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Database: UniProt
Entry: Q4Q4C4_LEIMA
LinkDB: Q4Q4C4_LEIMA
Original site: Q4Q4C4_LEIMA 
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
//
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