ID   TBA6_NAEPR              Reviewed;         452 AA.
AC   Q962P8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Tubulin alpha-6 chain;
GN   Name=TUBA6;
OS   Naegleria pringsheimi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=234921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30961 / NB-1;
RX   PubMed=12137945; DOI=10.1016/s0378-1119(02)00509-7;
RA   Chung S., Cho J.-Y., Cheon H.-J., Paik S.-Y., Lee J.-H.;
RT   "Cloning and characterization of a divergent alpha-tubulin that is
RT   expressed specifically in dividing amebae of Naegleria gruberi.";
RL   Gene 293:77-86(2002).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC       two moles of GTP, one at an exchangeable site on the beta chain and one
CC       at a non-exchangeable site on the alpha chain.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Note=Present in
CC       the nuclei and mitotic spindle-fibers but absent in flagellar axonemes
CC       or cytoskeletal microtubules.
CC   -!- DEVELOPMENTAL STAGE: Expressed in actively growing cells and repressed
CC       quickly when these cells were induced to differentiate.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AF401640; AAK84065.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q962P8; -.
DR   SMR; Q962P8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR013838; Beta-tubulin_BS.
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; PTHR11588; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..452
FT                   /note="Tubulin alpha-6 chain"
FT                   /id="PRO_0000048196"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  50470 MW;  553C69323CFB49D0 CRC64;
     MREIINIHIG QAGIQAGEQV WSLMCAEHGI NQDGTRNSTS ANGNSDCSVL FSEGSRGKYV
     PRNLMVDLEP SVVDSVRNSS YKELYHPAQM ITGREDAANN FARGHYTVGK DMLDVTVDRL
     RKIADNCTSL QGFQIFHSVG GGTGSGFASL LVERLSVEFP KKCKLSYTVY PSPQLATSVV
     EPYNSVLSTH SLLEHNDISV VLDNQAIYDI CKQRLKIERA NYRNLNHVIS QTVSAITCSL
     RFSGSLNVDM NEYQTNLVPY PRIHFMLSSL APMISRQENY YHENNVAELT SSVFEADNMM
     AKCNPRDGKY IASCLMYRGD VVNKEVTDAV KNVKSKANIQ FVDWSPCAFK IGVNSQKPTV
     LPDSEFAQVE RSCAMISNNT AISQVFERMN DKFDLLYAKR AYVHHFVSEG MEEGEFAEAR
     EDLAALEKDY TELASNSVNE EDSMLDEGET LN