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Database: UniProt
Entry: L5NY26_9EURY
LinkDB: L5NY26_9EURY
Original site: L5NY26_9EURY 
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
//
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