ID Q5UK87_9DINO Unreviewed; 389 AA.
AC Q5UK87;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Tubulin beta chain {ECO:0000256|ARBA:ARBA00013288, ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Kryptoperidinium foliaceum.
OC Eukaryota; Sar; Alveolata; Dinophyceae; Peridiniales; Kryptoperidiniaceae;
OC Kryptoperidinium.
OX NCBI_TaxID=160619 {ECO:0000313|EMBL:AAV32828.1};
RN [1] {ECO:0000313|EMBL:AAV32828.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP 1326 {ECO:0000313|EMBL:AAV32828.1};
RX PubMed=15666722; DOI=10.1111/j.1550-7408.2004.tb00604.x;
RA McEwan M.L., Keeling P.J.;
RT "HSP90, tubulin and actin are retained in the tertiary endosymbiont genome
RT of Kryptoperidinium foliaceum.";
RL J. Eukaryot. Microbiol. 51:651-659(2004).
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}.
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; AY713392; AAV32828.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5UK87; -.
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; 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 3: Inferred from homology;
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..361
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAV32828.1"
FT NON_TER 389
FT /evidence="ECO:0000313|EMBL:AAV32828.1"
SQ SEQUENCE 389 AA; 43442 MW; 3F64D4723DCB4370 CRC64;
VISDEHGIDP TGTYHGDSDL QLERINVYYN EATGGRYVPR AILMDLEPGT MDSVRAGPFG
QLFRPDNFVF GQTGAGNNWA KGHYTEGAEL IDSVLDVVRK EAEGCDCLQG FQMTHSLGGG
TGSGMGMLLI SKVREEYPDR IMETFSVIPS PKVSDTVVEP YNAVLSFHQL VENADECFLL
DNEALYDICF RTLKLTTPTY GDLNHLVSAA ISGVTTCLRF PGQLNCDLRK IAVNLIPFPR
LHFFMTGFAP LTSRGSQQYR ALTVPELTQQ MFDAKNMMCA ADPRHGRYLT AAALFRGRMS
TKEVDEQMLN VQNKNSSYFV EWIPNNIKVS VCDIPPKGLK MAVAFAGNST AIQEMFKRVA
EYFTAMFRRK AFLHWYTGEG MDEMEFTEA
//
