ID A0A1S3CXK7_DIACI Unreviewed; 231 AA.
AC A0A1S3CXK7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN Name=LOC103507227 {ECO:0000313|RefSeq:XP_008469900.1};
GN Synonyms=LOC103520961 {ECO:0000313|RefSeq:XP_008484282.1};
OS Diaphorina citri (Asian citrus psyllid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC Diaphorininae; Diaphorina.
OX NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_008469900.1};
RN [1] {ECO:0000313|RefSeq:XP_008469900.1, ECO:0000313|RefSeq:XP_008484282.1}
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 -!- 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. {ECO:0000256|ARBA:ARBA00024953}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC -!- SUBUNIT: Component of the proteasome complex.
CC {ECO:0000256|RuleBase:RU004203}.
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. {ECO:0000256|ARBA:ARBA00026071}.
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_008469900.1; XM_008471678.3.
DR RefSeq; XP_008484282.1; XM_008486060.2.
DR RefSeq; XP_017304158.1; XM_017448669.1.
DR STRING; 121845.A0A1S3CXK7; -.
DR PaxDb; 121845-A0A1S3CXK7; -.
DR GeneID; 103507227; -.
DR GeneID; 103520961; -.
DR KEGG; dci:103507227; -.
DR KEGG; dci:103520961; -.
DR OMA; TFIYGYC; -.
DR OrthoDB; 754468at2759; -.
DR Proteomes; UP000079169; 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:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd03762; proteasome_beta_type_6; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
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:SF8; PROTEASOME SUBUNIT BETA; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
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|RuleBase:RU004203};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW Reference proteome {ECO:0000313|Proteomes:UP000079169}.
FT ACT_SITE 29
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 231 AA; 25215 MW; 5935E67EE1F8E5D5 CRC64;
MWNKDYNVNA YHGGVEAPDW LTAKHSCGTT IIAVEFDGGV VIGADSRSST GAYVANRVAD
KLTRVTDNIY CCRSGSAADT QAISDFVSYN LDLQRMELGE EPLVYSGAKL FQELVYSYRD
SLTAGIICAG WDRKKGGQVY CIPLGGMLMR QKMAMGGSGS TYLYGHMDNQ FKENMTKKEA
MDFVTRAICH AMARDGSSGG VVRLGVITGE APIERHVIYG KDLPYLTSDV K
//
