(data stored in ACNUC30630 zone)

SWISSPROT: ARC_BIFAA

ID   ARC_BIFAA               Reviewed;         515 AA.
AC   A1A0U4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   11-DEC-2019, entry version 73.
DE   RecName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000255|HAMAP-Rule:MF_02112};
DE            Short=ARC {ECO:0000255|HAMAP-Rule:MF_02112};
GN   Name=arc {ECO:0000255|HAMAP-Rule:MF_02112}; OrderedLocusNames=BAD_0546;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure.
CC       {ECO:0000255|HAMAP-Rule:MF_02112}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_02112}.
DR   EMBL; AP009256; BAF39327.1; -; Genomic_DNA.
DR   RefSeq; WP_011742988.1; NC_008618.1.
DR   SMR; A1A0U4; -.
DR   EnsemblBacteria; BAF39327; BAF39327; BAD_0546.
DR   GeneID; 4556126; -.
DR   KEGG; bad:BAD_0546; -.
DR   eggNOG; ENOG4105DHM; Bacteria.
DR   eggNOG; COG0464; LUCA.
DR   HOGENOM; HOG000245286; -.
DR   KO; K13527; -.
DR   OMA; CVDEFKE; -.
DR   BioCyc; BADO367928:G1G2R-593-MONOMER; -.
DR   Proteomes; UP000008702; Chromosome.
DR   GO; GO:0000502; C:proteasome complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   HAMAP; MF_02112; ARC_ATPase; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB.
DR   InterPro; IPR041626; Prot_ATP_OB_N.
DR   InterPro; IPR022482; Proteasome_ATPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR   Pfam; PF17758; Prot_ATP_OB_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03689; pup_AAA; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1A0U4.
DR   SWISS-2DPAGE; A1A0U4.
KW   ATP-binding; Coiled coil; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..515
FT                   /note="AAA ATPase forming ring-shaped complexes"
FT                   /id="PRO_0000396963"
FT   NP_BIND         240..245
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
FT   COILED          2..49
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   515 AA;  55781 MW;  E4DD0E81A0F6A054 CRC64;
     MNDHDEETLA SLQQANDQLM AKNHALVKAL SRATQEMTKT KAQLNQLAGP PMTFATMVRV
     HSAKTDGQGV QHASAEVAAG ARRMIVPIAA NLQASRLEPG RTVLLNENMV VVSQLDTDTL
     GAVRSVRQVC DDGRLLVADG GGNVTLVRCS GTLAKQAISA GDRVNVDASL RFALSLVPPE
     NDDDLVLEEV PDVTFADIGG LDEQIERIRD AVQMPFQHRE LFERYDLKPP KGVLLYGPPG
     NGKTLIAKAV ANALAEGTDA GSGVFLSVKG PELLNKFVGE SERLIRMIFK RARERAADGK
     PVIVFIDEMD SLLRTRGTGV SSDVETTIVP QFLTELDGVE SLDNVMVIGA SNRIDMIDPA
     VLRPGRLDVK IRVDRPGIQQ ATQIVRHYLT DKLPLSPNVD AKALIGVLVN DIYAQDEHRH
     LCDICDDHGQ WRPVYLADVV SGAVLKNIVD RAKTYAVKLS ITTGQAAAIG INLLAKAVDE
     EYGETRDALL DADPEQWSRI NGLEPGRVTG IRPVA
//

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