ID A0A0D8XG65_DICVI Unreviewed; 449 AA.
AC A0A0D8XG65;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=DICVIV_11294 {ECO:0000313|EMBL:KJH42719.1};
OS Dictyocaulus viviparus (Bovine lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH42719.1, ECO:0000313|Proteomes:UP000053766};
RN [1] {ECO:0000313|EMBL:KJH42719.1, ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH42719.1,
RC ECO:0000313|Proteomes:UP000053766};
RA Mitreva M.;
RT "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX PubMed=26856411; DOI=10.1038/srep20316;
RA McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA Sternberg P.W., Gasser R.B., Mitreva M.;
RT "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT lungworm biology and support future intervention.";
RL Sci. Rep. 6:20316-20316(2016).
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; KN716635; KJH42719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D8XG65; -.
DR STRING; 29172.A0A0D8XG65; -.
DR Proteomes; UP000053766; Unassembled WGS sequence.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053766}.
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 426..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 49909 MW; C5303AC7C8091711 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI QPDGSYKGES DLQLERINVY YNEASGGKYV
PRAILVDLEP GTMDSVRSGP FGALFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAEGCDCL QGFQLTHSLG GGTGSGMGTL LIAKIREEYP DRIMASFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETF CIDNEALYDI CFRTLKLTNP TYGDLNHLVS VTMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLSAKGAQA YRALTVAELT QQMFDAKNMM
AACDPRHGRY LTVAAMFRGR MSMREVDDQM MSVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMAATFVGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEATA DDEGEIEEGV ENDTYAAET
//
