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
//