ID A0A1D7YPF0_9ACTN Unreviewed; 588 AA.
AC A0A1D7YPF0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=AAA ATPase forming ring-shaped complexes {ECO:0000256|HAMAP-Rule:MF_02112};
DE Short=ARC {ECO:0000256|HAMAP-Rule:MF_02112};
GN Name=arc {ECO:0000256|HAMAP-Rule:MF_02112};
GN ORFNames=BFF78_33290 {ECO:0000313|EMBL:AOR37473.1};
OS Streptomyces fodineus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR37473.1, ECO:0000313|Proteomes:UP000094960};
RN [1] {ECO:0000313|Proteomes:UP000094960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA Kim M.-K., Kim S.B.;
RT "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer. Assembles into a hexameric ring structure.
CC {ECO:0000256|HAMAP-Rule:MF_02112}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000256|HAMAP-
CC Rule:MF_02112, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; CP017248; AOR37473.1; -; Genomic_DNA.
DR RefSeq; WP_069783961.1; NZ_CP017248.1.
DR AlphaFoldDB; A0A1D7YPF0; -.
DR KEGG; spun:BFF78_33290; -.
DR Proteomes; UP000094960; Chromosome.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis 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 Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR InterPro; IPR041626; Prot_ATP_ID_OB_N.
DR InterPro; IPR022482; Proteasome_ATPase.
DR NCBIfam; TIGR03689; pup_AAA; 1.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR Pfam; PF17758; Prot_ATP_ID_OB_N; 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_02112,
KW ECO:0000256|RuleBase:RU003651};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_02112};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02112,
KW ECO:0000256|RuleBase:RU003651}; Proteasome {ECO:0000313|EMBL:AOR37473.1}.
FT DOMAIN 265..419
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..94
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT BINDING 276..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 588 AA; 65059 MW; 9B7ACCB8AD0BEB1E CRC64;
MAAHDDDMNR GIRPGRGSDD PAGQIAYLEQ EIAVLRRKLA DSPRHTRILE ERIVELQTNL
AGVSAQNERL ANTLREARDQ IVALKEEVDR LAQPPAGFGV FLQANEDGTA DIFTGGRKLR
VNVSPSVDLD DLRRGQEVML NEALNVVEAM EYERVGDIVT LKEILEDGER ALVLGHTDEE
RVVRLAEPLL DVTIRAGDAL LLEPRSGYVY EVVPKSEVEE LVLEEVPDIG YEAIGGLGNQ
IEAIRDAVEL PYLYPDLFKE HELRPPKGVL LYGPPGCGKT LIAKAVANSL AKKVAEVTGQ
AAGKSFFLNI KGPELLNKYV GETERQIRLV FQRAREKASE GTPVIVFFDE MESLFRTRGS
GVSSDVENTI VPQLLAEIDG VEGLENVVVI GASNREDMID PAILRPGRLD VKIKIERPDA
EAAKDIFGKY LTERLPLHAD DLSEHGGDKA TTVQSMIQTA VEQMYAESEE NRFLEVTYAN
GDKEVLYFKD FNSGAMIENI VGRAKKMAIK DFLEKSQKGL RVSHLLQACV DEFKENEDLP
NTTNPDDWAR ISGKKGERIV YIRTLITGKQ GADTGRSIDT VANTGQYL
//