(data stored in ACNUC10043 zone)

HOGENOM: IGNAA_1_PE100

ID   IGNAA_1_PE100                        STANDARD;      PRT;   407 AA.
AC   IGNAA_1_PE100; E0SPT1;
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; (IGNAA_1.PE100).
GN   Name=pan; OrderedLocusNames=Igag_0101;
OS   IGNISPHAERA AGGREGANS DSM 17230.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignisphaera.
OX   NCBI_TaxID=583356;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS IGNAA_1.PE100.
CC       Ignisphaera aggregans DSM 17230 chromosome, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:E0SPT1_IGNAA
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; E0SPT1; -.
DR   EMBL; CP002098; ADM26953.1; -; Genomic_DNA.
DR   RefSeq; YP_003858833.1; NC_014471.1.
DR   GeneID; 9715417; -.
DR   GenomeReviews; CP002098_GR; Igag_0101.
DR   KEGG; iag:Igag_0101; -.
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; IGNAA_1.PE100; -.
KW   Proteasome-activating nucleotidase;
KW   ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm;
KW   Hydrolase; Nucleotide-binding; Proteasome.
SQ   SEQUENCE   407 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MASRMALEDS GFIKDVSNIN YEKNLENRVR ELEIELSMLK EIIAKYREEL EYYKSQVEKL
     MAPPLIEATV IEVLDDERAL VKSSSGPTLI VRILETIDKS KLKPGTSVAL NQRGSTIVEI
     LPRSEDPYVQ AFEVIEKPNI SYDDIGGLEQ QIQELREAIE LPLKNPHIFK ILGIEPPKGV
     LLYGPPGCGK TLLAKAIAHE TNATFIRLVA SELAQKFIGE GARIVREVFE LARKKAPSII
     LIDEIDAIAA RRIDVGTSGE REIHRTLTQL LAEMDGFNPL DNVKIIATTN RLDILDPAIL
     RPGRFDKIIE IPLPNTRGRY EILKIHTRKM PLAEDVDLVK IAQITEGATG ADLKAICVEA
     ALKALRENRF IVSMEDFNYA IKKVIKNRYR PYAQILSNNI TAVMMYQ
//

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