ID Q84KN7_OXYMA Unreviewed; 390 AA.
AC Q84KN7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Tubulin beta chain {ECO:0000256|ARBA:ARBA00013288, ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN Name=btub {ECO:0000313|EMBL:AAO49333.1};
OS Oxyrrhis marina (Dinoflagellate).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Oxyrrhinales; Oxyrrhinaceae;
OC Oxyrrhis.
OX NCBI_TaxID=2969 {ECO:0000313|EMBL:AAO49333.1};
RN [1] {ECO:0000313|EMBL:AAO49333.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12656195; DOI=10.1099/ijs.0.02328-0;
RA Saldarriaga J.F., McEwan M.L., Fast N.M., Taylor F.J., Keeling P.J.;
RT "Multiple protein phylogenies show that Oxyrrhis marina and Perkinsus
RT marinus are early branches of the dinoflagellate lineage.";
RL Int. J. Syst. Evol. Microbiol. 53:355-365(2003).
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; AF482404; AAO49333.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84KN7; -.
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 32..229
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 231..368
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAO49333.1"
FT NON_TER 390
FT /evidence="ECO:0000313|EMBL:AAO49333.1"
SQ SEQUENCE 390 AA; 43610 MW; 3155152696505A33 CRC64;
IGAKFWEVLS DEHGIDPTGT YHGDSDLQLE RINVYYNEAT GGRYVPRAIL MDLEPGTMDS
VRAGPFGQLF RPDNFVFGQT GAGNNWAKGH YTEGAELIDS VLDVVRKEAE GCDCLQGFQI
THSLGGGTGS GMGTLLISRI REEYPDRIMA SFSVIPSPKV SDTVVEPYNA VLSFHQLVEN
ADEVMTMDNE ALYDICFRTL KLTTPTYGDL NHLVSAAMSG ITSCIRFPGQ LNCDLRKLAV
NMIPFPRLHF FMVGFAPLTS RGSQQYRALT VPELTQQMFD AKNMMCAADP RHGRYLTACA
MFRGRMSTKE VDEQMLNVQN KNSSYFVEWI PNNIKQSVCD IPPKGLKMSV AFLGNSTAIQ
EMFKRVAEQF TAMFRRKAFL HWYTGEGMDE
//
