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Database: UniProt
Entry: A0A1V4CW28_9ACTN
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ID   A0A1V4CW28_9ACTN        Unreviewed;       255 AA.
AC   A0A1V4CW28;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Proteasome subunit alpha {ECO:0000256|HAMAP-Rule:MF_00289};
DE   AltName: Full=20S proteasome alpha subunit {ECO:0000256|HAMAP-Rule:MF_00289};
DE   AltName: Full=Proteasome core protein PrcA {ECO:0000256|HAMAP-Rule:MF_00289};
GN   Name=prcA {ECO:0000256|HAMAP-Rule:MF_00289};
GN   ORFNames=VT50_0232580 {ECO:0000313|EMBL:OPF71849.1};
OS   Streptomyces antioxidans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF71849.1, ECO:0000313|Proteomes:UP000033615};
RN   [1] {ECO:0000313|EMBL:OPF71849.1, ECO:0000313|Proteomes:UP000033615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC164 {ECO:0000313|Proteomes:UP000033615};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Streptomyces antioxidans MUSC 164.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the proteasome core, a large protease complex
CC       with broad specificity involved in protein degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_00289}.
CC   -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase ARC-20S
CC       proteasome complex, likely via the docking of the C-termini of ARC into
CC       the intersubunit pockets in the alpha-rings, may trigger opening of the
CC       gate for substrate entry. Interconversion between the open-gate and
CC       close-gate conformations leads to a dynamic regulation of the 20S
CC       proteasome proteolysis activity. {ECO:0000256|HAMAP-Rule:MF_00289}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_00289}.
CC   -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 beta
CC       subunits that assemble into four stacked heptameric rings, resulting in
CC       a barrel-shaped structure. The two inner rings, each composed of seven
CC       catalytic beta subunits, are sandwiched by two outer rings, each
CC       composed of seven alpha subunits. The catalytic chamber with the active
CC       sites is on the inside of the barrel. Has a gated structure, the ends
CC       of the cylinder being occluded by the N-termini of the alpha-subunits.
CC       Is capped by the proteasome-associated ATPase, ARC. {ECO:0000256|HAMAP-
CC       Rule:MF_00289}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00289}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|HAMAP-
CC       Rule:MF_00289, ECO:0000256|PROSITE-ProRule:PRU00808}.
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:OPF71849.1}.
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DR   EMBL; LAKD02000118; OPF71849.1; -; Genomic_DNA.
DR   RefSeq; WP_046088108.1; NZ_LAKD02000118.1.
DR   AlphaFoldDB; A0A1V4CW28; -.
DR   OrthoDB; 9775643at2; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000033615; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01906; proteasome_protease_HslV; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_00289_B; Proteasome_A_B; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR022296; Proteasome_asu_bac.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   NCBIfam; TIGR03691; 20S_bact_alpha; 1.
DR   PANTHER; PTHR11599:SF15; PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00289};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP-
KW   Rule:MF_00289}.
FT   REGION          218..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   255 AA;  27941 MW;  73C3F4D0B19D011E CRC64;
     MTTPFYVSPQ QAMADRAEYA RKGIARGRSV VVLQYTDGIV FVAENPSRAL HKVSEIYDRI
     AFAAVGKYNE FENLRIGGVR YADLRGYTYD REDVTARGLA NVYAQTLGTI FSSAAEKPYE
     VELIVAEVGE GPEDDQIYRL PHDGSIVDEH GSVAVGGNAD QISSYLDQRH RDGMTLAEAL
     KLAVDSLSRD NNGGERSLTA EHLEVAVLDR TRPQKRKFKR VLGGQLSRLM EPGEGGADAE
     ASPESPEEPS SDSED
//
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