ID A0A3N6LJX2_9EURY Unreviewed; 410 AA.
AC A0A3N6LJX2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ORFNames=EA462_11890 {ECO:0000313|EMBL:RQG89073.1};
OS Natrarchaeobius halalkaliphilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrarchaeobius.
OX NCBI_TaxID=1679091 {ECO:0000313|EMBL:RQG89073.1, ECO:0000313|Proteomes:UP000273828};
RN [1] {ECO:0000313|EMBL:RQG89073.1, ECO:0000313|Proteomes:UP000273828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArcht-Sl {ECO:0000313|EMBL:RQG89073.1,
RC ECO:0000313|Proteomes:UP000273828};
RA Sorokin D.Y., Elcheninov A.G., Kostrikina N.A., Bale N.J.,
RA Sinninghe Damste J.S., Khijniak T.V., Kublanov I.V., Toshchakov S.V.;
RT "Natrarchaeobius chitinivorans gen. nov., sp. nov., and Natrarchaeobius
RT haloalkaliphilus sp. nov., alkaliphilic, chitin-utilizing haloarchaea from
RT hypersaline alkaline lakes.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQG89073.1}.
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DR EMBL; REFY01000004; RQG89073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6LJX2; -.
DR OrthoDB; 77269at2157; -.
DR Proteomes; UP000273828; Unassembled WGS sequence.
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:SF140; PROTEASOME-ACTIVATING NUCLEOTIDASE 1; 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|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00553};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_00553}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00553};
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:UP000273828}.
FT DOMAIN 185..324
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..73
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 196..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
SQ SEQUENCE 410 AA; 46090 MW; FDD814669ED506D9 CRC64;
MSRSPSLPDR PHREIDPDLP DDERFEALRG HFADLVDVHE QLEGQLEDAE NRRQRLQERV
DRVERENETL KSSSLYIATV EDVIDDGEVV VKQHGNNQEV LTEVSPRMAE RVTAGDRVAV
NDSFAIQTVL EAETDARAQS MEITERPSVG YEDIGGIDEQ IREVREAVEQ PLIEPELFEE
VGIDPPSGVL LYGPPGTGKT MLAKAVANKT DATFIKMAGS ELVRKFIGEG SRLVRDLFEM
AREREPAIIF IDEIDAIAAT RTESKTSGDA EVQRTMMQLL AEMDGFEARG EIRIIAATNR
FDMLDRAILR PGRFDRLIEV PEPNRDGREQ IFEIHTRGMN VTDDVDFDTL ADDTEGYSGA
DIESLATEAG MFAIRNEREE IRHQDFLDAV EKVENDDSSD VVSSAGYFYQ
//
