ID   A0A1Y2M9T2_EPING        Unreviewed;      1199 AA.
AC   A0A1Y2M9T2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=TOG domain-containing protein {ECO:0000259|SMART:SM01349};
GN   ORFNames=B5807_02877 {ECO:0000313|EMBL:OSS52772.1};
OS   Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX   NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS52772.1, ECO:0000313|Proteomes:UP000193240};
RN   [1] {ECO:0000313|EMBL:OSS52772.1, ECO:0000313|Proteomes:UP000193240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS52772.1,
RC   ECO:0000313|Proteomes:UP000193240};
RA   Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT   "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT   strain isolated from New Zealand.";
RL   Genome Announc. 0:0-0(2017).
CC   -!- FUNCTION: Microtubule binding protein that promotes the stabilization
CC       of dynamic microtubules. Required for mitotic spindle formation.
CC       {ECO:0000256|ARBA:ARBA00024889}.
CC   -!- SUBUNIT: Interacts with microtubules. {ECO:0000256|ARBA:ARBA00011375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|ARBA:ARBA00004186}.
CC   -!- SIMILARITY: Belongs to the CLASP family.
CC       {ECO:0000256|ARBA:ARBA00009549}.
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DR   EMBL; KZ107839; OSS52772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2M9T2; -.
DR   STRING; 105696.A0A1Y2M9T2; -.
DR   InParanoid; A0A1Y2M9T2; -.
DR   OMA; GNAPHDF; -.
DR   OrthoDB; 1369289at2759; -.
DR   Proteomes; UP000193240; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:UniProt.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024395; CLASP_N_dom.
DR   InterPro; IPR034085; TOG.
DR   PANTHER; PTHR21567; CLASP; 1.
DR   PANTHER; PTHR21567:SF9; CLIP-ASSOCIATING PROTEIN; 1.
DR   Pfam; PF12348; CLASP_N; 2.
DR   SMART; SM01349; TOG; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193240}.
FT   DOMAIN          1..230
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          517..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1199 AA;  130377 MW;  A907AF8DC7516A18 CRC64;
     MEEQTAALLA ALKKQASTNV DKRLDLFGSL KSNIKHQRVP ESCQADILEC IRIAMTAQTS
     AQLVTTGFST LSHLIKRLVL QKETHILSVH AGMLCPVLLE HLGNAREAHR SAASVLLVEL
     YHYCHPEIDA GIHGAMGGTN PRAKETAMHW VVKMNKNHAL PFKSYVNQLV VNLEDADPEV
     RNVAKTAIVQ LYQNAPGTAQ INLKKQLAAH NVRKGTVAFI TSHLDDAAAA AALDDHSHTS
     EPAPTAAPAL APVRERPLPA PRAKTLQPDM GFADSLAAEQ PPPTEAVSMD PIHIYTQREL
     EDIFRDMAPP FEGRENEQNW IGRDKNTLKL RRILKGNAPT EFHAAFVVGV KSLLDGILKV
     ANTLRTTMST NGCQLVQELA STLGPAIDPW AEILLQTFIK MCAATKNIAA QNGNTTVDAL
     LSNISYNNRV LQHIQFASQD KNVQPRCFSA GWMKTLIRKH KSHIEHSGGL DSFDKILRKG
     LTDANPKVRE AYRSTYWAFA LIWPEKANAM YETLEKREKS GLDRDPNNPN ASSLGSSQTS
     ATSSFSKSLG AGAARTSLKE KIAEQRRAKL AASKGVADRP SSAAASYETP RSLSTKSLGA
     GSRTTSTAST ATNGPARPPS AMSGDSTKSA LKTSTGTGSL MSGTVRRPIR RPEMNRPKTA
     DPYAMRQTKI TPSTTTTPEK TPAVKSLKKS VGSTTTSAAR SRPQTQNSPN ASPVRSKSRV
     DTGRTTTHRK NPSIGSHRAS PAASPHKDED LTMVKPFVRS QSHHDGTAPF RQRNGMDKRV
     SIDSDALDLD EDNFTMVVPN LTRPMSQRVQ STPAKPNAAG SHLPIPSPRA ASVLSTSLLP
     AQSPRQISPD RSAPEEVEVY EDPLAGDEPS TAGQELDTPV LGELPINERS NERQRITDSD
     ANAMTGIGME DFDRGHHKTT STDTVVHTEN KDANSPETLK NRQLLASALK KIEGRTVDAG
     MFRKIQDAIK SGQEIWGPND EVFGRLLVAC LDYFQTPMEE LRLPALKAGS CKSQALATIR
     AMLSLYRKET AKYFSRVLCT ILYAKAQHEN TSHIAGDMEA TANEIVRYGQ VSDCLNSVLA
     LVENMPASTS DSSPSALASG STRTMTMSLR TLASLVEISG SRNFTLSREQ THRLGQLAVR
     CMEDQDPDVR KANIELCVTL HERIVGPGGE TKAFWEAVAG AGEQQLNLLT YYLAKKQKA
//