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VAT_THEAC
ID   VAT_THEAC               Reviewed;         745 AA.
AC   O05209;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=VCP-like ATPase;
GN   Name=vat; OrderedLocusNames=Ta0840;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=9119075; DOI=10.1016/s0014-5793(97)00138-5;
RA   Pamnani V., Tamura T., Lupas A.N., Peters J., Cejka Z., Ashraf W.,
RA   Baumeister W.;
RT   "Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue
RT   from the archaeon Thermoplasma acidophilum.";
RL   FEBS Lett. 404:263-268(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
RN   [3]
RP   3D-STRUCTURE BY ELECTRON TOMOGRAPHY.
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=10356978; DOI=10.1016/s0014-5793(99)00431-7;
RA   Rockel B., Walz J., Hegerl R., Peters J., Typke D., Baumeister W.;
RT   "Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon
RT   Thermoplasma acidophilum as studied by electron tomography.";
RL   FEBS Lett. 451:27-32(1999).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.;
CC   -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. CDC48 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U78072; AAC45089.1; -; Genomic_DNA.
DR   EMBL; AL445065; CAC11969.1; -; Genomic_DNA.
DR   PIR; T37458; T37458.
DR   RefSeq; WP_010901251.1; NC_002578.1.
DR   PDB; 1CZ4; NMR; -; A=1-183.
DR   PDB; 1CZ5; NMR; -; A=1-183.
DR   PDB; 5G4F; EM; 7.00 A; A/B/C/D/E/P=1-726.
DR   PDB; 5G4G; EM; 7.80 A; A/B/C/D/E/F=6-726.
DR   PDB; 5VC7; EM; 3.90 A; A/C/D/E/F/G=183-745.
DR   PDB; 5VCA; EM; 3.90 A; M/N/O/P/Q/R=183-745.
DR   PDB; 7DBO; X-ray; 1.90 A; A/B=1-91.
DR   PDBsum; 1CZ4; -.
DR   PDBsum; 1CZ5; -.
DR   PDBsum; 5G4F; -.
DR   PDBsum; 5G4G; -.
DR   PDBsum; 5VC7; -.
DR   PDBsum; 5VCA; -.
DR   PDBsum; 7DBO; -.
DR   AlphaFoldDB; O05209; -.
DR   BMRB; O05209; -.
DR   SMR; O05209; -.
DR   STRING; 273075.Ta0840; -.
DR   EnsemblBacteria; CAC11969; CAC11969; CAC11969.
DR   GeneID; 1456383; -.
DR   KEGG; tac:Ta0840; -.
DR   eggNOG; arCOG01308; Archaea.
DR   HOGENOM; CLU_000688_12_2_2; -.
DR   OMA; HACHDIK; -.
DR   OrthoDB; 2808at2157; -.
DR   EvolutionaryTrace; O05209; -.
DR   Proteomes; UP000001024; 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   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; SSF50692; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54585; SSF54585; 1.
DR   TIGRFAMs; TIGR01243; CDC48; 1.
DR   PROSITE; PS00674; AAA; 2.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..745
FT                   /note="VCP-like ATPase"
FT                   /id="PRO_0000084624"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         508..515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   STRAND          4..12
FT                   /evidence="ECO:0007829|PDB:7DBO"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:7DBO"
FT   HELIX           28..34
FT                   /evidence="ECO:0007829|PDB:7DBO"
FT   STRAND          41..56
FT                   /evidence="ECO:0007829|PDB:7DBO"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:7DBO"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:7DBO"
FT   HELIX           71..77
FT                   /evidence="ECO:0007829|PDB:7DBO"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:7DBO"
FT   STRAND          96..103
FT                   /evidence="ECO:0007829|PDB:1CZ4"
FT   TURN            106..109
FT                   /evidence="ECO:0007829|PDB:1CZ5"
FT   HELIX           116..124
FT                   /evidence="ECO:0007829|PDB:1CZ4"
FT   STRAND          149..160
FT                   /evidence="ECO:0007829|PDB:1CZ4"
FT   STRAND          169..172
FT                   /evidence="ECO:0007829|PDB:1CZ4"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:1CZ5"
SQ   SEQUENCE   745 AA;  83139 MW;  B195EB2044FCF1F2 CRC64;
     MESNNGIILR VAEANSTDPG MSRVRLDESS RRLLDAEIGD VVEIEKVRKT VGRVYRARPE
     DENKGIVRID SVMRNNCGAS IGDKVKVRKV RTEIAKKVTL APIIRKDQRL KFGEGIEEYV
     QRALIRRPML EQDNISVPGL TLAGQTGLLF KVVKTLPSKV PVEIGEETKI EIREEPASEV
     LEEVSRISYE DIGGLSEQLG KIREMIELPL KHPELFERLG ITPPKGVILY GPPGTGKTLI
     ARAVANESGA NFLSINGPEI MSKYYGQSEQ KLREIFSKAE ETAPSIIFID EIDSIAPKRE
     EVQGEVERRV VAQLLTLMDG MKERGHVIVI GATNRIDAID PALRRPGRFD REIEIGVPDR
     NGRKEILMIH TRNMPLGMSE EEKNKFLEEM ADYTYGFVGA DLAALVRESA MNALRRYLPE
     IDLDKPIPTE ILEKMVVTED DFKNALKSIE PSSLREVMVE VPNVHWDDIG GLEDVKREIK
     ETVELPLLKP DVFKRLGIRP SKGFLLYGPP GVGKTLLAKA VATESNANFI SIKGPEVLSK
     WVGESEKAIR EIFKKAKQVA PAIVFLDEID SIAPRRGTTS DSGVTERIVN QLLTSLDGIE
     VMNGVVVIGA TNRPDIMDPA LLRAGRFDKL IYIPPPDKEA RLSILKVHTK NMPLAPDVDL
     NDIAQRTEGY VGADLENLCR EAGMNAYREN PDATSVSQKN FLDALKTIRP SVDEEVIKFY
     RTLSETMSKS VSERRKQLQD QGLYL
 
 
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