ID D6BQ93_9GLOM Unreviewed; 201 AA.
AC D6BQ93;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Beta-tubulin {ECO:0000313|EMBL:ADD12933.1};
DE Flags: Fragment;
OS Dentiscutata heterogama.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Dentiscutata.
OX NCBI_TaxID=1316150 {ECO:0000313|EMBL:ADD12933.1};
RN [1] {ECO:0000313|EMBL:ADD12933.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WV858 {ECO:0000313|EMBL:ADD12933.1};
RX PubMed=20943151;
RA Morton J.B., Msiska Z.;
RT "Ontogeny and phylogeny of a Scutellospora heterogama mutant, with
RT implications for morphological recognition of species in Glomeromycota.";
RL Fungal Biol. 114:410-420(2010).
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 -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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DR EMBL; FJ896107; ADD12933.1; -; Genomic_DNA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; 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; 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; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 89..200
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADD12933.1"
FT NON_TER 201
FT /evidence="ECO:0000313|EMBL:ADD12933.1"
SQ SEQUENCE 201 AA; 22486 MW; 48EEA9D13273559C CRC64;
EYPDRMMCTF SVVPSPKVSD TVVEPYNATL SVHQLVENSD ETFCIDNEAL YDICFRTLKL
STPTYGDLNH LVSAVMSGTT ACLRFPGQLN ADLRKLAVNM VPFPRLHFFM VGFAPLTSRG
SEGYRAVSVP ELTQQIFDAK NMMAASDPRH GRYLTVSAIF RGRCSMKEVE DQMXAVQTKN
SSYFVEWIPN NVKTAVCDIP P
//
