ID Q4PL62_PLABE Unreviewed; 453 AA.
AC Q4PL62;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=PBK173_000068300 {ECO:0000313|EMBL:CXI04804.1},
GN PBNK65E_000065900 {ECO:0000313|EMBL:SCN22736.1}, PBNK65NY_000065400
GN {ECO:0000313|EMBL:SCL92308.1}, PBSP11A_000065600
GN {ECO:0000313|EMBL:SCM15637.1}, PBSP11RLL_000065500
GN {ECO:0000313|EMBL:SCM17429.1};
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821 {ECO:0000313|EMBL:AAY78954.1};
RN [1] {ECO:0000313|EMBL:AAY78954.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANKA {ECO:0000313|EMBL:AAY78954.1};
RX PubMed=16115694; DOI=10.1016/j.molbiopara.2005.07.003;
RA Kooij T.W., Franke-Fayard B., Renz J., Kroeze H., van Dooren M.W.,
RA Ramesar J., Augustijn K.D., Janse C.J., Waters A.P.;
RT "Plasmodium berghei alpha-tubulin II: a role in both male gamete formation
RT and asexual blood stages.";
RL Mol. Biochem. Parasitol. 144:16-26(2005).
RN [2] {ECO:0000313|EMBL:AAY78954.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANKA {ECO:0000313|EMBL:AAY78954.1};
RA Kooij T.W.A., Renz J., Ramesar J., Janse C.J., Waters A.P.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000219860, ECO:0000313|Proteomes:UP000219974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K173 {ECO:0000313|EMBL:CXI04804.1,
RC ECO:0000313|Proteomes:UP000069549}, NK65 ny
RC {ECO:0000313|EMBL:SCL92308.1, ECO:0000313|Proteomes:UP000516480},
RC NK65e {ECO:0000313|EMBL:SCN22736.1,
RC ECO:0000313|Proteomes:UP000220214}, SP11 Antwerpcl1
RC {ECO:0000313|EMBL:SCM15637.1, ECO:0000313|Proteomes:UP000219860}, and
RC SP11 RLL {ECO:0000313|EMBL:SCM17429.1,
RC ECO:0000313|Proteomes:UP000219974};
RG Pathogen Informatics;
RL Submitted (AUG-2016) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
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; DQ070855; AAY78954.1; -; Genomic_DNA.
DR EMBL; LT160024; CXI04804.1; -; Genomic_DNA.
DR EMBL; LT608140; SCL92308.1; -; Genomic_DNA.
DR EMBL; LT608252; SCM15637.1; -; Genomic_DNA.
DR EMBL; LT608268; SCM17429.1; -; Genomic_DNA.
DR EMBL; LT614630; SCN22736.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4PL62; -.
DR SMR; Q4PL62; -.
DR VEuPathDB; PlasmoDB:PBANKA_0417700; -.
DR OMA; ESCYDIC; -.
DR Proteomes; UP000069549; Chromosome 4.
DR Proteomes; UP000219860; Chromosome 4.
DR Proteomes; UP000219974; Chromosome 4.
DR Proteomes; UP000220214; Chromosome 4.
DR Proteomes; UP000516480; Chromosome 4.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; 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 CDD; cd02186; alpha_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; 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 InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF239; TUBULIN ALPHA CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352}.
FT DOMAIN 49..246
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 248..393
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 434..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 50207 MW; FEAC58ECE62DB035 CRC64;
MREVISIHVG QAGIQVGNAC WELFCLEHGI QPDGQMPPDQ AGRANDDAFN TFFSETGAGK
HVPRCVFVDL EPTVVDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEVIDVCLD
RIRKLADNCT GLQGFLMFSA VGGGTGSGFG CLMLERLSVD YGKKSKLNFC CWPSPQVSTA
VVEPYNSVLS THSLLEHTDV AIMLDNEAIY DICKKNLDIE RPTYTNLNRL IAQVISSLTA
SLRFDGALNV DVTEFQTNLV PYPRIHFMLS SYAPVVSAEK AYHEQLSVSE ITNSAFEPAN
MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
TVVPGGDLAK VMRAVCMISN STAIAEVFSR MDQKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGIETN DGEGEDEGYE ADY
//
