ID A0A4J3_9EUKA Unreviewed; 380 AA.
AC A0A4J3;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Chrysochromulina sp. NIES-1333.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=407208 {ECO:0000313|EMBL:ABJ80991.1};
RN [1] {ECO:0000313|EMBL:ABJ80991.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIES 1333 {ECO:0000313|EMBL:ABJ80991.1};
RX PubMed=16982820; DOI=10.1093/molbev/msl120;
RA Kim E., Simpson A.G., Graham L.E.;
RT "Evolutionary relationships of apusomonads inferred from taxon-rich
RT analyses of 6 nuclear encoded genes.";
RL Mol. Biol. Evol. 23:2455-2466(2006).
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; DQ980513; ABJ80991.1; -; mRNA.
DR AlphaFoldDB; A0A4J3; -.
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 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:ABJ80991.1"
FT NON_TER 380
FT /evidence="ECO:0000313|EMBL:ABJ80991.1"
SQ SEQUENCE 380 AA; 42386 MW; 3A722F42C54BD906 CRC64;
VVSDEHGIDP TGTYHGDSDL QLERINVYYN EATGGRYVPR NILMDLEPGT MDSVRSGPFG
QIFRPDNFVF GQSGAGNNWA KGHYTEGAEL IDAVLDVVRK EAEGCDCLQG FTMTHSLGGG
TGSGMGTLLI SKIREEYPDR VMCTYSVFPS PKVSDTVVEP YNCVLSAHQL VENSNESLLL
DNEALYDICF RTLKLTTPTF GDLNHLVAAV MSATTCCLRF PGQLNCDLRK LAVNMIPFPR
LHFFMIGFSP LTSRGSQQYR ALTVPELTRQ MFDAKNMMAA ADPRHGRYLT ACALFRGRMS
TKEVDEQMLN VQNKNSSYFV EWIPNNLKCA ICDIPPKGLK MSVGFCGNST CMQEVMKRVA
EQFTSMFRRK AFLHWYTGEG
//
