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Database: UniProt
Entry: A0A1G9QIH7_9EURY
LinkDB: A0A1G9QIH7_9EURY
Original site: A0A1G9QIH7_9EURY 
ID   A0A1G9QIH7_9EURY        Unreviewed;       359 AA.
AC   A0A1G9QIH7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Tubulin-like protein CetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN   Name=cetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN   ORFNames=SAMN04487949_0879 {ECO:0000313|EMBL:SDM10852.1};
OS   Halogranum gelatinilyticum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae.
OX   NCBI_TaxID=660521 {ECO:0000313|EMBL:SDM10852.1, ECO:0000313|Proteomes:UP000199451};
RN   [1] {ECO:0000313|Proteomes:UP000199451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10119 {ECO:0000313|Proteomes:UP000199451};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNHL01000001; SDM10852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9QIH7; -.
DR   STRING; 660521.SAMN04487949_0879; -.
DR   OrthoDB; 329751at2157; -.
DR   Proteomes; UP000199451; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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 cycle {ECO:0000313|EMBL:SDM10852.1};
KW   Cell division {ECO:0000313|EMBL:SDM10852.1};
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:UP000199451}.
FT   DOMAIN          2..202
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   REGION          335..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         10..14
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT   BINDING         106..108
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT   BINDING         138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT   BINDING         165
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT   BINDING         183
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
SQ   SEQUENCE   359 AA;  37312 MW;  A2B7E3D0A2992D7F CRC64;
     MKTVLIGVGQ AGGKLATSLV EFDDRMGFDA ITGALAINSA KADLQPLPLE TVLVGQDKVN
     GHGVGGDNEL GAEVMQSDAR EVMGALDGNI TAAAEAIVVV AGLGGGTGSG GAPVVVKELQ
     RVYDVPVYAL GVLPGRGEGA MFQVNAGRSL KTLAREADSV LLVDNDAWRS SGESMEEGYD
     AINEAIARRV GLLLASGEAV EGVGESVVDS SEIINTLRSG GIASLGYASA EAGEDAADNI
     NTVMSTARRA LLTGASLPDA TTADSALVVV AAESDRIPRK GVERARRWIE DETGSMQVRG
     GDFPLGSERI ATLVLLGGVE RSTRVEQFIE RAKEAREEAK QERQDPNTAF ANDELDSLF
//
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