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Proteasome subunit beta type (EC 3.4.25.1)

 F9WAG4_TRYCI            Unreviewed;       205 AA.
F9WAG4;
19-OCT-2011, integrated into UniProtKB/TrEMBL.
19-OCT-2011, sequence version 1.
28-MAR-2018, entry version 35.
RecName: Full=Proteasome subunit beta type {ECO:0000256|RuleBase:RU004203};
EC=3.4.25.1 {ECO:0000256|RuleBase:RU004203};
ORFNames=TCIL3000_0_00860 {ECO:0000313|EMBL:CCD15804.1},
TCIL3000_0_05230 {ECO:0000313|EMBL:CCD14226.1};
Trypanosoma congolense (strain IL3000).
Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
Nannomonas.
NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCD14226.1, ECO:0000313|Proteomes:UP000000702};
[1] {ECO:0000313|Proteomes:UP000000702}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IL3000 {ECO:0000313|Proteomes:UP000000702};
Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J.,
Aslett M., Brown R., Corton N., Harris D., Hauser H., Gamble J.,
Gilderthorp R., McQuillan J., Quail M.A., Sanders M., Van Tonder A.,
Ginger M.L., Donelson J.E., Field M.C., Barry J.D., Berriman M.,
Hertz-Fowler C.;
"Divergent evolution of antigenic variation in African trypanosomes.";
Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IL3000;
Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J.,
Aslett M., Brown R., Corton N., Harris D., Hauser H., Gamble J.,
Gilderthorp R., McQuillan J., Quail M.A., Sanders M., van Tonder A.,
Ginger M.L., Donelson J.E., Field M.C., Barry J.D., Berriman M.,
Hertz-Fowler C.;
"Divergent evolution of antigenic variation in African trypanosomes.";
Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:CCD14226.1, ECO:0000313|Proteomes:UP000000702}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IL3000 {ECO:0000313|EMBL:CCD14226.1,
ECO:0000313|Proteomes:UP000000702};
PubMed=22331916; DOI=10.1073/pnas.1117313109;
Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H.,
Gamble J., Gilderthorp R., Marcello L., McQuillan J., Otto T.D.,
Quail M.A., Sanders M.J., van Tonder A., Ginger M.L., Field M.C.,
Barry J.D., Hertz-Fowler C., Berriman M.;
"Antigenic diversity is generated by distinct evolutionary mechanisms
in African trypanosome species.";
Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
-!- FUNCTION: The proteasome is a multicatalytic proteinase complex
which is characterized by its ability to cleave peptides with Arg,
Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
slightly basic pH. {ECO:0000256|RuleBase:RU004203}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000256|RuleBase:RU004203}.
-!- SUBUNIT: The 20S proteasome core is composed of 28 subunits that
are arranged in four stacked rings, resulting in a barrel-shaped
structure. The two end rings are each formed by seven alpha
subunits, and the two central rings are each formed by seven beta
subunits. {ECO:0000256|RuleBase:RU004203}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
Nucleus {ECO:0000256|RuleBase:RU004203,
ECO:0000256|SAAS:SAAS00551005}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000256|RuleBase:RU004203}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:CCD14226.1}.
-----------------------------------------------------------------------
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EMBL; CAEQ01001432; CCD14226.1; -; Genomic_DNA.
EMBL; CAEQ01002062; CCD15804.1; -; Genomic_DNA.
MEROPS; T01.983; -.
Proteomes; UP000000702; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:InterPro.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
CDD; cd03759; proteasome_beta_type_3; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR033811; Proteasome_beta_3.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF62; PTHR11599:SF62; 1.
Pfam; PF00227; Proteasome; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000000702};
Cytoplasm {ECO:0000256|RuleBase:RU004203};
Hydrolase {ECO:0000256|RuleBase:RU004203};
Nucleus {ECO:0000256|RuleBase:RU004203,
ECO:0000256|SAAS:SAAS00039288};
Protease {ECO:0000256|RuleBase:RU004203};
Proteasome {ECO:0000256|RuleBase:RU004203};
Reference proteome {ECO:0000313|Proteomes:UP000000702};
Threonine protease {ECO:0000256|RuleBase:RU004203}.
SEQUENCE 205 AA; 22457 MW; 599B5B33588C923F CRC64;
MSILTYSGGS CLAMAGKECF VIISDNRLGE GLKTISMDVP KLHVINDGIV MGLTGLRTDQ
QTFAQKVRFR TEMYKLREER EINGKAFAAL VASMLYEARF GPWFVEPVIG TIDRKTGEVY
LCATDLIGAP CEPEDYVCAG TCAESLHGMC EALWRPGLEA EELFEIAAQA MLSACDRDSL
SGYGAVAAIV TKDKLITRLI RGRKD


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