PAN_PYRHO
ID PAN_PYRHO Reviewed; 399 AA.
AC O57940;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=PH0201;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29270.1; -; Genomic_DNA.
DR PIR; G71242; G71242.
DR PDB; 5EQT; X-ray; 1.94 A; A=136-392.
DR PDBsum; 5EQT; -.
DR AlphaFoldDB; O57940; -.
DR SMR; O57940; -.
DR STRING; 70601.3256587; -.
DR EnsemblBacteria; BAA29270; BAA29270; BAA29270.
DR KEGG; pho:PH0201; -.
DR eggNOG; arCOG01306; Archaea.
DR OMA; YNMTTFE; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..399
FT /note="Proteasome-activating nucleotidase"
FT /id="PRO_0000084750"
FT REGION 397..399
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 19..60
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 184..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00553"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:5EQT"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5EQT"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:5EQT"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:5EQT"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:5EQT"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:5EQT"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:5EQT"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:5EQT"
FT TURN 323..326
FT /evidence="ECO:0007829|PDB:5EQT"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:5EQT"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 346..362
FT /evidence="ECO:0007829|PDB:5EQT"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:5EQT"
FT HELIX 383..391
FT /evidence="ECO:0007829|PDB:5EQT"
SQ SEQUENCE 399 AA; 45177 MW; 5D2F62F7F530C42E CRC64;
MSVMSGDEVQ FQGDYDDYIT YLKRRIRQLE LQVRMLEADK ERLERELSRL RSEMSRLRQP
PAFAGTVIEV LDEDRAIVQN YNGPRFVVRI APWIDRKKLR PGTRVALDQR TMAVVEILPT
SKDPTVLGFE VIERPNVTYN DIGGLKKQLQ ELREAIELPL KHPELFEEVG IDPPKGVLLY
GPPGCGKTLM AKALAHEVNA TFIRVVGSEL VRKYIGEGAR LVHELFELAK EKAPTIIFID
EIDAIGAKRM DETTGGEREV NRTLMQLLAE MDGFDPRGNV KVIAATNRPD ILDPALLRPG
RFDRLIEVPL PDFEGRLEIL KVHTRRMKLK GVDLRAIAEM TEGASGADLK AIATEAGMFA
IRERRTYVTQ EDFLKAVDKV LGNERKLLQQ ITSHEVIYG
