ID V4HH42_9EURY Unreviewed; 392 AA.
AC V4HH42;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Tubulin-like protein CetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN Name=cetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN ORFNames=K933_00817 {ECO:0000313|EMBL:ESP90060.1};
OS Candidatus Halobonum tyrrellensis G22.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobonum.
OX NCBI_TaxID=1324957 {ECO:0000313|EMBL:ESP90060.1, ECO:0000313|Proteomes:UP000017840};
RN [1] {ECO:0000313|EMBL:ESP90060.1, ECO:0000313|Proteomes:UP000017840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G22 {ECO:0000313|EMBL:ESP90060.1,
RC ECO:0000313|Proteomes:UP000017840};
RX PubMed=24336364;
RA Ugalde J.A., Narasingarao P., Kuo S., Podell S., Allen E.E.;
RT "Draft Genome Sequence of 'Candidatus Halobonum tyrrellensis' Strain G22,
RT Isolated from the Hypersaline Waters of Lake Tyrrell, Australia.";
RL Genome Announc. 1:e01001-13(2013).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01946}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESP90060.1}.
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DR EMBL; ASGZ01000002; ESP90060.1; -; Genomic_DNA.
DR RefSeq; WP_023392764.1; NZ_ASGZ01000002.1.
DR AlphaFoldDB; V4HH42; -.
DR STRING; 1324957.K933_00817; -.
DR PATRIC; fig|1324957.4.peg.171; -.
DR eggNOG; arCOG02202; Archaea.
DR OrthoDB; 329751at2157; -.
DR Proteomes; UP000017840; Unassembled WGS sequence.
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 PRINTS; PR00423; CELLDVISFTSZ.
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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000017840}.
FT DOMAIN 2..201
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT BINDING 112..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
SQ SEQUENCE 392 AA; 41820 MW; 12D8AB6037CDB690 CRC64;
MKLGTIGVGN AGSKVVDKMV EFETLTNRSL CRDALVINTA RTDLSKPDHV PEERRILIGD
THQKAKGHGV GGDVEVGAEV AKNDIDEIRR AFDDVDIHEV DAILVCASLG GGTGSGAGPV
VINELQKMYD EPVYALGVLP GQFEGGRPAL NAARSLQSFV ANVDNFIAFD NDAWRSKDQT
VGEGYAGMNR ELATRLVTLL GAGEYDEPTV AENVMDASDI MRTLDTGGIS SIGYASTPVE
DADEEEGLLG RFRETEAVES GSTPAAKING LVRRAVNSRL TLPCESSSAD RALIVLSGPP
SELSRKGLES AREWIEDEVD TVDVLAGDDP REGASALSAV VLLSNVTETP RIDAIQQQAV
DAQDKIAHQD AVREEEIEDL ITDDQGKIDP VL
//