ID Q002C8_9CRYP Unreviewed; 384 AA.
AC Q002C8;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
OS Goniomonas truncata.
OC Eukaryota; Cryptophyceae; Cyathomonadacea; Goniomonadaceae; Goniomonas.
OX NCBI_TaxID=31325 {ECO:0000313|EMBL:ABJ81012.1};
RN [1] {ECO:0000313|EMBL:ABJ81012.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TMG005 {ECO:0000313|EMBL:ABJ81012.1};
RX PubMed=16982820; DOI=10.1093/molbev/msl120;
RA Kim E., Simpson A.G., Graham L.E.;
RT "Evolutionary relationships of apusomonads inferred from taxon-rich
RT analyses of 6 nuclear encoded genes.";
RL Mol. Biol. Evol. 23:2455-2466(2006).
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|RuleBase:RU000352}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; DQ980534; ABJ81012.1; -; mRNA.
DR AlphaFoldDB; Q002C8; -.
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 2: Evidence at transcript level;
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 27..224
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 226..371
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABJ81012.1"
FT NON_TER 384
FT /evidence="ECO:0000313|EMBL:ABJ81012.1"
SQ SEQUENCE 384 AA; 42599 MW; 6E92E9C61978CCEF CRC64;
LFCLEHGIQP DGQMPSDKTI GGGDDAFNTF FSETGAGKYV PRCVFVDLEP TVIDEVRTGT
YRQLFHPEQL ISGKEDAANN FARGHYTIGK EIVDLVLDRI RKLADNCTGL QGFMIFHAVG
GGTGSGLGAL LCERLSVDYG KKSKIGFCTW PSPQVSNAVV EPYNMVLSTH TLLEHMDVAI
MLDNEAIYDL CRRSLDIERP TYTNLNRLIA QVISSLTASL RFDGALNVDL TEFQTNLVPY
PRIHFMLSSF APVISAEKAY HEQLSVAEIT NAVFEPASMM VKCDPRHGKY MACCLMYRGD
VVPKDVNASV ATIKTKRTIQ FVDWCPTGFK RGINYQPPTV VPGGDLAKVQ RAVCMISNST
AIAEVFSRQD HKFDLMYSKR AFVH
//
