(data stored in SCRATCH zone)

SWISSPROT: D5E9I3_METMS

ID   D5E9I3_METMS            Unreviewed;       429 AA.
AC   D5E9I3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 53.
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=Mmah_0302 {ECO:0000313|EMBL:ADE35834.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35834.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35834.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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. {ECO:0000256|HAMAP-
CC       Rule:MF_00553, ECO:0000256|RuleBase:RU003651}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001994; ADE35834.1; -; Genomic_DNA.
DR   RefSeq; WP_013036777.1; NC_014002.1.
DR   EnsemblBacteria; ADE35834; ADE35834; Mmah_0302.
DR   GeneID; 8982435; -.
DR   KEGG; mmh:Mmah_0302; -.
DR   eggNOG; arCOG01306; Archaea.
DR   eggNOG; COG1222; LUCA.
DR   HOGENOM; HOG000225143; -.
DR   KO; K03420; -.
DR   OMA; ARCKLRY; -.
DR   OrthoDB; 30571at2157; -.
DR   BioCyc; MMAH547558:G1GHT-298-MONOMER; -.
DR   Proteomes; UP000001059; 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:ATPase 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   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; IPR023501; Nucleotidase_PAN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB.
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   3: Inferred from homology;
DR   PRODOM; D5E9I3.
DR   SWISS-2DPAGE; D5E9I3.
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:ADE35834.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00553,
KW   ECO:0000256|RuleBase:RU003651};
KW   Proteasome {ECO:0000256|HAMAP-Rule:MF_00553, ECO:0000313|EMBL:ADE35834.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          204..343
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NP_BIND         215..220
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT   COILED          36..91
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
FT   BINDING         354
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00553"
SQ   SEQUENCE   429 AA;  47955 MW;  9961E26A1117367B CRC64;
     MNETSDDTLN QGNYGLKNMS DIEYDYMGSE GDEDFSKYLL DRMKQLESRN SKLKEQCDQI
     ESEKKYVESQ KVKYEREVRK LRSEINRLKT VPLIVANIID VIDSNKVLIR SSSGPQFMVG
     VSQYIDDSRL VAGVRVALNQ QTLSIVDVLP STEEPEVSAM EVLESQDISY EDIGGLDNQI
     QDIIECVELP LIKPESFERV GVEPPKGVLL HGPPGTGKTM MAKAVAHRTD ATFIRVVGSE
     LVQKYIGEGS RLVREVFDMA RKKAPSIIFI DELDAIAATR LSDTNGADRE VQRTLMQLLA
     EMDGFENRGD IRIIAATNRV DILDPAIIRP GRFDRMVEVP MPDTESRSLI LRIHSRGLSL
     ALDVDFDKLA TLTENTSGAD LHALTTEAGM FAVRNDRDSV TMADFMAAID KVLKPRQPQV
     NEHPASMFV
//

If you have problems or comments...

PBIL Back to PBIL home page