ID A0A1C6UE39_9ACTN Unreviewed; 593 AA.
AC A0A1C6UE39;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=GA0070603_1358 {ECO:0000313|EMBL:SCL52234.1};
OS Micromonospora chersina.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL52234.1, ECO:0000313|Proteomes:UP000198605};
RN [1] {ECO:0000313|EMBL:SCL52234.1, ECO:0000313|Proteomes:UP000198605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL52234.1,
RC ECO:0000313|Proteomes:UP000198605};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FMIB01000002; SCL52234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6UE39; -.
DR STRING; 47854.GA0070603_1358; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000198605; 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; 1.10.8.60; -; 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:SCL52234.1}.
FT DOMAIN 270..424
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 11..94
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
FT BINDING 281..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02112"
SQ SEQUENCE 593 AA; 65896 MW; EF563BE26A927679 CRC64;
MARSDDADSR AARWEKEAHD LSTQVAFLQE ELALVRRKLT ESPRHVRQLE ERLAATQAQL
ARLTENNERL VSTLKEARAQ IVTLKEEIDR LAQPPSGYGV FLAKHEDGTV DVFTGGRKLR
VAVSPSLEVD ELRRGQEVLL NDALNIVDAF GYERVGEVVM LKEILAGPEG APGDRALVVS
HSDEERIVHL AETLIGSPIR AGDSLMIEPR SAYAYERIPK SEVEELVLEE VPDVDYTDIG
GLHSQIEQIR DAVELPFLHA DLFREHQLRP PKGILLYGPP GCGKTLIAKA VANSLAKKIA
ERRGEEKHTS FFLNIKGPEL LNKYVGETER HIRLIFQRAR EKAGEGTPVI VFFDEMDSVF
RTRGSGVSSD VENTIVPQLL SEIDGVEGLE NVIVIGASNR EDMIDPAILR PGRLDVKIKI
ERPDAEAAKD IFSKYILSGL PLHPDDLAEH GGDPQATVAA MIDAVVLRMY SETEENRFLE
VTYANGDKEV LYFKDFNSGA MIQNIVDRGK KMAIKEFLTS GRKGLRLQHL LDACVDEFRE
NEDLPNTTNP DDWARISGKK GERIVYIRTL VSGGKGAEAG RSIETASNTG QYL
//