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Database: UniProt
Entry: A0JHM3_9EUKA
LinkDB: A0JHM3_9EUKA
Original site: A0JHM3_9EUKA 
ID   A0JHM3_9EUKA            Unreviewed;       401 AA.
AC   A0JHM3;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE   Flags: Fragment;
GN   Name=tuba {ECO:0000313|EMBL:CAJ87187.1};
OS   Telonema subtile.
OC   Eukaryota; Eukaryota incertae sedis; Telonemida; Telonema.
OX   NCBI_TaxID=232287 {ECO:0000313|EMBL:CAJ87187.1};
RN   [1] {ECO:0000313|EMBL:CAJ87187.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Shalchian-Tabrizi K., Eikrem W., Klaveness D., Vaulot D., Minge M.A.,
RA   Le Gal F., Romari K., Throndsen J., Botnen A., Massana R., Thomsen H.A.,
RA   Jakobsen K.S.;
RT   "Telonemia, a new protist phylum with affinity to chromist lineages.";
RL   Proc. R. Soc. Lond., B, Biol. Sci. 0:0-0(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; AM237835; CAJ87187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0JHM3; -.
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          38..235
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          237..382
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAJ87187.1"
FT   NON_TER         401
FT                   /evidence="ECO:0000313|EMBL:CAJ87187.1"
SQ   SEQUENCE   401 AA;  44433 MW;  9537953ACC01002E CRC64;
     NSPLVGNACW ELYCLEHGIQ FDGQMPADKT IGGGDDSFNT FFSETGAGKH VPRTIYLDLE
     PTVIDEVRTG TYRQLYHPEQ LISGKEDAAN NYARGHYTVG KEIVDLALDR LRKLADQCTG
     LQGFMVFNTV GGGTGSGLGS LLLERLSVDY GKKSKLGFCV YPSPQISTAV VEPYNAVLAT
     HSLLEHTDVA VMLDNEAIYD ICRRCLDIER PTYTNLNRLI SQVISSLTAS LRFDGALNVD
     ITEFQTNLVP YPRIHFMVSS YSPVISAEKA YHESLSVAEI TNSCFEPANM MTKCDPRHGK
     YMACCMMYRG DVVPKDVNAA IATIKTKRTI QFVDWCPTGF KCGINYQPPT VVPGGDLAKV
     QRACCMISNT TTVAEVFARI DHKFDLMYSK RAFVHWYVGE G
//
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