ID U1P759_9EURY Unreviewed; 399 AA.
AC U1P759;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cell division GTPase {ECO:0000313|EMBL:ERH06156.1};
DE Flags: Fragment;
GN ORFNames=J07HN4v3_01766 {ECO:0000313|EMBL:ERH06156.1};
OS Halonotius sp. J07HN4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halonotius.
OX NCBI_TaxID=1070774 {ECO:0000313|EMBL:ERH06156.1, ECO:0000313|Proteomes:UP000030639};
RN [1] {ECO:0000313|EMBL:ERH06156.1, ECO:0000313|Proteomes:UP000030639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HN4 {ECO:0000313|Proteomes:UP000030639};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
CC -!- SIMILARITY: Belongs to the CetZ family.
CC {ECO:0000256|ARBA:ARBA00006877}.
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DR EMBL; KE356578; ERH06156.1; -; Genomic_DNA.
DR AlphaFoldDB; U1P759; -.
DR eggNOG; arCOG02202; Archaea.
DR HOGENOM; CLU_058152_0_0_2; -.
DR Proteomes; UP000030639; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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-KW.
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:ERH06156.1};
KW Cell division {ECO:0000313|EMBL:ERH06156.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030639}.
FT DOMAIN 2..233
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT REGION 73..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 399
FT /evidence="ECO:0000313|EMBL:ERH06156.1"
SQ SEQUENCE 399 AA; 42127 MW; 12072DF5E2ED9DBF CRC64;
MKLALFGVGN AGTRLLDQLI HAEDETGRNF TEGHVLAFNT APAAFEAATE IPDDRQVLIG
DTHPEVSHEL VSFDPDEDDT AVDSETPTDA DSAGVDGDPN LGATVANDEL PEIRRSLDLV
DDTEVDAAVV IAGLGGGTGA GVSSVLLEEL GSIYEIPIYV LGVLPAASES DRRALTAARA
VRTLVPLADA VLPVDNEAWR RNADPLAEQY ETINETIATR FVSLFAAGEA DPTSVSEMRI
DPADLRRTFG VGGLASIGYA THELDTEDRG FLYRLKKLLG LVDEEPSGPT DAATVKQLVG
RALGSKLTLP CEVTSADRVL LILSGPPSAI SRKGFETGRY LLEDETGTVE ILAGDEPLPG
ADTITATVLL SNVTDVPRLS TIQERAVDAL SAFENESPA
//