ID R9ACL7_WALI9 Unreviewed; 883 AA.
AC R9ACL7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Tubulin beta chain {ECO:0000313|EMBL:EOQ99953.1};
GN ORFNames=J056_001183 {ECO:0000313|EMBL:EOQ99953.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ99953.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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}.
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DR EMBL; KE007237; EOQ99953.1; -; Genomic_DNA.
DR RefSeq; XP_009269181.1; XM_009270906.1.
DR AlphaFoldDB; R9ACL7; -.
DR STRING; 1299270.R9ACL7; -.
DR GeneID; 20374135; -.
DR KEGG; wic:J056_001183; -.
DR eggNOG; KOG1375; Eukaryota.
DR HOGENOM; CLU_015718_1_1_1; -.
DR OrthoDB; 899149at2759; -.
DR Proteomes; UP000014064; 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:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02187; beta_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; IPR002453; Beta_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:SF492; TUBULIN BETA-4 CHAIN; 1.
DR Pfam; PF00091; Tubulin; 2.
DR Pfam; PF03953; Tubulin_C; 2.
DR PRINTS; PR01163; BETATUBULIN.
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 Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064}.
FT DOMAIN 48..245
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 247..384
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT DOMAIN 481..678
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 680..817
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 883 AA; 99062 MW; 14B73D759E086BC1 CRC64;
MGREIVHLQT GQCGNQIGSK FWETLSEEHA IDESGAYYGD IDQQLERINV YYNEAAEKKF
VPRSVLVDLE PGTIETVQAS SIGGLFRPDN MIFGQSSAGN NWAKGHYTEG AELVDQILDV
TRREAENCDC LQGFQIAHSL GGGTGSGLGT LLISKIREEF PDRMMATFSV VPSPKVSDTV
VEPYNAVLSV HQLVENSDLT FCIDNEALYD ICFKTLKMST PNYGDLNHLV SMVMSGVTTC
LRFPGQLNSD LRKLAVNMVP FPRLHFFMVG YAPLTAKGTS QFRAVSVPEL TQQMFDAKNM
MAASDPRNGR YLTVAAYFRG KVSMKEVEEQ MQAVQNKNSD YFVEWIPNNI QTAHCDIAPK
DTKMAVTFIG NTTSIQELFH RVNDQFSAMF RRKAFLHWYT GEGMDEMEFT EAESNMADLL
SEYQQYENAG VEEEEYYEEE VMEDECGNQI GAKFWDVIGE EHGLDGAGNY KGDIDEQLER
INVYYNEAQT GRYVPRAVLV DLEPGTMDAI KSSSLGDLFR PDNMVHGQSG AGNNWAKGHY
TEGAELVDSV LDVLRKEAEA TDCLQGFQIT HSLGGGTGSG MGTLLVSKIR EEFPDRMMAT
FSVVPSPKVS DTVVEPYNAV LSVNQLVENS DETFCIDNEA LYDICFRTLK LSTPTYGDLN
HLVSIVMSGI TTCLRFPGQL NSDLRKLAVN LVPFPRLHFF MLGYAPLTAR GSQQYRAVSV
PELTQQMFDA RNMMAASDPR SGRYLTVAAY FRGKVSMKEV EDQMNNMQNK NSDYFVEWIP
NNVQTALCNV APKGSKMSAT FIANTTAIQD LFKRVHDQFS AMFRRKAFLH WYTGEGMDEM
EFTEAESNMQ DLISEYQQYE SAGIDEDIEE EYVEEGVEEY VEE
//
