ID   ACTH_THEVO              Reviewed;         326 AA.
AC   Q97B19;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Archaeal actin homolog;
GN   OrderedLocusNames=TV0640; ORFNames=TVG0633900;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC   -!- FUNCTION: Polymerizes into bundles of filaments. Polymerization
CC       requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the
CC       deoxy form of NTP can also support the polymerization reaction (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thermophilic archaeal actin family.
CC       {ECO:0000305}.
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DR   EMBL; BA000011; BAB59782.1; -; Genomic_DNA.
DR   RefSeq; WP_010916899.1; NC_002689.2.
DR   AlphaFoldDB; Q97B19; -.
DR   SMR; Q97B19; -.
DR   STRING; 273116.14324856; -.
DR   EnsemblBacteria; BAB59782; BAB59782; BAB59782.
DR   GeneID; 1441747; -.
DR   KEGG; tvo:TVG0633900; -.
DR   eggNOG; arCOG03062; Archaea.
DR   HOGENOM; CLU_851534_0_0_2; -.
DR   OMA; TESWGIG; -.
DR   OrthoDB; 68684at2157; -.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd10227; ParM_like; 1.
DR   InterPro; IPR040607; ALP_N.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR042051; ParM-like.
DR   Pfam; PF17989; ALP_N; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding.
FT   CHAIN           1..326
FT                   /note="Archaeal actin homolog"
FT                   /id="PRO_0000285696"
FT   BINDING         10..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         285..288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  34970 MW;  FCAA0C004823B223 CRC64;
     MVVIGLDVGY GDTKVIGIDG KRIIFPSRWA VTETESWGIG GKIPVLSTDG GQTKFIYGRY
     ASGNNIRVPQ GDGRLASKEA FPLIAAALWE SGIHNDGSPV DLVIGSGTPL GTFDLEVKAA
     KEALENKILT VTGPEGEVRQ YNVTRLIMRP QGVGAALYLL NQGIIEQQPG YGVVIDVGSR
     TTDVLTINLM DMEPVVELSF SLQIGVGDAI SNLSRKIAKE TGFVVPFDLA QEALSKPVMF
     RQKQVGGPEV AGPILEDLAN RIIENIRLNL RGEVDRITSL IPVGGGANLI GDRFDEIAPG
     TTVRIKPEDL QFANALGYRD AAERSM