PRS6A_SOLLC
ID PRS6A_SOLLC Reviewed; 423 AA.
AC P54776;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=26S proteasome regulatory subunit 6A homolog;
DE AltName: Full=LEMA-1;
DE AltName: Full=Mg(2+)-dependent ATPase 1;
DE AltName: Full=Tat-binding protein homolog 1;
DE Short=TBP-1;
GN Name=TBP1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. UC82B; TISSUE=Fruit;
RX PubMed=7766893; DOI=10.1007/bf00020884;
RA Prombona A., Tabler M., Providaki M., Tsagris M.;
RT "Structure and expression of LeMA-1, a tomato protein belonging to the
RT SEC18-PAS1-CDC48-TBP-1 protein family of putative Mg(2+)-dependent
RT ATPases.";
RL Plant Mol. Biol. 27:1109-1118(1995).
CC -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the 26S
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; X74426; CAA52445.1; -; mRNA.
DR PIR; S56672; S56672.
DR AlphaFoldDB; P54776; -.
DR SMR; P54776; -.
DR STRING; 4081.Solyc01g099760.2.1; -.
DR PaxDb; P54776; -.
DR PRIDE; P54776; -.
DR eggNOG; KOG0652; Eukaryota.
DR InParanoid; P54776; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P54776; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1..423
FT /note="26S proteasome regulatory subunit 6A homolog"
FT /id="PRO_0000084705"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 423 AA; 47505 MW; EB2A7390109E65F3 CRC64;
MATPMAEDSN FEDDQLHAMS TEDIIRASRL LDNEIRIIKE ELQRTNLELD SFKEKIKENQ
EKIKLNKQLP YLVGNIVEIL EMNPEEEAEE DGANIDLDSQ RKGKCVVLKT STRQTIFLPV
VGLVDPDNLK PGDLVGVNKD SYLILDTLPS EYDSRVKAME VDEKPTEDYH DIGGLEKQIQ
ELVEAIVLPM THQERFQKLG VRPPKGVLLY GPPGTGKTLM ARACAAQTNA TFLKLAGPQL
VQMFIGDGAK LVRDAFQLAK EKSPCIIFID EIDAIGTKRF DSEVSGDREV QRTMLELLNQ
LDGFSSDDRI KVIAATNRAD ILDPALMRSG RLDRKIEFPH PTEEARARIL QIHSRKMNVN
PDVNFEELAR STDDFNGAQL KAVCVEAGML ALRRDATEVT HEDFNEGIIQ VQAKKKASLN
YYA
