ID A8WEW7_9BILA Unreviewed; 450 AA.
AC A8WEW7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
OS Cyathostomum catinatum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Cyathostomum.
OX NCBI_TaxID=59891 {ECO:0000313|EMBL:ABW90087.1};
RN [1] {ECO:0000313|EMBL:ABW90087.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FBZ-R {ECO:0000313|EMBL:ABW90091.1}, and FBZ-S
RC {ECO:0000313|EMBL:ABW90087.1};
RX PubMed=18367189; DOI=10.1016/j.ijpara.2008.02.001;
RA Hodgkinson J.E., Clark H.J., Kaplan R.M., Lake S.L., Matthews J.B.;
RT "The role of polymorphisms at beta tubulin isotype 1 codons 167 and 200 in
RT benzimidazole resistance in cyathostomins.";
RL Int. J. Parasitol. 38:1149-1160(2008).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; EU251440; ABW90087.1; -; mRNA.
DR EMBL; EU251442; ABW90089.1; -; mRNA.
DR EMBL; EU251444; ABW90091.1; -; mRNA.
DR EMBL; EU251446; ABW90093.1; -; mRNA.
DR EMBL; EU251447; ABW90094.1; -; mRNA.
DR EMBL; EU251448; ABW90095.1; -; mRNA.
DR EMBL; EU251449; ABW90096.1; -; mRNA.
DR AlphaFoldDB; A8WEW7; -.
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; IPR013838; Beta-tubulin_BS.
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.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 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 47..244
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 246..383
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 428..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 50232 MW; 437A8F3088B6FC69 CRC64;
MREIVHIQAG QCGNQIGSKF WEVISDEHGI QPDGTYKGES DLQLERINVY YNEAHGGKYV
PRAVLVDLEP GTMDSVRSGT FGALFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAEGCDCL QGFQLTHSLG GGTGSGMGTL LIAKIREEYP DRIMASFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETF CIDNEALYDI CFRTLKLTNP TYGDLNHLVS MTMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLSAKGSQA YRASTVAELT QQMFDAKNMM
AACDPRHGRY LTVAAMFRGR MSMREVDDQM MSVQNKNSSY FVEWIPNNVK TSVCDIPPRG
LKMAATFVGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEATA DDEGDLDGTV ENETYQDQEE
//