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Database: UniProt
Entry: A0A061F3T0_THECC
LinkDB: A0A061F3T0_THECC
Original site: A0A061F3T0_THECC 
ID   A0A061F3T0_THECC        Unreviewed;       245 AA.
AC   A0A061F3T0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|PIRNR:PIRNR001213};
GN   ORFNames=TCM_026771 {ECO:0000313|EMBL:EOY11666.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY11666.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY11666.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- FUNCTION: Non-catalytic component of the proteasome.
CC       {ECO:0000256|PIRNR:PIRNR001213}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR001213}.
CC       Nucleus {ECO:0000256|PIRNR:PIRNR001213}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family.
CC       {ECO:0000256|PIRNR:PIRNR001213}.
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DR   EMBL; CM001883; EOY11666.1; -; Genomic_DNA.
DR   RefSeq; XP_017977172.1; XM_018121683.1.
DR   AlphaFoldDB; A0A061F3T0; -.
DR   SMR; A0A061F3T0; -.
DR   STRING; 3641.A0A061F3T0; -.
DR   EnsemblPlants; EOY11666; EOY11666; TCM_026771.
DR   EnsemblPlants; Tc05v2_t026900.1; Tc05v2_p026900.1; Tc05v2_g026900.
DR   GeneID; 18600579; -.
DR   Gramene; EOY11666; EOY11666; TCM_026771.
DR   Gramene; Tc05v2_t026900.1; Tc05v2_p026900.1; Tc05v2_g026900.
DR   KEGG; tcc:18600579; -.
DR   eggNOG; KOG0185; Eukaryota.
DR   HOGENOM; CLU_072435_0_1_1; -.
DR   InParanoid; A0A061F3T0; -.
DR   OMA; KGYGTQT; -.
DR   OrthoDB; 116867at2759; -.
DR   Proteomes; UP000026915; Chromosome 5.
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; cd03760; proteasome_beta_type_4; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR016295; Proteasome_beta4.
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:SF5; PROTEASOME SUBUNIT BETA TYPE-4; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PIRSF; PIRSF001213; Psome_endopept_beta; 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|PIRNR:PIRNR001213};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR001213};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PIRNR:PIRNR001213};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915}.
SQ   SEQUENCE   245 AA;  27677 MW;  62A66CA000D83FA0 CRC64;
     MNFMDSKQPE SGLLGPESDS QRTLYPYVTG TSVVALKYKD GILMAADMGG SYGSTLRYKS
     VERMKPIGKH SLLGASGEIS DFQEILRFLD ELILYDNMWD DGNSLGPKEV HNYLTRVMYN
     RRNKFNPLWN SLVLGGVKNG QKYLGTVSMI GVNFEDNHVA TGFGNHLARP ILRQEWHENL
     SFEDGVKLLE KCMRVLLYRD RSAVNKLQIA KITEEGMTIS QPYSLKTHWE LSAFQNPTQG
     AVGSW
//
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