ID Q9UAC3_CRYPV Unreviewed; 454 AA.
AC Q9UAC3;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN ORFNames=CPATCC_001765 {ECO:0000313|EMBL:QOY42153.1};
OS Cryptosporidium parvum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=5807 {ECO:0000313|EMBL:AAD20239.1};
RN [1] {ECO:0000313|EMBL:AAM69358.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Human isolate {ECO:0000313|EMBL:AAM69358.1};
RA Nelson R.G., Gut J., Hackbarth C.J.;
RT "The cloning and sequence analysis of alpha and beta tubulin from
RT Cryptosporidium parvum.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAD20239.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10519222; DOI=10.1111/j.1550-7408.1999.tb06073.x;
RA Bonafonte M.T., Garmon D., Mead J.R.;
RT "Characterization of an alpha-tubulin gene of Cryptosporidium parvum.";
RL J. Eukaryot. Microbiol. 46:545-547(1999).
RN [3] {ECO:0000313|EMBL:QOY42153.1, ECO:0000313|Proteomes:UP000593906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOWA-ATCC {ECO:0000313|EMBL:QOY42153.1,
RC ECO:0000313|Proteomes:UP000593906};
RA Baptista R.P., Li Y., Sateriale A., Ansell B., Jex A., Sanders M.,
RA Brooks K., Tracey A., Berriman M., Striepen B., Cotton J.A.,
RA Kissinger J.C.;
RT "Consistent, comparative and evidence-based genome assembly and annotation
RT for Cryptosporidium parvum, C. hominis and C. tyzzeri.";
RL Submitted (SEP-2019) 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; AF082877; AAD20239.1; -; Genomic_DNA.
DR EMBL; U65379; AAM69358.1; -; Genomic_DNA.
DR EMBL; CP044419; QOY42153.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UAC3; -.
DR SMR; Q9UAC3; -.
DR VEuPathDB; CryptoDB:cgd4_2860; -.
DR VEuPathDB; CryptoDB:CPATCC_0019790; -.
DR Proteomes; UP000593906; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 50..247
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 249..394
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT COILED 419..446
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 454 AA; 50458 MW; 97CBB5E49ECAAF46 CRC64;
MREVISIHVG QAGIQIGNAC WELFCLEHGI NPDGTMPMSE QNMGISDDAF NTFFSETGAG
KHVPRAVFVD LEPTVVDEIR SGTYRQLFHP EQLINGKEDA ANNFARGHYT VGKEILEVCL
DRIRKLADNC TGLQGFLMFN AVGGGTGAGL GTLLLERLSV DYGKKSKLNF CTWPSPQLST
AVVEPYNAVL STHSLLEHAD VAVMLDNEAI YDICRRNLNI EQPAYTNLNR LIAQVISSLT
ASLRFDGALN VDITEFQTNL VPYPRIHFML SSYAPIISAE KAFHEQLSVA EITNAVFEPQ
NQMAKCDPRH GKYMACCLMY RGDVVPKDTN AAVATIKTKR TIQFVDWCPT GFKCGINYQP
PTVVPGGDLA KVMRACCMIS NSTAIAEVFN RMDHKFDLMY SKRAFVHWYV GEGMEEGEFS
EAREDLAALE KDYEEVGIEI ADGEDEEVHY EGDF
//
