ID   PSA6_TOBAC              Reviewed;         246 AA.
AC   Q9XG77;
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-6;
DE   AltName: Full=20S proteasome alpha subunit A;
DE   AltName: Full=20S proteasome subunit alpha-1;
GN   Name=PAA1; Synonyms=PSA1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin 38; TISSUE=Style;
RX   PubMed=10080698; DOI=10.1023/a:1006102110889;
RA   Bahrami A.R., Gray J.E.;
RT   "Expression of a proteasome alpha-type subunit gene during tobacco
RT   development and senescence.";
RL   Plant Mol. Biol. 39:325-333(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 (By
CC       similarity). {ECO:0000250}.
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; Y16644; CAB39975.1; -; mRNA.
DR   RefSeq; NP_001312884.1; NM_001325955.1.
DR   AlphaFoldDB; Q9XG77; -.
DR   SMR; Q9XG77; -.
DR   STRING; 4097.Q9XG77; -.
DR   MEROPS; T01.971; -.
DR   PRIDE; Q9XG77; -.
DR   ProMEX; Q9XG77; -.
DR   GeneID; 107815705; -.
DR   KEGG; nta:107815705; -.
DR   OMA; IDAHLMA; -.
DR   PhylomeDB; Q9XG77; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03754; proteasome_alpha_type_6; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR034642; Proteasome_subunit_alpha6.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..246
FT                   /note="Proteasome subunit alpha type-6"
FT                   /id="PRO_0000124139"
SQ   SEQUENCE   246 AA;  27303 MW;  7152CE4FC6155A64 CRC64;
     MSRGSGGGYD RHITIFSPEG RLFQVEYAFK AVKAAGITSI GVRGKDSVCV VTQKKVPDKL
     LDQTSVSHLF PITKYLGLLA TGMTADARTL VQQARNEAAE FRFKYGYEMP VDVLSKWIAD
     KSQVYTQHAY MRPLGVVAMI LGIDEEKGPQ LFKCDPAGHF FGHKATSAGS KEQEAINFLE
     KKMKNDPAFS YEETVQTAIS ALQSVLQEDF KASEIEVGVV KKEDPIFRVL TTEEIDEHLT
     AISERD