ID A0A166DC00_9AGAM Unreviewed; 864 AA.
AC A0A166DC00;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tubulin alpha-4A chain-like protein {ECO:0000313|EMBL:KZT38354.1};
GN ORFNames=SISSUDRAFT_1062080 {ECO:0000313|EMBL:KZT38354.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT38354.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT38354.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT38354.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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 -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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DR EMBL; KV428065; KZT38354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166DC00; -.
DR STRING; 1314776.A0A166DC00; -.
DR Proteomes; UP000076798; 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; 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:SF417; TUBULIN ALPHA-4 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 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:UP000076798}.
FT DOMAIN 48..245
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 247..392
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT DOMAIN 465..662
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 664..809
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 864 AA; 95162 MW; 371835B0D23C1F0A CRC64;
MREVISLHVG QAGVQIGNAC WELYTVEHGL SPDGRLVANS PSANDDGFST FFSESGSGKH
VPRSLYIDLE PSVIDEVRTG TYRTLFHPET LVTGKEDAAN NYARGHYTVG KEQIDIVMDK
VRRLADNCSG LQGFFVFHAF GGGTGSGFGA LLLDRLSTDY GKKSKLEFSV YPAPKMANSV
VEPYNSVLTT HTTLEHSDCS FMVDNEAIYD ICKKNLNIAS PSFSNLNRLI AQVVSSVTAS
LRFDGSLNVD LNEFQTNLVP FPRIHFPLAT YAPIISAEKA HHEQNSVADM TFACFEAGNQ
MVKCDPREGK YMACCLLYRG DVVPKDVNAA VSVIKTKRTI QFVDWCPTGF KLGICNEPPA
LVPGGDLAKV SRSLCMLSNT TAISSAWSRL DHKFDLLYSK RAFVHWYVGE GMEEGEFSEA
REDLAALEKD YEEVGLDGEL YTIEHGLTPD GRLTQASPSH SDSGFSTFFS ETNSGKHVPR
ALFVDLEPSV IDEIKTGTYR SLFHPETLVT GKEDAANNYA RGHYTVGKEL IDGVMDKVRR
LADNCTGLQG FFVFHSFGGG TGSGFGALLM DRLSNDYGKK SKLEFSVYPS PKMSSSVVEP
YNAVLTTHTT LEHSDCSFMV DNEAIYDISK KNLGVSSPSY TNLNRLIAQV VSSVTASLRF
DGSLNVDLNE FQTNLVPFPR IHFPLATYAP LISADKAFHE QNSVAEMTMS CFENGSQMVK
CDPREGKFMA CCLLYRGDVV PKDVQAAIAT IKTKRTIQFV DWCPTGFKLG VCNEPPALVP
GGDLAKVSRS VCMLSNTTAI ATAWSRLDHK FDLLYSKRAF VHWYVGEGME EGEFSEARED
LAALEKDYYE VAADSLEEEE VGEY
//
