ID   A0A2I2GBB9_9EURO        Unreviewed;       907 AA.
AC   A0A2I2GBB9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Putative spindle pole body component {ECO:0000313|EMBL:PLB50170.1};
GN   ORFNames=P170DRAFT_380598 {ECO:0000313|EMBL:PLB50170.1};
OS   Aspergillus steynii IBT 23096.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB50170.1, ECO:0000313|Proteomes:UP000234275};
RN   [1] {ECO:0000313|EMBL:PLB50170.1, ECO:0000313|Proteomes:UP000234275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB50170.1,
RC   ECO:0000313|Proteomes:UP000234275};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) 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:PLB50170.1}.
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DR   EMBL; MSFO01000003; PLB50170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2GBB9; -.
DR   STRING; 1392250.A0A2I2GBB9; -.
DR   VEuPathDB; FungiDB:P170DRAFT_380598; -.
DR   OrthoDB; 5477703at2759; -.
DR   Proteomes; UP000234275; 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   Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT   DOMAIN          1..234
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          277..509
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          244..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..562
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..746
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..815
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..865
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   907 AA;  98048 MW;  4947BAEBFEE09E72 CRC64;
     MAEGEEDFSS LPLPDRFSHK AWKVRKEGYE DAKKQFEKTA DESDPVFTPF LQDPSLWKGA
     VADSNVAAQQ EGLGSYCTFL KFGGTQACTR TRGYTVFPIV EKGLPSARPA AKTNALEALL
     LCVEMDKADP VIEEMIPGLS HKVPKVIAAT LMGLRTIYHN FGCKIVDPKP VLKALPKVFG
     HADKNVRAEA QNLTVELYRW LKEAIKPLFW GDLKQVQQTD LDKLFENVKQ EPSPKQERLT
     KAQQDAMAVA SSAPEGGEVG DEPEEFEEDA GEVDAFDLAE PVDVLAKAPG DFLDQVSSSK
     WKDRKDALDA LHAVLDVPKI KDGQYNDIVQ ALAKCMKDAN IAVVTVAAGC IDLLAKGLRS
     SFAKHRSVVM PPMMERLKEK KQTVADALGS ALDAVFLSTN LSECLEEILE FLKHKNPQVK
     QETLKFLIRC LRTTRDVPAK GEVKSIAEAG TKLLTDSSEV NRAGGAEVLG TLMKIMGERA
     MNPYLDGLDD IRKTKIKEFF ATAEVKAKER PKPVAAPPKA APAAGKKVVG GRKPALGMKK
     PAAAAPPAED PPIIPPSPAK PATRSIPSKL GAARPGGLPT PGTGLKKKLG GPGGIASPQA
     RRVISPPSEE QPPAPAAPKF GLARGLAGRP IAKPAAASEP APAPAAPQVS GMTAAERAEL
     EELRLEKERF SRTVEDLKYE RTKLNSQVTE LQNQNAQLIE DHTRDVLSIK AKETQLVRAR
     SDAETAEQTV QKQQREIERL KRELQRALRA SAASPPTAMS DSLNLPVPEA DSVYQDTSNG
     HGPMSRAGLQ HMGSRFDSSR PRSYASASPS EEKENNGLDS PGLGSREGGL GRRKLSPTFG
     TSYSGLGSPT RSSILGSSNA SGDDQPARRT EPAENWKRAA EVTTQLKARI EQMKAKQGLT
     RPPAQRQ
//