ID G5EJ51_BABMI Unreviewed; 411 AA.
AC G5EJ51;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Tubulin beta chain {ECO:0000256|ARBA:ARBA00013288, ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Babesia microti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5868 {ECO:0000313|EMBL:BAL04558.1};
RN [1] {ECO:0000313|EMBL:BAL04558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JM1 {ECO:0000313|EMBL:BAL04558.1};
RA Hirata H., Kawai S., Maeda M., Jinnai M., Fujisawa K., Katakai Y.,
RA Hikosaka K., Tanabe K., Yasutomi Y., Ishihara C.;
RT "Identification and Phylogenetic Analysis of Japanese Macaque Babesia-1
RT (JM-1) detected from a Japanese Macaque (Macaca fuscata fuscata).";
RL Am. J. Trop. Med. Hyg. 85:635-638(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; AB576642; BAL04558.1; -; Genomic_DNA.
DR AlphaFoldDB; G5EJ51; -.
DR VEuPathDB; PiroplasmaDB:BMR1_01G01045; -.
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 20..217
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 219..356
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAL04558.1"
SQ SEQUENCE 411 AA; 45986 MW; FD0C1A3297AF5D93 CRC64;
HGIDPTGTYV GDSPLQLERA NVFYNQSSGG RYVPRAILMD LEPGTMDSVR SGPYGELFRP
DNYVFGQSGA GNNWAKGHYT EGAELIDSVL DVVRKEAEGC DCLQGFQITH SLGGGTGSGM
GTLLISKIRE EYPDRIMETF SVFPSPKVSD TVVEPYNATL SVHQLVENAD EVQVIDNEAL
YDICFRTLKL STPTYGDLNH LVSAAMSGVT CSLRFPGQLN SDLRKLAVNL IPFPRLHFFM
IGFAPLTSRG SQQYRALTVP ELTQQMFDAK NMMCASDPRR GKYLTACAMF RGKMSTKEVD
EQMLNVQNKN SSFFVEWIPH NTKSSVCDIP PKGLKMAVTF VGNSTAIQEM FKRVSEQFTA
MFRRKAFLHW YTGEGMDEME FTEAESNMND LVSEYQQYQE ATVEDDDFDD E
//
