ID M0ATC7_NATA1 Unreviewed; 742 AA.
AC M0ATC7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=ATPase AAA {ECO:0000313|EMBL:ELZ01805.1};
GN ORFNames=C481_09802 {ECO:0000313|EMBL:ELZ01805.1};
OS Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS P-10747 / NBRC 102637 / 172P1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=29540 {ECO:0000313|EMBL:ELZ01805.1, ECO:0000313|Proteomes:UP000011554};
RN [1] {ECO:0000313|EMBL:ELZ01805.1, ECO:0000313|Proteomes:UP000011554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12278 {ECO:0000313|EMBL:ELZ01805.1,
RC ECO:0000313|Proteomes:UP000011554};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SIMILARITY: Belongs to the AAA ATPase family. CDC48 subfamily.
CC {ECO:0000256|ARBA:ARBA00009833}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ01805.1}.
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DR EMBL; AOIO01000023; ELZ01805.1; -; Genomic_DNA.
DR RefSeq; WP_006108995.1; NZ_AOIO01000023.1.
DR AlphaFoldDB; M0ATC7; -.
DR STRING; 29540.C481_09802; -.
DR PATRIC; fig|29540.5.peg.1997; -.
DR eggNOG; arCOG01308; Archaea.
DR OrthoDB; 77269at2157; -.
DR Proteomes; UP000011554; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd19529; RecA-like_VCP_r2; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01243; CDC48; 1.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011554}.
FT DOMAIN 5..89
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 106..178
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 222..358
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 495..632
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 722..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 81862 MW; 5DE99C8224D97095 CRC64;
MNEVQLEVAK AYPNDSGRGI ARLDPDTLLH LKLSPGDIIE IEGADTTAAK VWRADRQDWN
TDTVRIDGFT RQNADVGIGE RVTIRKAEAT KADSLVLAPP EEASVQFGSD AAGMVKRQIL
KRPVVGRDIV PVMSSTNHPF MRSPGQAIPL IAVETEPEGV VLITEDTDVE LREEPISGFE
KTGGGITYED IGGLQSEIQR VREMVELPMK HPQIFKKLGI EPPQGVLLHG PPGTGKTLLA
KAVANETSAS FFSIAGPEII SKYYGESEQQ LREIFEDASE ESPAIIFIDE LDSIAPKRED
VTGEVERRVV AQLLTMMDGL ETRGQVIVIA ATNRVDSVDP ALRRPGRFDR EIEIGVPDET
GREEILQIHT RGMPLSDDVN LSHLADETHG FVGADIESLT KEAAMKALRR YLPEIDLDEE
DIPPSLIDRM IVKRKDFRGA LNEVEPSAMR EVLVELPKIT WDDVGGLHDA KDQVKESVEW
PLNNPERFTR LGIDPPAGVL LYGPPGTGKT LMAKAVANET NANFISVRGP QLLSKWVGES
EKAIRQTFRK ARQVSPTVIF FDELDALAPG RGGETGSNVS ERVVNQLLTE LDGLEDMEDV
MVIGATNRPD MIDPALLRSG RFDRLVMIGE PDIEGRERIL DIHTQETPLA ADVTLREIAE
ITDGYVGSDL ESIAREAAIE ALREDHEANV VEMRHFRQAM ENVRPTITDD ILDYYEQIED
EFRGGSAGPD PTGRRGSRIG FQ
//