ID Q5UVN6_9PEZI Unreviewed; 323 AA.
AC Q5UVN6;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Lasiosphaeria lanuginosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Lasiosphaeriaceae; Lasiosphaeria.
OX NCBI_TaxID=260666 {ECO:0000313|EMBL:AAU04486.1};
RN [1] {ECO:0000313|EMBL:AAU04486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SMH2390 {ECO:0000313|EMBL:AAU04486.1};
RX AGRICOLA=IND43656196;
RA Miller A.N., Huhndorf S.M.;
RT "Using phylogenetic species recognition to delimit species boundaries
RT within Lasiosphaeria.";
RL Mycologia 96:1106-1127(2004).
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|ARBA:ARBA00011747,
CC 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; AY600257; AAU04486.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5UVN6; -.
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: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.
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 2..155
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 157..294
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAU04486.1"
FT NON_TER 323
FT /evidence="ECO:0000313|EMBL:AAU04486.1"
SQ SEQUENCE 323 AA; 36038 MW; 729DA9B781A3C3C9 CRC64;
FVFGQSGAGN NWAKGHYTEG AELVDQVLDV VRREAEGCDC LQGFQITHSL GGGTGAGMGT
LLISKIREEF PDRMMATFSV VPSPKVSDTV VEPYNATLSV HQLVENSDET FCIDNEALYD
ICMRTLKLSN PSYGDLNYLV SAVMSGVTVS LRFPGQLNSD LRKLAVNMVP FPRLHFFMVG
FAPLTSRGAH SFRAVSVPEL TQQMFDPKNM MAASDFRNGR YLTCSAIFRG KVSMKEVEDQ
MRNVQNKNSS YFVEWIPNNV QTALCSIPPR GLKMSSTFVG NSTAIQELFK RIGEQFTAMF
RRKAFLHWYT GEGMDQMEFT EAE
//
