ID K7NQR4_9EUKA Unreviewed; 360 AA.
AC K7NQR4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN Name=tubb {ECO:0000313|EMBL:AEX30312.1};
OS Codosiga botrytis.
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Codosiga.
OX NCBI_TaxID=1028796 {ECO:0000313|EMBL:AEX30312.1};
RN [1] {ECO:0000313|EMBL:AEX30312.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23083534; DOI=10.1016/j.protis.2012.09.002;
RA Paps J., Medina-Chacon L.A., Marshall W., Suga H., Ruiz-Trillo I.;
RT "Molecular phylogeny of unikonts: new insights into the position of
RT apusomonads and ancyromonads and the internal relationships of
RT opisthokonts.";
RL Protist 164:2-12(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 -!- 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}.
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DR EMBL; HQ896013; AEX30312.1; -; mRNA.
DR AlphaFoldDB; K7NQR4; -.
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; 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; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF492; TUBULIN BETA-4 CHAIN; 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 25..222
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 224..360
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEX30312.1"
FT NON_TER 360
FT /evidence="ECO:0000313|EMBL:AEX30312.1"
SQ SEQUENCE 360 AA; 39910 MW; E48791FD0E295A8C CRC64;
VISDEHGIDP AGTYQGDSDL QLERINVYYN EATGGKYVPR AVLVDLEPGT MDSVRAGPFG
QIFRPDNFVF GQSGAGNNWA KGHYTEGAEL VDSVLDVVRK EAESCDCLQG FQLTHSLGGG
TGSGLGTLLI SKIREEYPDR IMNTFSVCPS PKVSDTVVEP YNATLSVHQL VENTDETYCI
DNEALYDICF RTLKLTTPTY GDLNHLVSAT MSGVTTSLRF PGQLNADLRK LAVNMVPFPR
LHFFMPGFAP LTSRGSQQYR ALTVPELTQQ MFDSKNMMAA CDPRHGRYLT VATIFRGRMS
MKEVDEQMLN VQNKNSSYFV EWIPNNIKTA VCDIPPRGLK MSGTFIGNST AIQELFKRIR
//
