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Database: UniProt
Entry: A0A2H5Q9N3_CITUN
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ID   A0A2H5Q9N3_CITUN        Unreviewed;       273 AA.
AC   A0A2H5Q9N3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   ORFNames=CUMW_208840 {ECO:0000313|EMBL:GAY61293.1};
OS   Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY61293.1, ECO:0000313|Proteomes:UP000236630};
RN   [1] {ECO:0000313|EMBL:GAY61293.1, ECO:0000313|Proteomes:UP000236630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX   PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA   Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA   Fujiyama A., Kaminuma E., Nakamura Y.;
RT   "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT   unshiu Marc.) using a hybrid assembly approach.";
RL   Front. Genet. 8:180-180(2017).
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: The proteasome is a multicatalytic proteinase complex which
CC       is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC       Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC       pH. The proteasome has an ATP-dependent proteolytic activity.
CC       {ECO:0000256|ARBA:ARBA00002000}.
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 20S core complex of the 26S proteasome. The
CC       26S proteasome is composed of a core protease (CP), known as the 20S
CC       proteasome, capped at one or both ends by the 19S regulatory particle
CC       (RP/PA700). The 20S proteasome core is composed of 28 subunits that are
CC       arranged in four stacked rings, resulting in a barrel-shaped structure.
CC       The two end rings are each formed by seven alpha subunits, and the two
CC       central rings are each formed by seven beta subunits. The catalytic
CC       chamber with the active sites is on the inside of the barrel.
CC       {ECO:0000256|ARBA:ARBA00011517}.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAY61293.1}.
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DR   EMBL; BDQV01000265; GAY61293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5Q9N3; -.
DR   STRING; 55188.A0A2H5Q9N3; -.
DR   Proteomes; UP000236630; Unassembled WGS sequence.
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; cd03763; proteasome_beta_type_7; 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:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 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:UP000236630}.
FT   ACT_SITE        40
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ   SEQUENCE   273 AA;  29608 MW;  3104557FAB051A78 CRC64;
     MSNSAIDVPS RGGFSFDLCR RNDMLAKKGV NLPSFRKTGT TIVGLIFQDG VILGADTRAT
     EGPIVCDKNC EKIHYMAPNI YCCGAGTAAD TEAVTDMVSS QLQLHRYHTG RESRVVTALT
     LLKKHLFNYQ GYVQAALVLG GVDCTGPHLH TIYPHGSTDT LPFATMGSGS LAAMAMFESK
     YKEGLTKDEG IQLVVDAICS GIFNDLGSGS NVDVCVITKG HKEYLRNHLL PNPRTFVNAK
     GYSFPKKTEV LLTKITPLRE RVEVVEGGDA MEE
//
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