ID Q4Q4C4_LEIMA Unreviewed; 443 AA.
AC Q4Q4C4;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 127.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=LMJF_33_0792 {ECO:0000313|EMBL:CAJ06116.1}, LMJF_33_0794
GN {ECO:0000313|EMBL:CAJ06117.1}, LMJF_33_0796
GN {ECO:0000313|EMBL:CAJ06118.1}, LMJF_33_0798
GN {ECO:0000313|EMBL:CAJ06119.1}, LMJF_33_0800
GN {ECO:0000313|EMBL:CAJ06121.1}, LMJF_33_0802
GN {ECO:0000313|EMBL:CAJ06122.1}, LMJF_33_0804
GN {ECO:0000313|EMBL:CAJ06123.1}, LMJF_33_0806
GN {ECO:0000313|EMBL:CAJ06124.1}, LMJF_33_0808
GN {ECO:0000313|EMBL:CAJ06125.1}, LMJF_33_0810
GN {ECO:0000313|EMBL:CAJ06127.1}, LMJF_33_0812
GN {ECO:0000313|EMBL:CAJ06128.1}, LMJF_33_0814
GN {ECO:0000313|EMBL:CAJ06130.1}, LMJF_33_0816
GN {ECO:0000313|EMBL:CAJ06131.1}, LMJF_33_0818
GN {ECO:0000313|EMBL:CAJ06133.1}, LMJF_33_0819
GN {ECO:0000313|EMBL:CAJ06134.1}, LMJF_33_0820
GN {ECO:0000313|EMBL:CAJ06135.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ06117.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ06117.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Friedlin {ECO:0000313|EMBL:CAJ06117.1}, and MHOM/IL/81/Friedlin
RC {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAJ06117.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Friedlin {ECO:0000313|EMBL:CAJ06117.1}, and MHOM/IL/81/Friedlin
RC {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
RN [3] {ECO:0000313|EMBL:CAJ06117.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Friedlin {ECO:0000313|EMBL:CAJ06117.1};
RA Aslett M.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; FR796429; CAJ06116.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06117.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06118.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06119.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06121.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06122.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06123.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06124.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06125.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06127.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06128.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06130.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06131.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06133.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06134.1; -; Genomic_DNA.
DR EMBL; FR796429; CAJ06135.1; -; Genomic_DNA.
DR RefSeq; XP_001685823.1; XM_001685771.1.
DR RefSeq; XP_001685824.1; XM_001685772.1.
DR RefSeq; XP_001685825.1; XM_001685773.1.
DR RefSeq; XP_001685826.1; XM_001685774.1.
DR RefSeq; XP_001685827.1; XM_001685775.1.
DR RefSeq; XP_001685828.1; XM_001685776.1.
DR RefSeq; XP_001685829.1; XM_001685777.1.
DR RefSeq; XP_001685830.1; XM_001685778.1.
DR RefSeq; XP_001685831.1; XM_001685779.1.
DR RefSeq; XP_001685832.1; XM_001685780.1.
DR RefSeq; XP_001685833.1; XM_001685781.1.
DR RefSeq; XP_001685834.1; XM_001685782.1.
DR RefSeq; XP_001685835.1; XM_001685783.1.
DR RefSeq; XP_001685836.1; XM_001685784.1.
DR RefSeq; XP_001685837.1; XM_001685785.1.
DR RefSeq; XP_001685838.1; XM_001685786.1.
DR AlphaFoldDB; Q4Q4C4; -.
DR SMR; Q4Q4C4; -.
DR STRING; 5664.Q4Q4C4; -.
DR EnsemblProtists; CAJ06116; CAJ06116; LMJF_33_0792.
DR EnsemblProtists; CAJ06117; CAJ06117; LMJF_33_0794.
DR EnsemblProtists; CAJ06118; CAJ06118; LMJF_33_0796.
DR EnsemblProtists; CAJ06119; CAJ06119; LMJF_33_0798.
DR EnsemblProtists; CAJ06121; CAJ06121; LMJF_33_0800.
DR EnsemblProtists; CAJ06122; CAJ06122; LMJF_33_0802.
DR EnsemblProtists; CAJ06123; CAJ06123; LMJF_33_0804.
DR EnsemblProtists; CAJ06124; CAJ06124; LMJF_33_0806.
DR EnsemblProtists; CAJ06125; CAJ06125; LMJF_33_0808.
DR EnsemblProtists; CAJ06127; CAJ06127; LMJF_33_0810.
DR EnsemblProtists; CAJ06128; CAJ06128; LMJF_33_0812.
DR EnsemblProtists; CAJ06130; CAJ06130; LMJF_33_0814.
DR EnsemblProtists; CAJ06131; CAJ06131; LMJF_33_0816.
DR EnsemblProtists; CAJ06133; CAJ06133; LMJF_33_0818.
DR EnsemblProtists; CAJ06134; CAJ06134; LMJF_33_0819.
DR EnsemblProtists; CAJ06135; CAJ06135; LMJF_33_0820.
DR GeneID; 5654477; -.
DR GeneID; 5654478; -.
DR GeneID; 5654479; -.
DR GeneID; 5654480; -.
DR GeneID; 5654481; -.
DR GeneID; 5654482; -.
DR GeneID; 5654483; -.
DR GeneID; 5654484; -.
DR GeneID; 5654485; -.
DR GeneID; 5654486; -.
DR GeneID; 5654487; -.
DR GeneID; 5654488; -.
DR GeneID; 5654489; -.
DR GeneID; 5654490; -.
DR GeneID; 5654491; -.
DR GeneID; 5654492; -.
DR KEGG; lma:LMJF_33_0792; -.
DR KEGG; lma:LMJF_33_0794; -.
DR KEGG; lma:LMJF_33_0796; -.
DR KEGG; lma:LMJF_33_0798; -.
DR KEGG; lma:LMJF_33_0800; -.
DR KEGG; lma:LMJF_33_0802; -.
DR KEGG; lma:LMJF_33_0804; -.
DR KEGG; lma:LMJF_33_0806; -.
DR KEGG; lma:LMJF_33_0808; -.
DR KEGG; lma:LMJF_33_0810; -.
DR KEGG; lma:LMJF_33_0812; -.
DR KEGG; lma:LMJF_33_0814; -.
DR KEGG; lma:LMJF_33_0816; -.
DR KEGG; lma:LMJF_33_0818; -.
DR KEGG; lma:LMJF_33_0819; -.
DR KEGG; lma:LMJF_33_0820; -.
DR VEuPathDB; TriTrypDB:LmjF.33.0812; -.
DR VEuPathDB; TriTrypDB:LMJFC_330016000; -.
DR VEuPathDB; TriTrypDB:LMJLV39_330015200; -.
DR VEuPathDB; TriTrypDB:LMJSD75_330014900; -.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q4Q4C4; -.
DR OMA; EVEACEC; -.
DR Proteomes; UP000000542; Chromosome 33.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF429; TUBULIN BETA-1 CHAIN-RELATED; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000000542}.
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 443 AA; 49740 MW; CF57560B1EBF4975 CRC64;
MREIVSCQAG QCGNQIGSKF WEVIADEHGV DPTGSYQGDS DLQLERINVY FDESAGGRYV
PRAVLMDLEP GTMDSVRAGP YGQLFRPDNF IFGQSGAGNN WAKGHYTEGA ELIDSVLDVC
RKEAESCDCL QGFQLSHSLG GGTGSGMGTL LISKLREEYP DRIMMTFSVI PSPRVSDTVV
EPYNTTLSVH QLVENSDESM CIDNEALYDI CFRTLKLTTP TFGDLNHLVA AVMSGVTCCL
RFPGQLNSDL RKLAVNLVPF PRLHFFMMGF APLTSRGSQQ YRGLSVAELT QQMFDAKNMM
QAADPRHGRY LTASALFRGR MSTKEVDEQM LNVQNKNSSY FIEWIPNNIK SSICDIPPKG
LKMSVTFIGN NTCIQEMFRR VGEQFTGMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATV EEEGEYDEEE EAY
//