAFSGEA GDTVQFAEYT QANAQLYSMR NGTDLSPSAL ANFVRGELAT SLRSRKPYNV NLLLGGVDPI THKPSLYWLD YLASLAKVPY AAHGYAQYYC LSILDKHHHP DITLHQGIKL LNLCTDELKR RLPIDFKGMT VKAVTKDGII DIEFDDDKVV KMA //