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