ID A8AA17_IGNH4 Unreviewed; 400 AA.
AC A8AA17;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Proteasome-activating nucleotidase {ECO:0000256|HAMAP-Rule:MF_00553};
DE Short=PAN {ECO:0000256|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasomal ATPase {ECO:0000256|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory ATPase {ECO:0000256|HAMAP-Rule:MF_00553};
DE AltName: Full=Proteasome regulatory particle {ECO:0000256|HAMAP-Rule:MF_00553};
GN Name=pan {ECO:0000256|HAMAP-Rule:MF_00553};
GN OrderedLocusNames=Igni_0587 {ECO:0000313|EMBL:ABU81769.1};
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591 {ECO:0000313|EMBL:ABU81769.1, ECO:0000313|Proteomes:UP000000262};
RN [1] {ECO:0000313|EMBL:ABU81769.1, ECO:0000313|Proteomes:UP000000262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125
RC {ECO:0000313|Proteomes:UP000000262};
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H.Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(2008).
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:0000256|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:0000256|HAMAP-Rule:MF_00553}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00553}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|HAMAP-Rule:MF_00553,
CC ECO:0000256|RuleBase:RU003651}.
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DR EMBL; CP000816; ABU81769.1; -; Genomic_DNA.
DR AlphaFoldDB; A8AA17; -.
DR STRING; 453591.Igni_0587; -.
DR KEGG; iho:Igni_0587; -.
DR eggNOG; arCOG01306; Archaea.
DR HOGENOM; CLU_000688_2_0_2; -.
DR OrthoDB; 77269at2157; -.
DR PhylomeDB; A8AA17; -.
DR Proteomes; UP000000262; 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:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00553; PAN; 1.
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_2nd.
DR NCBIfam; TIGR01242; proteasome-activating nucleotidase; 1.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF155; 26S PROTEASOME REGULATORY SUBUNIT 10B; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00553,
KW ECO:0000256|RuleBase:RU003651};
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00553};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00553};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00553};
KW Hydrolase {ECO:0000313|EMBL:ABU81769.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00553,
KW ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP-
KW Rule:MF_00553}; Reference proteome {ECO:0000313|Proteomes:UP000000262}.
FT DOMAIN 168..307
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 21..48
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 179..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
SQ SEQUENCE 400 AA; 44261 MW; B6BF2DB49CBE39C6 CRC64;
MVAFDIDRKF GGEESDDVED VELLKRKINR LTKEVKRLKS ELEYWKGEVN KLTNPPLIEA
TLLDVLPDGR AVVKSSAGPV LVVEVSSRVP KELLKPGISV AVNQRGSTVV DVLKGLEDPY
VKAMEVVERP KTRYSDVGGL KQQLEEVREV VELPLKNPEM FKEIGIEPLK GVLLYGPPGC
GKTLIARAVA GEVGATFIRV VGSELVNKFI GEGARIVREV FNMARKKAPS IIFIDEIDAI
AAKRIEMGTS GEREVQRTLM QLLAELDGFD PLSGVAVIAA TNRLDILDPA ILRPGRFDRI
IYIPPPDKKG RLEILQIHTR NMRMADDVDL EKIAEMTEGA TGADLKAIVT EAGYNALRNK
RKYVTMEDFL AAVDKVMRKR AGASYRLSPR EGAPIQIHTM
//
