ID A0A2U9B912_SCOMX Unreviewed; 868 AA.
AC A0A2U9B912;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative tubulin alpha chain {ECO:0000313|EMBL:AWP00272.1};
GN ORFNames=SMAX5B_004326 {ECO:0000313|EMBL:AWP00272.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP00272.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP00272.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) 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 -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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DR EMBL; CP026246; AWP00272.1; -; Genomic_DNA.
DR Proteomes; UP000246464; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 2.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 2.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 2.
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:SF349; TUBULIN ALPHA CHAIN; 1.
DR Pfam; PF00091; Tubulin; 2.
DR Pfam; PF03953; Tubulin_C; 2.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 2.
DR SMART; SM00865; Tubulin_C; 2.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 2.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 2.
DR PROSITE; PS00227; TUBULIN; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000246464}.
FT DOMAIN 34..231
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 233..378
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT DOMAIN 467..664
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 666..811
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 847..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 96542 MW; C997560104139810 CRC64;
MGNACWELYC LEHGIQPDGQ MPSDKTVGGG DDSFNTFFSE TGAGKHVPRA VFVDLEPTVI
DEVRTGTYRQ LFHPEQLITG KEDAANNYAR GHYTIGKEII DLVLDRTRKL ADQCTGLQGF
LIFHSFGGGT GSGFTSLLME RLSVDYGKKS KLEFAVYPAP QVSTAVVEPY NSILTTHTTL
EHSDCAFMVD NEAIYDICRR NLDIERPTYT NLNRLIGQIV SSITASLRFD GALNVDLTEF
QTNLVPYPRI HFPLATYAPV ISAEKAYHEQ LTVAEITNAC FEPANQMVKC DPRHGKYMAC
CLLYRGDVVP KDVNSAIATI KTKRTIQFVD WCPTGFKVGI NYQPPTVVPG GDLAKVQRAV
CMLSNTTAIA EAWARLDHKF DLMYAKRAFV HWYVGEGMEE GEFSEAREDM AALEKDYEER
ECISMHVGQA GTQMGNACWE LYCLEHGIQP DGQMPSDKTV GGGDDSFNTF FSETGAGKHV
PRAVFVDLEP TVIDEVRTGT YRQLFHPEQL ITGKEDAANN YARGHYTIGK EIIDLVLDRT
RKLADQCTGL QGFLIFHSFG GGTGSGFTSL LMERLSVDYG KKSKLEFAVY PAPQVSTAVV
EPYNSILTTH TTLEHSDCAF MVDNEAIXDI CRRNLDIERP TYTNLNRLIG QIVSSITASL
RFDGALNVDL TEFQTNLVPY PRIHFPLATY APVISAEKAY HEQLSVADIT NACFEPANQM
VKCDPRHGKY MACCLLYRGD VVPKDVNSAI AAIKTKRTIQ FVDWCPTGFK VGINYQPPTV
VPGGDLAKVQ RAVCMLSNTT AIAEAWARLD HKFDLMYAKR AFVHWYVGEG MEEGEFSEAR
EDMAALEKDY EEVGTDSVGD DDEEGEEY
//
