ID PRS2_METTH Reviewed; 372 AA.
AC O27092;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Putative 26S proteasome regulatory subunit homolog MTH_1011;
GN OrderedLocusNames=MTH_1011;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the 26S
CC complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AE000666; AAB85507.1; -; Genomic_DNA.
DR PIR; H69001; H69001.
DR AlphaFoldDB; O27092; -.
DR SMR; O27092; -.
DR STRING; 187420.MTH_1011; -.
DR PaxDb; 187420-MTH_1011; -.
DR EnsemblBacteria; AAB85507; AAB85507; MTH_1011.
DR KEGG; mth:MTH_1011; -.
DR PATRIC; fig|187420.15.peg.994; -.
DR HOGENOM; CLU_000688_21_3_2; -.
DR InParanoid; O27092; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19481; RecA-like_protease; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR000641; CbxX/CfxQ.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23076:SF37; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR PRINTS; PR00819; CBXCFQXSUPER.
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; Nucleotide-binding; Proteasome; Reference proteome.
FT CHAIN 1..372
FT /note="Putative 26S proteasome regulatory subunit homolog
FT MTH_1011"
FT /id="PRO_0000084755"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 372 AA; 42599 MW; 4A6F03002E5745C2 CRC64;
MVKFNNIIYD PQVSDKKFPV QASDPEREAK LVVLQPVGYP FVCNLMEAPR IDAVNKELFE
IYARDQWEGF RAAEGSYLFD QKLLPDYAFK IIRAHPDGSK ITRNTSIILL ENDREEFHEV
RSSITMDDVI GQEDAKIKCR IIMKYLEDPD RFRDWAPRNV LFHGSPGTGK TMLAKSLANE
LKVPLYLIKA TSLIGEHVGD GARQIHELYE LASKTAPSVI FIDEMDAIGL DRRYQSLRGD
VSEVVNALLT EMDGINQNWG VVTIGATNNP ELLDKAIRSR FEEEIEFKLP DDEERKLMLE
KYIETMPLKV DFPVDKLVKL TREMSGRDIK DRVLKTALHR AIAEDSESVR AEHIEYALKE
RKVSGEPKHM FA
//
