ID A0A0F7IFT7_9EURY Unreviewed; 390 AA.
AC A0A0F7IFT7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Tubulin-like protein CetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN Name=cetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN ORFNames=GAH_02010 {ECO:0000313|EMBL:AKG90719.1};
OS Geoglobus ahangari.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG90719.1, ECO:0000313|Proteomes:UP000034723};
RN [1] {ECO:0000313|EMBL:AKG90719.1, ECO:0000313|Proteomes:UP000034723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=234 {ECO:0000313|EMBL:AKG90719.1,
RC ECO:0000313|Proteomes:UP000034723};
RA Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA Kashefi K.;
RT "The complete genome sequence of the hyperthermophilic, obligate iron-
RT reducing archaeon Geoglobus ahangari strain 234T.";
RL Submitted (APR-2015) 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; CP011267; AKG90719.1; -; Genomic_DNA.
DR RefSeq; WP_048096892.1; NZ_CP011267.1.
DR AlphaFoldDB; A0A0F7IFT7; -.
DR STRING; 113653.GAH_02010; -.
DR GeneID; 24804574; -.
DR KEGG; gah:GAH_02010; -.
DR PATRIC; fig|113653.22.peg.1977; -.
DR HOGENOM; CLU_058152_0_0_2; -.
DR InParanoid; A0A0F7IFT7; -.
DR OrthoDB; 329751at2157; -.
DR Proteomes; UP000034723; 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}; Reference proteome {ECO:0000313|Proteomes:UP000034723}.
FT DOMAIN 2..200
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 109..111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
SQ SEQUENCE 390 AA; 42378 MW; 732A24F19DA3616C CRC64;
MRFFAIGFGQ AGGKILDLFM ENEKLRGSNT LKALAVNTAR TDLMGLKHIP PKNRILIGQT
IVKGHGVGTD NKLGAKIAQE EIETVLNAID EMGTHEIDAF LIIAGLGGGT GSGGSPVLAK
YLSEMYSEPV YAVGVLPAPE EGKLYSLNAA RSMITLLKYV DNLILVDNGA WKFEGMSLRE
SYAKINEEIV RRLAILARAG EPVEEGLVGE MVVDSSEVIN TLRGGGISSI GYATLPIQEK
KKGGGLFGFL KKKEEQVVTA EEDRSTRISS LVRKAALGRL TIPCNIGSAE RALVLVAGPP
EYLDRKGLEK AKLWLEEQIA GVEVRAGDYP TRRTKHIAAL VVLANVTDIP RVKQLQKLAA
EAKEEVEIAE KERIEKTISL FEEEDLEPLF
//
