CETZ_PYRHO
ID CETZ_PYRHO Reviewed; 365 AA.
AC O59060;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=PH1335;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30441.1; -; Genomic_DNA.
DR PIR; A71005; A71005.
DR RefSeq; WP_010885424.1; NC_000961.1.
DR AlphaFoldDB; O59060; -.
DR SMR; O59060; -.
DR STRING; 70601.3257758; -.
DR EnsemblBacteria; BAA30441; BAA30441; BAA30441.
DR GeneID; 1443661; -.
DR KEGG; pho:PH1335; -.
DR eggNOG; arCOG02202; Archaea.
DR OMA; LYQANAG; -.
DR OrthoDB; 23481at2157; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..365
FT /note="Tubulin-like protein CetZ"
FT /id="PRO_0000114415"
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 365 AA; 40118 MW; DC987E91C761F5B2 CRC64;
MRAIIIGIGQ CGTKIADIFS LVDFEALAIN TSKSDLEYLK HIPPERRILV GESIVGGKGV
NANPLLGREA MKRDLPMVMK KISSLVGYED VDIFFLTFGF GGGTGAGGTP VLAEALKEEY
PDSLVVAIGA LPLKEEGIRP TINAAITIDK LSRIVDSIIA IDNNKLKESD EDISQAYEKI
NYAIVERIAS LLALIDVPGE QTLDASDLKF VLRAMGSFAT VGYAKADATK IKSLSRLIIR
SFENEGLYLD VNLESALYGL VAIHGPPEVL KAKEIFDALS ELSQRIRGKQ IFRGFYPDPR
EREVEVVTLL SGIYESKSIE NIVITAKRYA REFMKAKEEG EMKKRELLKG LPDFEDIYPG
EVDEG