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CETZ_PYRFU
ID   CETZ_PYRFU              Reviewed;         366 AA.
AC   Q8U0S7;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Tubulin-like protein CetZ {ECO:0000255|HAMAP-Rule:MF_01946};
GN   Name=cetZ {ECO:0000255|HAMAP-Rule:MF_01946}; Synonyms=ftsZ3;
GN   OrderedLocusNames=PF1507;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Involved in cell shape control. {ECO:0000255|HAMAP-
CC       Rule:MF_01946}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01946}.
CC   -!- SIMILARITY: Belongs to the CetZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01946}.
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DR   EMBL; AE009950; AAL81631.1; -; Genomic_DNA.
DR   RefSeq; WP_011012654.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U0S7; -.
DR   SMR; Q8U0S7; -.
DR   STRING; 186497.PF1507; -.
DR   EnsemblBacteria; AAL81631; AAL81631; PF1507.
DR   GeneID; 41713325; -.
DR   KEGG; pfu:PF1507; -.
DR   PATRIC; fig|186497.12.peg.1570; -.
DR   eggNOG; arCOG02202; Archaea.
DR   HOGENOM; CLU_058152_0_0_2; -.
DR   OMA; LYQANAG; -.
DR   OrthoDB; 23481at2157; -.
DR   PhylomeDB; Q8U0S7; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   HAMAP; MF_01946; CetZ; 1.
DR   InterPro; IPR032907; CetZ.
DR   InterPro; IPR045061; FtsZ/CetZ.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR30314; PTHR30314; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR00423; CELLDVISFTSZ.
DR   SMART; SM00864; Tubulin; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..366
FT                   /note="Tubulin-like protein CetZ"
FT                   /id="PRO_0000114414"
FT   BINDING         10..14
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
FT   BINDING         103..105
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
FT   BINDING         136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
FT   BINDING         163
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
FT   BINDING         181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01946"
SQ   SEQUENCE   366 AA;  40027 MW;  A735B1A91A122BF2 CRC64;
     MRAIIIGIGQ CGTKIADIFS LVDFEALAIN TSRGDLEYLK HIPPDRRILI GESIVGGKGV
     NANPVLGREA MKRDLPMVMK KISSLVGFED VDIFFLTFGF GGGTGAGGTP VLAEALKEEY
     PDSLVVAIGA LPLKEEGIRP TINAAITIDK LSKIVDSIIA IDNNKLKESN EDISQAYERI
     NYAIVERIAS LLALIDVPGE QTLDASDLKF VLRAMGSFAT VGYAKADATK IKSLSRLIIR
     SFENEGLYLD VNIESALYGL VAIHGPPEAL KANEIFEALN ELTQRIRGKQ IFRGFYPDPR
     EREVEVVTLL SGIYESKSIE EIVITAKKYA QEFLKAKEEG ESKKKKLLSG LPDFDDIYPG
     EADDQS
 
 
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