ID L5NY26_9EURY Unreviewed; 387 AA.
AC L5NY26;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Tubulin-like protein CetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN Name=cetZ {ECO:0000256|HAMAP-Rule:MF_01946};
GN ORFNames=D320_05281 {ECO:0000313|EMBL:ELK55315.1};
OS Haloferax sp. BAB-2207.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1296625 {ECO:0000313|EMBL:ELK55315.1, ECO:0000313|Proteomes:UP000010764};
RN [1] {ECO:0000313|EMBL:ELK55315.1, ECO:0000313|Proteomes:UP000010764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB2207 {ECO:0000313|EMBL:ELK55315.1,
RC ECO:0000313|Proteomes:UP000010764};
RA Joshi M.N., Sharma A.C., Pandit A.S., Pandya R.V., Desai S.M.,
RA Jasmani F.P., Pandey A., Saxena A.K., Bagatharia S.B.;
RT "Whole genome sequencing of Haloferax sp. BAB-2207.";
RL Submitted (DEC-2012) 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}.
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:ELK55315.1}.
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DR EMBL; ANPG01000109; ELK55315.1; -; Genomic_DNA.
DR AlphaFoldDB; L5NY26; -.
DR PATRIC; fig|1243180.4.peg.951; -.
DR Proteomes; UP000010764; 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 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:ELK55315.1};
KW Cell division {ECO:0000313|EMBL:ELK55315.1};
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}.
FT DOMAIN 1..198
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT REGION 354..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3..7
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 103..105
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
FT BINDING 180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01946"
SQ SEQUENCE 387 AA; 40787 MW; CD284962CC0AF97C CRC64;
MGQAGGNVLD ALLRYEQRTN ADYVVDAVAY NTASADLRGL DLVPEENRIL FGADEVSGHG
VGADNELAAE LAERDSRQLL RGTDGAPTST ADAFLIFAGL GGGTGSGAAP VLAKHLNRIY
EQPIYGVGIL PAADEGALYS RNAARSLRAF VDVTDHVFAF DNGAWAESGE DVAQAHDTMN
EELVRRLGIL FASGEVAESG TVAESVVDSS EVINTLRGGG ISTIGYAASE LPESDGGGGF
SIKGLLGGDS SSTDELDSIN RITTQTRKAV LGQLTLPCDV DSASRGLVVV SGPPEWLNRK
AVERSRTWVE EQTGSMEVRG GDYPLSESNH VGVLVLLGDV SRSDRVAEIR STAVEAEQNR
RERSASDAAD REDGTEAVVD DRLDSLF
//