ID C7FB08_9CILI Unreviewed; 346 AA.
AC C7FB08;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Tubulin beta chain {ECO:0000256|ARBA:ARBA00013288, ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Philasterides dicentrarchi.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Philasteridae;
OC Philasterides.
OX NCBI_TaxID=282688 {ECO:0000313|EMBL:ACU33176.1};
RN [1] {ECO:0000313|EMBL:ACU33176.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21036479; DOI=10.1016/j.vetpar.2010.10.011;
RA Budino B., Lamas J., Pata M.P., Arranz J.A., Sanmartin M.L., Leiro J.;
RT "Intraspecific variability in several isolates of Philasterides
RT dicentrarchi (syn. Miamiensis avidus), a scuticociliate parasite of farmed
RT turbot.";
RL Vet. Parasitol. 175:260-272(2011).
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; GQ342956; ACU33176.1; -; mRNA.
DR AlphaFoldDB; C7FB08; -.
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; 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; 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 17..214
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 216..346
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACU33176.1"
FT NON_TER 346
FT /evidence="ECO:0000313|EMBL:ACU33176.1"
SQ SEQUENCE 346 AA; 38214 MW; 04A655B130A0B401 CRC64;
PPTGTYHGDS DLQLERINVY YNEATGGRYV PRAILMDLEP GTMDSVRAGP FGQLFRPDNF
VFGQTGAGNN WAKGHYTEGA ELIDSVLDVV RKEAEGCDCL QGFQITHSLG GGTGSGMGTL
LISKVREEYP DRIMETFSVV PSPKVSDTVV EPYNATLSVH QLVENADECM IIDNEALYDI
CFRTLKLTTP TYGDLNHLVS ASISGVTTCL RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF
APLTSRGSQQ YRALTVPELT QQMFDAKNMM CAADPRHGRY LTASALFRGR MSTKEVDEQM
LNVQNKNSSY FVEWIPNNIK SSICDIPPKG LKMAVTFVGN STATKK
//
