ID C0SKA4_9CHLO Unreviewed; 368 AA.
AC C0SKA4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN Name=btub {ECO:0000313|EMBL:ABO61465.1};
OS Chlamydomonas sp. CCMP225.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=429245 {ECO:0000313|EMBL:ABO61465.1};
RN [1] {ECO:0000313|EMBL:ABO61465.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP225 {ECO:0000313|EMBL:ABO61465.1};
RA Beaudoin D.J., Gast R.J., Conte M.A., Cummings M.P.;
RT "Analysis of Cold Tubulin Sequences and Their Implication for Cold-
RT Adaptation of Microtubules.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; EF432459; ABO61465.1; -; mRNA.
DR AlphaFoldDB; C0SKA4; -.
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 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 6..203
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 205..342
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABO61465.1"
FT NON_TER 368
FT /evidence="ECO:0000313|EMBL:ABO61465.1"
SQ SEQUENCE 368 AA; 41121 MW; 121708DCEF108C2A CRC64;
LQLERINVYY NEATGGRYVP RAVLMDLEPG TMDSVRAGPF GQLFRPDNFV FGQTGAGNNW
AKGHYTEGAE LIDSVLDVVR KEAEGCDCLQ GFQMCHSLGG GTGSGMGTLL ISKVRGEYPD
RIMETFSVIP SPKVSDTVVE PYNAVLSFHQ LVENADECFL LDNEALYDIC FRTLKLTTPT
YGDLNHLVSA AMSGVTTCLR FPGQLNCDLR KIAVNLIPFP RLHFFMTGFA PLTSRGSQQY
RALTVPELTQ QMFDAKNMMC AADPRHGRYL TAAALFRGRM STKEVDEQML NVQNKNSSYF
VEWIPNNIKA SVCDIPPKGL KMAVAFAGNS TAIQEMFKRV AEYFTAMFRR KAFLHWYTGE
GMDEMEFT
//
