ID   SAV_SULAC               Reviewed;         780 AA.
AC   Q07590; Q4JAH4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Protein SAV;
GN   Name=sav; OrderedLocusNames=Saci_0838;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=8289263; DOI=10.1016/s0022-2836(05)80047-6;
RA   Confalonieri F., Marsault J., Duguet M.;
RT   "SAV, an archaebacterial gene with extensive homology to a family of highly
RT   conserved eukaryotic ATPases.";
RL   J. Mol. Biol. 235:396-401(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Not yet known, shows ATPase activity.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. CDC48 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY80205.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L17042; AAA72002.1; -; Unassigned_DNA.
DR   EMBL; CP000077; AAY80205.1; ALT_INIT; Genomic_DNA.
DR   PIR; S43859; S43859.
DR   AlphaFoldDB; Q07590; -.
DR   SMR; Q07590; -.
DR   STRING; 330779.Saci_0838; -.
DR   PRIDE; Q07590; -.
DR   EnsemblBacteria; AAY80205; AAY80205; Saci_0838.
DR   KEGG; sai:Saci_0838; -.
DR   PATRIC; fig|330779.12.peg.802; -.
DR   eggNOG; arCOG01308; Archaea.
DR   HOGENOM; CLU_000688_12_2_2; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 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   InterPro; IPR015415; Vps4_C.
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   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 1.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54585; SSF54585; 1.
DR   TIGRFAMs; TIGR01243; CDC48; 1.
DR   PROSITE; PS00674; AAA; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..780
FT                   /note="Protein SAV"
FT                   /id="PRO_0000084623"
FT   BINDING         253..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         528..535
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        267
FT                   /note="A -> R (in Ref. 1; AAA72002)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   780 AA;  87396 MW;  669F1AE15D05E45E CRC64;
     MRINILRVEY HSKTAHSILL QLDLFKKVKV ICHMSQSIKF RVTEARQRDV GKKVARISET
     SMRKLNVEAG DYIEIIGQDG NSALAQVMPA YDISDDEIRI DGYIRKSIKV GIGDDVTVRK
     TNVSPASKVV LAPTQPIRFD NSFVEYVKDT LMDKPLAKGE TLPIPIYTGT LELTVVNTQP
     SNYVYVTGST NIEIREEPVK ESSLAYPKVS WEDIGDLEEA KQKIREIVEW PMRHPELFQR
     LGIDPPKGIL LYGPPGTGKT LLARALANEI GAYFITVNGP EIMSKFYGES EQRIREIFKE
     AEENAPSIIF IDEIDAIAPK REDVTGEVEK RVVAQLLTLM DGIKGRGRVI VIGATNRPDA
     IDPALRRPGR FDREIEIRPP DTKGRKDILQ VHTRNMPITD DVDLDKLAEM TYGYTGADLA
     ALAKEAAIYA LRRFVDEKKL NLDQPTIPAE IIKELKVSMN DFLNALKSIQ PSLLREVYVE
     VPKVNWNDIG GLDNVKQQLR EAVEWPLRFP ELFTKSGVTP PKGILLFGPP GTGKTMLAKA
     VATESGANFI AVRGPEILSK WVGESEKAIR EIFRKARQAA PTVIFFDEID SIAPIRGLST
     DSGVTERIVN QLLAEMDGIV PLNKVVIIAA TNRPDILDPA LLRPGRFDRL IYVPPPDKTA
     RFEILKVHTK NVPLAEDVSL EDIAEKAEGY TGADLEALVR EATINAMRSI YSMCDKQSRD
     ECKGNMECYQ KHIKECMNKT SFKVSKEDFE KALNVVKASL TQADIQRYER FSKELKRAIA