ID F8WR14_9EUKA Unreviewed; 404 AA.
AC F8WR14;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 22-FEB-2023, entry version 41.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN Name=TUB1 {ECO:0000313|EMBL:BAK61740.1};
OS Collozoum amoeboides.
OC Eukaryota; Sar; Rhizaria; Retaria; Polycystinea; Collodaria; Sphaerozoidae;
OC Collozoum.
OX NCBI_TaxID=1041365 {ECO:0000313|EMBL:BAK61740.1};
RN [1] {ECO:0000313|EMBL:BAK61740.1}
RP NUCLEOTIDE SEQUENCE.
RA Ishitani Y., Ishikawa S.A., Inagaki Y., Tsuchiya M., Takahashi K.,
RA Takishita K.;
RT "Multigene phylogenetic analyses including diverse radiolarian species
RT support the "Retaria" hypothesis - The sister relationship of Radiolaria
RT and Foraminifera.";
RL Mar. Micropaleontol. 81:32-42(2011).
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 -!- 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|RuleBase:RU000352}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; AB613234; BAK61740.1; -; mRNA.
DR AlphaFoldDB; F8WR14; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02187; beta_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; IPR002453; Beta_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:SF429; TUBULIN BETA-1 CHAIN-RELATED; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
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.
PE 2: Evidence at transcript level;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352}.
FT DOMAIN 40..237
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 239..376
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAK61740.1"
FT NON_TER 404
FT /evidence="ECO:0000313|EMBL:BAK61740.1"
SQ SEQUENCE 404 AA; 45122 MW; F9770FE6D3D5496E CRC64;
PAGQCGNQIG AKFWEVISDE HGIDPTGTYH GDSDLQLERI NVYYNEATGG RYVPRAILMD
LEPGTMDSVR AGPFGQLFRP DNFVFGQTGA GNNWAKGHYT EGAELIDSVL DVVRKEAESC
DCLQGFQITH SLGGGTGSGM GTLLISKIRE EYPDRMMCTF SIFPSPKVSD TVVEPYNATL
SVHQLVENAD EVMVIDNEAL YDICFRTLKL TTPTYGDLNH LVSAAMSGIT CCLRFPGQLN
SDLRKLAVNL IPFPRLHFFM IGFAPLTSRG SQQYRALTVP ELTQQMFDAK NMMCASDPRH
GRYLTASAMF RGRMSTKEVD EQMLNVQNKN SSYFVEWIPN NIKSSVCDIP PKGLKMSTTF
IGNTTAIQDM FKRVAEQFTA MFRRKAFLHW YTGEGMDEME FTRG
//