ID A2F8W4_TRIV3 Unreviewed; 191 AA. AC A2F8W4; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203}; GN ORFNames=TVAG_403280 {ECO:0000313|EMBL:EAX98646.1}; OS Trichomonas vaginalis (strain ATCC PRA-98 / G3). OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae; OC Trichomonas. OX NCBI_TaxID=412133 {ECO:0000313|EMBL:EAX98646.1, ECO:0000313|Proteomes:UP000001542}; RN [1] {ECO:0000313|EMBL:EAX98646.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G3 {ECO:0000313|EMBL:EAX98646.1}; RA Amadeo P., Zhao Q., Wortman J., Fraser-Liggett C., Carlton J.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAX98646.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G3 {ECO:0000313|EMBL:EAX98646.1}; RX PubMed=17218520; DOI=10.1126/science.1132894; RA Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q., RA Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S., RA Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C., RA Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S., RA Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D., RA Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y., RA Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M., RA Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J., RA Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B., RA Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A., RA Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S., RA Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M., RA Johnson P.J.; RT "Draft genome sequence of the sexually transmitted pathogen Trichomonas RT vaginalis."; RL Science 315:207-212(2007). CC -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase CC complex which is characterized by its ability to cleave peptides with CC Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or CC slightly basic pH. The proteasome has an ATP-dependent proteolytic CC activity. {ECO:0000256|RuleBase:RU004203}. CC -!- SUBUNIT: Component of the proteasome complex. CC {ECO:0000256|RuleBase:RU004203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}. CC Nucleus {ECO:0000256|RuleBase:RU004203}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. CC {ECO:0000256|RuleBase:RU004203}. 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; DS113667; EAX98646.1; -; Genomic_DNA. DR RefSeq; XP_001311576.1; XM_001311575.1. DR AlphaFoldDB; A2F8W4; -. DR STRING; 5722.A2F8W4; -. DR MEROPS; T01.984; -. DR GeneID; 4756446; -. DR KEGG; tva:TVAG_2v0689170; -. DR VEuPathDB; TrichDB:TVAG_403280; -. DR VEuPathDB; TrichDB:TVAGG3_0689170; -. DR eggNOG; KOG0177; Eukaryota. DR InParanoid; A2F8W4; -. DR OMA; RGPTVLK; -. DR Proteomes; UP000001542; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IBA:GO_Central. DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. 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; 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; PS51476; PROTEASOME_BETA_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|RuleBase:RU004203}; KW Nucleus {ECO:0000256|RuleBase:RU004203}; KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203}; KW Reference proteome {ECO:0000313|Proteomes:UP000001542}. SQ SEQUENCE 191 AA; 21398 MW; FF4C704A60E6FC18 CRC64; MLSIVGLQGP DWVLIAADSS VSSSIICMSE NYDRIAQLDD RHALAMSGET GDCLQLSEYL QGNVALYKFR NGVELSSDAL AHFIRHTMAK AVRKSPYEVN MLLSGYDGKP HLYFMDYLGT LQSIPYGAQG YCQYFVMSVF DKHYKEGLTL EDGKELMKLA LNQIKQRFTV APHGFIVKLV DKNGITKIDL E //