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Database: UniProt
Entry: A0A0A2VMD9_BEABA
LinkDB: A0A0A2VMD9_BEABA
Original site: A0A0A2VMD9_BEABA 
ID   A0A0A2VMD9_BEABA        Unreviewed;       871 AA.
AC   A0A0A2VMD9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Spindle pole body component alp14 {ECO:0000313|EMBL:KGQ07497.1};
GN   ORFNames=BBAD15_g7181 {ECO:0000313|EMBL:KGQ07497.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ07497.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ07497.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ07497.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC       {ECO:0000256|ARBA:ARBA00025722}.
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:KGQ07497.1}.
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DR   EMBL; ANFO01000683; KGQ07497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2VMD9; -.
DR   STRING; 1245745.A0A0A2VMD9; -.
DR   eggNOG; KOG1820; Eukaryota.
DR   HOGENOM; CLU_008401_0_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0099080; C:supramolecular complex; IEA:UniProt.
DR   GO; GO:0061863; F:microtubule plus end polymerase; IEA:InterPro.
DR   GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR   GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:InterPro.
DR   GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR   GO; GO:0007051; P:spindle organization; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR048492; Stu2_CTS.
DR   InterPro; IPR034085; TOG.
DR   InterPro; IPR045110; XMAP215.
DR   InterPro; IPR048491; XMAP215_CLASP_TOG.
DR   PANTHER; PTHR12609:SF0; CYTOSKELETON-ASSOCIATED PROTEIN 5; 1.
DR   PANTHER; PTHR12609; MICROTUBULE ASSOCIATED PROTEIN XMAP215; 1.
DR   Pfam; PF21042; Stu2_CTS; 1.
DR   Pfam; PF21041; XMAP215_CLASP_TOG; 2.
DR   SMART; SM01349; TOG; 2.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT   DOMAIN          1..233
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          274..506
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          225..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          634..731
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        225..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..266
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..594
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   871 AA;  94350 MW;  DCF64760063D72BC CRC64;
     MAEEEDYSSI PLPDRFTHKL WKVRKGAYEE AAKQFALTPD ESDPFFRPFL SDVGLWKSAV
     LDANVVSQQE GVIALCAFLK YAGRDAGLRT RNHTIGPIVE KCLSSSRAAT KQNAIEALLL
     YVELDVAGPV VEDVLPGLAH RTPKNVIATL NALTQIVHNY GCKIVDPKPI LKALPKAFGA
     ADKNVRAEAT SLTVELYRWL REAMKPLFWG ELKPTQHTDL EAQFEKVKAE PPPKQERLLR
     SQQEVVEAAP EDDGDGYDEG GDEPEGADEL DAFALAEPVD VSKKISPNFT ELLASSKWKD
     RKEAVDGLYE ALNVPRIKET DFGEVNRGLA KCMKDANVLV VTQAALCIEL LAKGLRQSFA
     KYRAIVMQPI MERLKEKKQT VSDALSAALD AVFASTTFSD CMEDITTALG NKNPQVKEGT
     MKFLIRCLRT TRDVPSKPEI AAVCESGKKL LAESTPGLRD GGAEILGTVM KIIGERAMTP
     LIEGLDDIRK TKVKEFYASA EVKAKEKPKA PPAPKAAPKK AVAGKRPVAK KAAPVMPATE
     PPAKPGSKLG MPKSSGLGGL KAPQKRTLAA PGTASPRRPA AGPPIMPSDD EPVAPPAQPR
     IGASRGLAGR SLAKSAAAPA MPPPDSPPRA SGFSAVERAE LEELRAANDR LTRQVDDMRQ
     ERSKFLSEIQ ELKNQNAGLI EDHTRDVLSI KAKETQLVRA RSDAEATEGV NDRLRRELER
     LKRALNKAET IGGGSGVVSP AITSPTRDDV GIFHDAGLAS GGYNRASFAS TMSEEKENSE
     MVYPRNKISP ELRYGSGASS GRGSPARGYR TANPPREESV DSMGPPRRER PVSSLPQPSG
     GGESWRRAAE VTSQLKARIE QMKAKQGFAR P
//
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