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Database: UniProt
Entry: Q25023_HAECO
LinkDB: Q25023_HAECO
Original site: Q25023_HAECO 
ID   Q25023_HAECO            Unreviewed;       472 AA.
AC   Q25023;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN   Name=tub12-164 {ECO:0000313|EMBL:AAA29169.1};
OS   Haemonchus contortus (Barber pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6289 {ECO:0000313|EMBL:AAA29169.1};
RN   [1] {ECO:0000313|EMBL:AAA29169.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole animal {ECO:0000313|EMBL:AAA29169.1};
RX   PubMed=1741017; DOI=10.1016/0166-6851(92)90227-B;
RA   Geary T.G., Nulf S.C., Favreau M.A., Tang L., Prichard R.K.,
RA   Hatzenbuhler N.T., Shea M.H., Alexander S.J., Klein R.D.;
RT   "Three beta-tubulin cDNAs from the parasitic nematode Haemonchus
RT   contortus.";
RL   Mol. Biochem. Parasitol. 50:295-306(1992).
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; M76492; AAA29169.1; -; mRNA.
DR   AlphaFoldDB; Q25023; -.
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"
SQ   SEQUENCE   472 AA;  52075 MW;  10D0F87F4E5BF818 CRC64;
     MREIVHVQAG QCGNQIGAKF WEVISDEHGI QPDGSYKGES DLQLERINVY YNEANGGKYV
     PRAVLVDLEP GTMDSVRSGP FGALFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKEAEGCDCL QGFQLTHSLG GGTGSGMGTL LIAKIREEYP DRIMSSFSVV PSPKVSDTVV
     EPYNATLSVH QLVENTDETF CIDNEALYDI CFRTLKLTNP TYGDLNHLVS VTMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLSAKGAQA YRALTVSELT QQMFDAKNMM
     AACDPRHGRY LTVAAMFRGR MSMREVDDQM MSVQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMAATFVGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNGLVS
     EYQQYQEATA DDEGEMEGAV ENDTYAEGNS VIGSSTAGSP YLKSVSLVNV SV
//
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