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Database: UniProt
Entry: A0A256IB11_9EURY
LinkDB: A0A256IB11_9EURY
Original site: A0A256IB11_9EURY 
ID   A0A256IB11_9EURY        Unreviewed;       407 AA.
AC   A0A256IB11;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=DJ70_15410 {ECO:0000313|EMBL:OYR53744.1};
OS   Halorubrum halodurans.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=1383851 {ECO:0000313|EMBL:OYR53744.1, ECO:0000313|Proteomes:UP000216308};
RN   [1] {ECO:0000313|EMBL:OYR53744.1, ECO:0000313|Proteomes:UP000216308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cb34 {ECO:0000313|EMBL:OYR53744.1,
RC   ECO:0000313|Proteomes:UP000216308};
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:OYR53744.1}.
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DR   EMBL; NHPJ01000136; OYR53744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256IB11; -.
DR   OrthoDB; 77269at2157; -.
DR   Proteomes; UP000216308; 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   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:UP000216308}.
FT   DOMAIN          184..323
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          32..73
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT   BINDING         195..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT   BINDING         334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
SQ   SEQUENCE   407 AA;  45403 MW;  24AF548B02EFF2DE CRC64;
     MSHSPSLPDR PRLELDPEMS EAERLEAIRQ HYRRIVHVND ELENRLEDAQ GRRGDLKADV
     DELKRENEVL KTSSLYIASV EELTDEGVVI KQHGNNQEVL TQAATRLDAD LRPGDRVAIN
     DSFAIQQVLD DETDSRAQAM EVTESPDVEY ADIGGIDEQI REVREAVEDP LENPEQFETV
     GVEPPSGVLL HGPPGTGKTM LAKAVANESD ATFIKMAGSE LVRKFIGEGS RLVRDLFELA
     AEREPAVIFI DEIDAVASKR TDSKTSGDAE VQRTMMQLLS EMDGFDERGE IRIIAATNRF
     DMLDEAILRP GRFDRLIEVP EPDAEGRERI LEIHTQEMNV ADDVDVSEVA TDLEGYSGAD
     IASVATEAGM FAIRDGRTEV VQSDFERARE KLKDVEGADD QVIHYQY
//
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