ID A0A2G1WLY1_9EURY Unreviewed; 405 AA.
AC A0A2G1WLY1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=DJ69_03250 {ECO:0000313|EMBL:PHQ40000.1};
OS Halorubrum persicum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1383844 {ECO:0000313|EMBL:PHQ40000.1, ECO:0000313|Proteomes:UP000222824};
RN [1] {ECO:0000313|EMBL:PHQ40000.1, ECO:0000313|Proteomes:UP000222824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C49 {ECO:0000313|EMBL:PHQ40000.1,
RC ECO:0000313|Proteomes:UP000222824};
RX PubMed=24782836; DOI=10.3389/fmicb.2014.00140;
RA Fullmer M.S., Soucy S.M., Swithers K.S., Makkay A.M., Wheeler R.,
RA Ventosa A., Gogarten J.P., Papke R.T.;
RT "Population and genomic analysis of the genus Halorubrum.";
RL Front. Microbiol. 5:140-140(2014).
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:PHQ40000.1}.
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DR EMBL; NHOA01000020; PHQ40000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1WLY1; -.
DR OrthoDB; 77269at2157; -.
DR Proteomes; UP000222824; 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; 1.20.5.170; -; 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 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 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};
KW 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}.
FT DOMAIN 182..321
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 BINDING 193..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
SQ SEQUENCE 405 AA; 45194 MW; 983AE5D6374874FB CRC64;
MTDTVDDVEL PYDEGSASRQ EKIESLQEEL DVLESQNEEM RDKLLDANAE NNKYQQKLER
LTHENKKLKQ SPLFVATVQE ITPDGAVIKQ HGNNQEALTE ITAEMREKLN PDDRVAVNNS
LSVVKKLEKE TDVRARVMQV EHSPDVTYAD IGGLEDQMQE VRETVEMPLE HPDMFEDVGI
QPPSGVLLYG PPGTGKTMLA KAVANETDAT FIKMAGSELV HKFIGEGAKL VRDLFEVARE
NQPAVLFIDE IDAIASKRTD SKTSGDAEVQ RTMMQLLSEM DGFDERGEVR IIAATNRFDM
LDPAILRPGR FDRLIEVPKP NTEGREIIFQ IHTRKMNLAS DIDFTELAEL TPDASGADIK
AICTEAGMFA IRDDRTEVTL DDFLGAHEKL QTDDETGADD SLAFA
//
