(data stored in ACNUC10043 zone)

HOGENOM: METPS_1_PE1002

ID   METPS_1_PE1002                       STANDARD;      PRT;   412 AA.
AC   METPS_1_PE1002; D1YXA2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Proteasome-activating nucleotidase; Short=PAN;AltName:
DE   Full=Proteasomal ATPase;AltName: Full=Proteasome regulatory
DE   ATPase;AltName: Full=Proteasome regulatory particle; (METPS_1.PE1002).
GN   Name=pan-2; Synonyms=pan; OrderedLocusNames=MCP_1002;
OS   METHANOCELLA PALUDICOLA SANAE.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanocellales;
OC   Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS METPS_1.PE1002.
CC       Methanocella paludicola SANAE chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D1YXA2_METPS
CC   -!- FUNCTION: ATPase which is responsible for recognizing, binding,
CC       unfolding and translocation of substrate proteins into the
CC       archaeal 20S proteasome core particle. Is essential for opening
CC       the gate of the 20S proteasome via an interaction with its C-
CC       terminus, thereby allowing substrate entry and access to the site
CC       of proteolysis. Thus, the C-termini of the proteasomal ATPase
CC       function like a 'key in a lock' to induce gate opening and
CC       therefore regulate proteolysis. Unfolding activity requires energy
CC       from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S
CC       proteasome association which triggers gate opening, and supports
CC       translocation of unfolded substrates (By similarity).
CC   -!- SUBUNIT: Homohexamer. The hexameric complex has a two-ring
CC       architecture resembling a top hat that caps the 20S proteasome
CC       core at one or both ends. Upon ATP-binding, the C-terminus of PAN
CC       interacts with the alpha-rings of the proteasome core by binding
CC       to the intersubunit pockets (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil
CC       domain that may assist in substrate recognition, an interdomain
CC       involved in PAN hexamerization, and a C-terminal ATPase domain of
CC       the AAA type (By similarity).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC   -!- GENE_FAMILY: HOG000225143 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D1YXA2; -.
DR   EMBL; AP011532; BAI61074.1; -; Genomic_DNA.
DR   RefSeq; YP_003356057.1; NC_013665.1.
DR   ProteinModelPortal; D1YXA2; -.
DR   GeneID; 8681025; -.
DR   GenomeReviews; AP011532_GR; MCP_1002.
DR   KEGG; mpd:MCP_1002; -.
DR   OMA; ISMPDED; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0022623; C:proteasome-activating nucleotidase complex; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:HAMAP.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:HAMAP.
DR   GO; GO:0043335; P:protein unfolding; IEA:HAMAP.
DR   HAMAP; MF_00553; PAN; 1; -.
DR   InterPro; IPR005937; 26S_Psome_P45.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR023501; Nucleotidase_PAN.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   HOGENOMDNA; METPS_1.PE1002; -.
KW   proteasome-activating nucleotidase;
KW   ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Proteasome.
SQ   SEQUENCE   412 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADGSGVDIQ EDVPVSDFSK YLLDRVRQLE ERNVRLKEEY RKIELEKKSV ENKKVQYERE
     NRKLTAELDR LKTPPLLVGT VVDVMANNKL VIKSSSGPKF VVNSSQFINS KDIFPGAKVA
     LNQQSLAVIE VLPPVKDPMV LGMEVIEAPN IDYQNIGGLE DQINEIKETV ELPLLKPELF
     EKVGIQPPKG VLLYGPPGTG KTLLAKAVAH STKASFIRII GSELVQKYIG EGARMVRELF
     ELAKEKSPSI IFIDEIDSIG AKRLDSITSG DREVQRTLVQ LLAEMDGFDP RGNVRILAAT
     NRPDILDPAL LRPGRFDRII KVPMPNAEAR TEILKIHARR MNLADDVNLK KIGQMTDDTS
     GADLSAIVME AGMFAIRGNR DIVTNDDFTQ AMQKVLGERN KNLTEMNMTV FA
//

If you have problems or comments...

PBIL Back to PBIL home page