ID Q868U5_9ALVE Unreviewed; 387 AA.
AC Q868U5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Tubulin beta chain {ECO:0000256|ARBA:ARBA00013288, ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN Name=btub2 {ECO:0000313|EMBL:AAO49330.1};
OS Perkinsus marinus.
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=31276 {ECO:0000313|EMBL:AAO49330.1};
RN [1] {ECO:0000313|EMBL:AAO49330.1}
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; AF482401; AAO49330.1; -; Genomic_DNA.
DR AlphaFoldDB; Q868U5; -.
DR SMR; Q868U5; -.
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:AAO49330.1"
FT NON_TER 387
FT /evidence="ECO:0000313|EMBL:AAO49330.1"
SQ SEQUENCE 387 AA; 43147 MW; 4FD8ED0C3E8F3BED CRC64;
IGAKFWEVIS DEHGIDPTGT YHGDSDLQLE RINVYYNEAT GGRYVPRAVL MDLEPGTMDS
VRAGPFGQLF RPDNFVFGQS GAGNNWAKGH YTEGAELIDS VLDVVRKEAE GCDCLQGFQI
CHSMGGGTGS GMGTLLISKI REEYPDRIME TFSVFPSPKV SDTVVEPYNA TLSVHQLVEN
ADEVMVLDNE ALYDICFRTL KLTTPTYGDL NHLVSAAMSG VTTCLRFPGQ LNADLRKLAV
NMIPFPRLHF FMTGFAPLTS RGSQQYRALT VPELTQQMFD AKNMMCASDP RHGRYLTATA
LFRGRMSTKE VDEQMLNVQN KNSSYFVEWI PNNIKSGVCD IPPKGLKMAV TFLGNSTAIQ
EMFKRVAEQF TAMFRRKAFL HWYTGEG
//
