GenomeNet

Database: UniProt
Entry: X6NNZ2_RETFI
LinkDB: X6NNZ2_RETFI
Original site: X6NNZ2_RETFI 
ID   X6NNZ2_RETFI            Unreviewed;       452 AA.
AC   X6NNZ2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN   ORFNames=RFI_09738 {ECO:0000313|EMBL:ETO27394.1};
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO27394.1, ECO:0000313|Proteomes:UP000023152};
RN   [1] {ECO:0000313|EMBL:ETO27394.1, ECO:0000313|Proteomes:UP000023152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24332546;
RA   Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA   Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA   Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT   "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL   Curr. Biol. 0:0-0(2013).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC       consisting of laterally associated linear protofilaments composed of
CC       alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC       of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC       forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC       GTPase activity of alpha-tubulin. {ECO:0000256|RuleBase:RU000352}.
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   -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC       hollow water-filled tube with an outer diameter of 25 nm and an inner
CC       diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC       form protofilaments running lengthwise along the microtubule wall with
CC       the beta-tubulin subunit facing the microtubule plus end conferring a
CC       structural polarity. Microtubules usually have 13 protofilaments but
CC       different protofilament numbers can be found in some organisms and
CC       specialized cells. {ECO:0000256|ARBA:ARBA00011747,
CC       ECO:0000256|RuleBase:RU000352}.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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:ETO27394.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ASPP01007287; ETO27394.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6NNZ2; -.
DR   EnsemblProtists; ETO27394; ETO27394; RFI_09738.
DR   Proteomes; UP000023152; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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; IPR013838; Beta-tubulin_BS.
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-4 CHAIN; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
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.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000352};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023152}.
FT   DOMAIN          45..235
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          237..385
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
SQ   SEQUENCE   452 AA;  51169 MW;  B15427EC8FEA9055 CRC64;
     MREIITIQVG QAGIQVGNAV WEQYCAEHNI STAGKQQRVT KDNSFKVFFE ETSSGQFVDL
     EPDVIDNMKS GPLGSLFDKD FLLSGKEDSA NIFSRGCFLG KQILDKMDDQ LRKLADNCDN
     LMGFMVTHSI GGGTGSGVGA LIFEGFNLYY KKKVRVGCSI FPSYSISSSV VEPYNALFAV
     GSLLDFTDIV LVFDNESMYN ICQRNLHIAK PDVSNVNRLI AKVMSSMTVS LRFGGELNAS
     LDELQMNLIP FPRLHFLTTG MSPIVSKMDV NTISNDVQTI TDECFKPTNW LVHYNSFDPM
     DDKYMSIVLN YRGNITSKEA NTSIQWLKKN DKVRLVEWCP TGFKIGLNDI PATILEQDDI
     GAFSKNAVMI ANNIGISRMF NERITRKFDL MYNQRAFVHW YLGYGRRERQ FGITRQDLGY
     LERDYLDVLS EQITDEAVDD YVNDDNNDTN YY
//
DBGET integrated database retrieval system