ID   A0A1H9N5B8_9PSEU        Unreviewed;       606 AA.
AC   A0A1H9N5B8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=SAMN04487818_102506 {ECO:0000313|EMBL:SER30835.1};
OS   Actinokineospora terrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=155974 {ECO:0000313|EMBL:SER30835.1, ECO:0000313|Proteomes:UP000199051};
RN   [1] {ECO:0000313|EMBL:SER30835.1, ECO:0000313|Proteomes:UP000199051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44260 {ECO:0000313|EMBL:SER30835.1,
RC   ECO:0000313|Proteomes:UP000199051};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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; FOGI01000002; SER30835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9N5B8; -.
DR   STRING; 155974.SAMN04487818_102506; -.
DR   Proteomes; UP000199051; Unassembled WGS sequence.
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; 1.20.5.170; -; 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:SER30835.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199051}.
FT   DOMAIN          281..438
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          57..98
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT   BINDING         292..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ   SEQUENCE   606 AA;  67218 MW;  05BC8CF87DAD0685 CRC64;
     MQHDRPGSRP ENADGEHGGV VDPGRERPEV SEAAQIRFLE EEVALLRRKL TESPRHSRLL
     EQRLAEATER VNQLTERNTK LVDTLREARS QLLALREEVD RLAQPPSGYG VFLVGHDDGT
     VDVFTAGRRM RVSVSPAVDG AALRRGQSVR LNEALTVVEG GGFERTGEVS TLRELLVADG
     EEVATRALVV GHADEERVVW LADPLTEAPL KAGDSLLVDG KSGYAYERVP KAEVEDLVLE
     EVPDVDYTDI GGLFRQIEQI RDAVELPFLH KDLFAEYELR PPKGVLLYGP PGCGKTLIAK
     AVANSLAKKV AAARGDHAPK DAKSYFLNIK GPELLNKFVG ETERHIRLIF QRAREKASEG
     TPVIVFFDEM DSIFRTRGSG VSSDVETTIV PQLLSEIDGV EGLENVIVIG ASNREDMIDP
     AILRPGRLDV KIKIERPDAE AARDIFSKYL TTNLPIHADD LAEFGGDKRV CIDAMIQHTV
     ERMYEETEDN RFLEVTYANG DKEVLYFRDF NSGAMIQNIV DRAKKAAIKS VLETRQAGLR
     VQHLLDAIVD EFAENEDLPN TTNPDDWARI SGKKGERIVY IRTLVTGKNQ ESGRAIDTAT
     NTGQYL
//