TBAA_PNECA
ID TBAA_PNECA Reviewed; 212 AA.
AC Q07972;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Tubulin alpha chain;
DE Flags: Fragment;
GN Name=TUB-A;
OS Pneumocystis carinii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX NCBI_TaxID=4754;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8292993; DOI=10.1111/j.1550-7408.1993.tb04468.x;
RA Stringer J.R., Stringer S.L., Zhang J., Baughman R., Smulian A.G.,
RA Cushion M.T.;
RT "Molecular genetic distinction of Pneumocystis carinii from rats and
RT humans.";
RL J. Eukaryot. Microbiol. 40:733-741(1993).
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.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; L19616; AAA16925.1; -; Unassigned_DNA.
DR AlphaFoldDB; Q07972; -.
DR SMR; Q07972; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN <1..>212
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048220"
FT NON_TER 1
FT NON_TER 212
SQ SEQUENCE 212 AA; 23835 MW; 5A9A8534E6B94AEA CRC64;
VDNEAIYDIC RRNLGIERPG YTNLNRLIAH VVSSITASLR FDGSLNVDLN EFQTNLVPYP
RIHFPLVTYA PVISAAKAVH EANSVSEITN ACFEPNNQMV KCDPRNGKYM ATCLLYRGDV
VTKDVNAAVA AVRTKRTIQF VDWCPTGFKL GVCYQPPQHV PHGDLAKVDR AVCMLSNTTS
IAEAWPRLDH KFDLMYSKRA FVHWYVGEGM EE