GenomeNet

Database: UniProt
Entry: A0A0V0VSH7_9BILA
LinkDB: A0A0V0VSH7_9BILA
Original site: A0A0V0VSH7_9BILA 
ID   A0A0V0VSH7_9BILA        Unreviewed;       717 AA.
AC   A0A0V0VSH7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Tubulin alpha-3 chain {ECO:0000313|EMBL:KRX66459.1};
GN   Name=mec-12 {ECO:0000313|EMBL:KRX66459.1};
GN   ORFNames=T09_6176 {ECO:0000313|EMBL:KRX66459.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX66459.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX66459.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX66459.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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   -!- SIMILARITY: Belongs to the tubulin family.
CC       {ECO:0000256|ARBA:ARBA00009636}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX66459.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JYDN01000011; KRX66459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VSH7; -.
DR   STRING; 181606.A0A0V0VSH7; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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:SF417; TUBULIN ALPHA-4 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681}.
FT   DOMAIN          293..513
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          515..660
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
SQ   SEQUENCE   717 AA;  80757 MW;  2AFA4E00536776BA CRC64;
     MLELTMFRTV KLFCYFINIF TLQEFIYKID YIPFLAVSAN PYLLSNEDIY SPWKMWPKSI
     FLPGSYPFMH RTDTNYILPK PFLTKFSNGI ATGSSRIQFL RGNLKIPNLR QGAIWDFNGQ
     LRAGPTLAHF NHDNEVQPRN PLNLSPKAKS ILENDPAFHE LSNQGLMKGV LQSPFWPNRC
     NSPYCSPDLA SFDSSTVYQG QKNFYYDGRI EFPVFTGKHG QGYRFNQGGD FYAGKHPTVV
     TVGHHREVIS IHVGQAGVQI GNACWELYCL EHGIQPDGQM PTDRSLGVAD DSFTTFFSET
     GTGRHVPRAI FVDLEPSVIE ITQMKIPPTY VFSEIDISLF VTDEVRTGTY RQLFHPEQLI
     NGKEDAANNY ARGHYTIGKE IIDLVLDRIR RLADNCTGLQ GFLIFHSFGG GTGSGFTSLL
     MERLSVDYGK KSKLEFAIYP APQVSTAVVE PYNSILTTHT TLEHSDCAFM VDNEAIYDIC
     RRNLDIERPT YTNLNRLIGQ IVSSITASLR FDGALNVDLT EFQTNLVPYP RIHFPLVTYA
     PVISAEKAYH EQLTVGEITN QCFDPANQMV KCDPRHGKYM AVCLLYRGDV VPKDVNAAIA
     AIKTKRTIQF VDWCPTGFKV GINYQPPTVV PGGDLAKVPR AVCMLSNTTA IAEAWARLDH
     KFDLMYAKRA FVHWYVGEGM EEGEFSEARE DLAALEKDYE EVGVDTVDGN GKEADEY
//
DBGET integrated database retrieval system