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Database: UniProt
Entry: A0A2Y9DDE6_TRIMA
LinkDB: A0A2Y9DDE6_TRIMA
Original site: A0A2Y9DDE6_TRIMA 
ID   A0A2Y9DDE6_TRIMA        Unreviewed;       201 AA.
AC   A0A2Y9DDE6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   Name=LOC101346461 {ECO:0000313|RefSeq:XP_004372010.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004372010.1};
RN   [1] {ECO:0000313|RefSeq:XP_004372010.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_004372010.1; XM_004371953.2.
DR   AlphaFoldDB; A0A2Y9DDE6; -.
DR   STRING; 127582.A0A2Y9DDE6; -.
DR   GeneID; 101346461; -.
DR   KEGG; tmu:101346461; -.
DR   InParanoid; A0A2Y9DDE6; -.
DR   OrthoDB; 158209at2759; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
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 {ECO:0000256|RuleBase:RU004203};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004203};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480}.
SQ   SEQUENCE   201 AA;  22728 MW;  D9D858B336511814 CRC64;
     MEYLIGIQGP DYVLVASDRV AASSIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI
     QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV NLLLAGYDEH EGPALYYMDY
     LAALAKAPFA AHGYGAFLTL SILDRYYTPT ISRERAVELL RKCLEELQKR FILNLPTFSV
     RVIDKNGIHD LENISFSKGG S
//
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