PAN_PYRFU
ID PAN_PYRFU Reviewed; 396 AA.
AC Q8U4H3;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Proteasome-activating nucleotidase {ECO:0000255|HAMAP-Rule:MF_00553};
DE Short=PAN {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasomal ATPase {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory ATPase {ECO:0000255|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory particle {ECO:0000255|HAMAP-Rule:MF_00553};
GN Name=pan {ECO:0000255|HAMAP-Rule:MF_00553}; OrderedLocusNames=PF0115;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: ATPase which is responsible for recognizing, binding,
CC unfolding and translocation of substrate proteins into the archaeal 20S
CC proteasome core particle. Is essential for opening the gate of the 20S
CC proteasome via an interaction with its C-terminus, thereby allowing
CC substrate entry and access to the site of proteolysis. Thus, the C-
CC termini of the proteasomal ATPase function like a 'key in a lock' to
CC induce gate opening and therefore regulate proteolysis. Unfolding
CC activity requires energy from ATP hydrolysis, whereas ATP binding alone
CC promotes ATPase-20S proteasome association which triggers gate opening,
CC and supports translocation of unfolded substrates. {ECO:0000255|HAMAP-
CC Rule:MF_00553}.
CC -!- SUBUNIT: Homohexamer. The hexameric complex has a two-ring architecture
CC resembling a top hat that caps the 20S proteasome core at one or both
CC ends. Upon ATP-binding, the C-terminus of PAN interacts with the alpha-
CC rings of the proteasome core by binding to the intersubunit pockets.
CC {ECO:0000255|HAMAP-Rule:MF_00553}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00553}.
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 the
CC AAA type. {ECO:0000255|HAMAP-Rule:MF_00553}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00553}.
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DR EMBL; AE009950; AAL80239.1; -; Genomic_DNA.
DR RefSeq; WP_011011227.1; NZ_CP023154.1.
DR PDB; 3WHK; X-ray; 2.60 A; A/B/C/D/E/F/G/H=125-309.
DR PDB; 3WHL; X-ray; 4.00 A; A/C/E/G=125-309.
DR PDBsum; 3WHK; -.
DR PDBsum; 3WHL; -.
DR AlphaFoldDB; Q8U4H3; -.
DR SMR; Q8U4H3; -.
DR STRING; 186497.PF0115; -.
DR PRIDE; Q8U4H3; -.
DR EnsemblBacteria; AAL80239; AAL80239; PF0115.
DR GeneID; 41711902; -.
DR KEGG; pfu:PF0115; -.
DR PATRIC; fig|186497.12.peg.119; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_0_2; -.
DR OMA; YNMTTFE; -.
DR OrthoDB; 30571at2157; -.
DR PhylomeDB; Q8U4H3; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0022623; C:proteasome-activating nucleotidase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00553; PAN; 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; IPR023501; Nucleotidase_PAN.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Nucleotide-binding; Proteasome; Reference proteome.
FT CHAIN 1..396
FT /note="Proteasome-activating nucleotidase"
FT /id="PRO_0000084749"
FT REGION 394..396
FT /note="Docks into pockets in the proteasome alpha-ring to
FT cause gate opening"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT COILED 16..57
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 181..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:3WHK"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:3WHK"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:3WHK"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:3WHK"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:3WHK"
FT STRAND 275..284
FT /evidence="ECO:0007829|PDB:3WHK"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:3WHK"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:3WHK"
SQ SEQUENCE 396 AA; 44805 MW; 791B3666AB853F96 CRC64;
MSEDEAQFHG NYDDYVTYLK RRIRQLELQV RMLEADKERL ERELSRLRSE MSRLRQPPAF
AGSVIEVLDD DRAIVQNYNG PRFVVRIAPW IDKSKLRPGT RVALDQRTMA IIEILPASKD
PAVLGFEVVE RPNVTYNDIG GLKKQLQELR EAIELPLKHP ELFEEVGIDP PKGVLLYGPP
GCGKTLMAKA IAHEVNATFI RVVGSELVRK YIGEGARLVH ELFELAKEKA PTIIFIDEID
AIGAKRLDET TGGEREVNRT LMQLLAEMDG FDPRGNVKVI AATNRPDILD PALLRPGRFD
RLIEVPLPDF EGRLEILKVH TRRMKLRGVD LRLIAELTEG ASGADLKAIA TEAGMFAIRE
RRTYVTQEDF LKAIDKVLGN EKKIIQQIMS HEVIYG
