ID A1C2D8_9EUKA Unreviewed; 314 AA.
AC A1C2D8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Alpha-tubulin {ECO:0000313|EMBL:ABL61226.1};
DE Flags: Fragment;
GN Name=Atub {ECO:0000313|EMBL:ABL61226.1};
OS uncultured Oxymonadida sp.
OC Eukaryota; Metamonada; Preaxostyla; Oxymonadida; environmental samples.
OX NCBI_TaxID=413579 {ECO:0000313|EMBL:ABL61226.1};
RN [1] {ECO:0000313|EMBL:ABL61226.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18211267; DOI=10.1111/j.1462-2920.2007.01430.x;
RA de Koning A.P., Noble G.P., Heiss A.A., Wong J., Keeling P.J.;
RT "Environmental PCR survey to determine the distribution of a non-canonical
RT genetic code in uncultivable oxymonads.";
RL Environ. Microbiol. 10:65-74(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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DR EMBL; DQ925219; ABL61226.1; -; mRNA.
DR AlphaFoldDB; A1C2D8; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02186; alpha_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 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 InterPro; IPR002452; Alpha_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF239; TUBULIN ALPHA CHAIN; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 2: Evidence at transcript level;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 1..109
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 111..256
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 295..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABL61226.1"
SQ SEQUENCE 314 AA; 34844 MW; 71D1039166245CFC CRC64;
FNSVGGGTGA GLGSLLLERL SVDYGKESKL SFTVYPSPQI SNAVVEPYNC VLSTHSLLEH
TVVCVMLDNE AIYDICRRSL DIERPTYTNL NRLIAQVISS LTASLRFDGA LNVDITEFQT
NLVPYPRIHF MLTSYAPVIS AEKAYHEQLS VAEITNSSFE PANMMAKCDP RHGKYMACCM
MYRGDVVPKD VNAAVAIIKT KRTIQFVDWC PTGFKCGINY QPPTVVPGGD LAKVQRAVCM
ISNSTAIAEV FSRIDRKFDL MYAKRAFVHW YVGEGMEEGE FSEAREDLAA LEKDYEEVGA
ESTGDEEEGG EEEY
//
