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Database: UniProt
Entry: D2RWE8_HALTV
LinkDB: D2RWE8_HALTV
Original site: D2RWE8_HALTV 
ID   D2RWE8_HALTV            Unreviewed;       392 AA.
AC   D2RWE8;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Tubulin-like protein CetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN   Name=cetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN   OrderedLocusNames=Htur_0639 {ECO:0000313|EMBL:ADB59537.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB59537.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB59537.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
CC   -!- FUNCTION: Involved in cell shape control. {ECO:0000256|HAMAP-
CC       Rule:MF_01946}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01946}.
CC   -!- SIMILARITY: Belongs to the CetZ family. {ECO:0000256|ARBA:ARBA00006877,
CC       ECO:0000256|HAMAP-Rule:MF_01946}.
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DR   EMBL; CP001860; ADB59537.1; -; Genomic_DNA.
DR   RefSeq; WP_012941858.1; NC_013743.1.
DR   AlphaFoldDB; D2RWE8; -.
DR   STRING; 543526.Htur_0639; -.
DR   GeneID; 8741221; -.
DR   KEGG; htu:Htur_0639; -.
DR   eggNOG; arCOG02202; Archaea.
DR   HOGENOM; CLU_058152_0_0_2; -.
DR   OrthoDB; 329751at2157; -.
DR   Proteomes; UP000001903; 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   CDD; cd02202; CetZ_tubulin-like; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   HAMAP; MF_01946; CetZ; 1.
DR   InterPro; IPR032907; CetZ.
DR   InterPro; IPR048737; CetZ_C.
DR   InterPro; IPR045061; FtsZ/CetZ.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR   PANTHER; PTHR30314:SF10; TUBULIN-LIKE PROTEIN CETZ; 1.
DR   Pfam; PF21011; CetZ_C; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   SMART; SM00864; Tubulin; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_01946}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01946};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01946};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01946}.
FT   DOMAIN          2..195
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   COILED          352..379
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         10..14
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT   BINDING         110..112
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT   BINDING         142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT   BINDING         169
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT   BINDING         187
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
SQ   SEQUENCE   392 AA;  41864 MW;  8D973CD42E6216FF CRC64;
     MKLAMIGFGQ AGGKIVDRFL DYDDRTGSGI VRAAIAVNSA KADLMGLKNI PQENRVLIGQ
     ARVKGHGVGA DNELGAEVAE EDIDEVQNAI DAIPTHEVDA FLVVAGMGGG TGSGGAPVLA
     KHLKRIYTIP VYGLGVLPGT DEGGIYTLNA ARSFQTFVRE VDNLMVFDND SWRQTGESVE
     GGYEQINEEI VRRFGILFGA GEVGDGQEVA ESVVDSSEII NTLSGGGVST VGFASEEVDL
     NTGGGLLSRF TGDAGGDDNL DAANTTNRIT SLVRKAALGR LTLPCEIEGT ERALLVLAGP
     SEYLNRKGIE RGRKWLEEET GSMEVRGGDY PREEPEVAAA ILLSGVTNVP RIKRLQQVAI
     EAQDNIDDIQ QESEENLEEL VEDDEDELEP LF
//
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