ID A0A0B2UG97_9MICR Unreviewed; 439 AA.
AC A0A0B2UG97;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=M896_030930 {ECO:0000313|EMBL:KHN70106.1};
OS Ordospora colligata OC4.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Ordosporidae;
OC Ordospora.
OX NCBI_TaxID=1354746 {ECO:0000313|EMBL:KHN70106.1, ECO:0000313|Proteomes:UP000031056};
RN [1] {ECO:0000313|EMBL:KHN70106.1, ECO:0000313|Proteomes:UP000031056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OC4 {ECO:0000313|EMBL:KHN70106.1,
RC ECO:0000313|Proteomes:UP000031056};
RA Pombert J.-F., Haag K.L., Beidas S., Ebert D., Keeling P.J.;
RT "The Ordospora colligata genome; evolution of extreme reduction in
RT microsporidia and host-to-parasite horizontal gene transfer.";
RL MBio 0:0-0(2014).
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|ARBA:ARBA00011747,
CC ECO:0000256|RuleBase:RU000352}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN70106.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JOKQ01000003; KHN70106.1; -; Genomic_DNA.
DR RefSeq; XP_014564148.1; XM_014708662.1.
DR AlphaFoldDB; A0A0B2UG97; -.
DR STRING; 1354746.A0A0B2UG97; -.
DR GeneID; 26261377; -.
DR VEuPathDB; MicrosporidiaDB:M896_030930; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; A0A0B2UG97; -.
DR OrthoDB; 899149at2759; -.
DR Proteomes; UP000031056; 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:SF492; TUBULIN BETA-4 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:UP000031056}.
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 439 AA; 49035 MW; F86D00004222CDC5 CRC64;
MREIIHLQTG QCGNQVGCKF WETISGEHGI DQTGRYVGES DNQLERINVY YNEASSKKYV
PRAVLIDLEP GTMDAVRQGP FGDLFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVMDVV
RKEAESSDCL QGFQITHSLG GGTGAGMGTL LLSKIREDFP DRMICTFSVV PSPKVSDTVV
EPYNATLSIH QLVENADETF CIDNEALYDI CFRTLKLSNP GYGDLNHLVS LVMSGVTTCL
RFPGQLNADL RKLAVNMIPF PRLHFFVVGF APLIAIGTQK FRTYSVSELT QQMFDSKNMM
TACDPRKGRY LTVAAVFRGK ISMKDVDEQM SMVQSKNSSL FVEWIPSNVK TAVCDIAPTG
LEMSATFVGN TTSIQELFKR ISDQFTVMFR RKAFLHWYTG EGMDEMEFSE AESNMNDLLS
EYQQYQDATV GDVEEFLVN
//
