ID Q95UU1_MONBE Unreviewed; 444 AA.
AC Q95UU1; A9USR7;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN Name=TUB_1 {ECO:0000313|EMBL:EDQ92151.1};
GN ORFNames=MONBRDRAFT_44315 {ECO:0000313|EMBL:EDQ92151.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:AAK27411.1};
RN [1] {ECO:0000313|EMBL:AAK27411.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 50154 {ECO:0000313|EMBL:AAK27411.1};
RX PubMed=11752452; DOI=10.1073/pnas.261477698;
RA King N., Carroll S.B.;
RT "A receptor tyrosine kinase from choanoflagellates: molecular insights into
RT early animal evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15032-15037(2001).
RN [2] {ECO:0000313|EMBL:EDQ92151.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 {ECO:0000313|EMBL:EDQ92151.1}, and MX1 / ATCC 50154
RC {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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}.
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DR EMBL; AY026071; AAK27411.1; -; mRNA.
DR EMBL; CH991544; EDQ92151.1; -; Genomic_DNA.
DR RefSeq; XP_001743437.1; XM_001743385.1.
DR AlphaFoldDB; Q95UU1; -.
DR STRING; 81824.Q95UU1; -.
DR EnsemblProtists; EDQ92151; EDQ92151; MONBRDRAFT_44315.
DR GeneID; 5888276; -.
DR KEGG; mbr:MONBRDRAFT_44315; -.
DR eggNOG; KOG1375; Eukaryota.
DR InParanoid; Q95UU1; -.
DR OMA; VMCIDNE; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001357}.
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"
FT COILED 408..442
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 444 AA; 49853 MW; 6DCC531140FDAAD3 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGKYV
PRAVLVDLEP GTMDSVRAGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAEGCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ACMSGVTTCL
RFPGQLNSDL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRNLSVPELT QQMFDAKNMM
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNIK TAVCDIPPRG
LKMSSTFVGN STAIQELFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEFDEEE EEME
//
