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PSA5_TRYBB
ID   PSA5_TRYBB              Reviewed;         246 AA.
AC   Q9XZG5;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Proteasome subunit alpha type-5;
DE   AltName: Full=20S proteasome subunit alpha-5;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=427;
RX   PubMed=10567215; DOI=10.1042/bj3440349;
RA   Yao Y., Toth C.R., Huang L., Wong M.L., Dias P., Burlingame A.L.,
RA   Coffino P., Wang C.C.;
RT   "Alpha-5 subunit in Trypanosoma brucei proteasome can self-assemble to form
RT   a cylinder of four stacked heptamer rings.";
RL   Biochem. J. 344:349-358(1999).
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   -!- 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; AF140353; AAD31877.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XZG5; -.
DR   SMR; Q9XZG5; -.
DR   OMA; FQVEYAR; -.
DR   BRENDA; 3.4.25.1; 6519.
DR   GO; GO:0005829; C:cytosol; ISA:GeneDB.
DR   GO; GO:0005634; C:nucleus; ISA:GeneDB.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISM:GeneDB.
DR   CDD; cd03753; proteasome_alpha_type_5; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR033812; Proteasome_alpha_type_5.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..246
FT                   /note="Proteasome subunit alpha type-5"
FT                   /id="PRO_0000124123"
SQ   SEQUENCE   246 AA;  27177 MW;  DAA6D211F5350A2C CRC64;
     MFSSKTEYDR GVNTFSPEGR IFQIEYAIEA IKLGSTSLGI QTPDAVIIAA EKRVPSTLVD
     PSSVNKILEI DHHIGTVLSG MVADARILVD HARVEAQNHR FTYDEPMSVE SCALATCDLS
     VQFGESGGRK KLMSRPFGVS LLIAGVDENG PQLWQTDPSG TYTRYDAQAI GGGAEAAQTV
     FSERYHRNMT VEEAENLTVQ ILRQVMEEKL TKTSVEIAIV PVSTGRLQIY DQEQIQRIID
     RQAEEN
 
 
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