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Database: UniProt
Entry: A0A010R7E4_9PEZI
LinkDB: A0A010R7E4_9PEZI
Original site: A0A010R7E4_9PEZI 
ID   A0A010R7E4_9PEZI        Unreviewed;      1155 AA.
AC   A0A010R7E4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=TOG domain-containing protein {ECO:0000259|SMART:SM01349};
GN   ORFNames=CFIO01_07040 {ECO:0000313|EMBL:EXF73624.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF73624.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF73624.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF73624.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:EXF73624.1}.
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DR   EMBL; JARH01001050; EXF73624.1; -; Genomic_DNA.
DR   RefSeq; XP_007602716.1; XM_007602654.1.
DR   AlphaFoldDB; A0A010R7E4; -.
DR   STRING; 1445577.A0A010R7E4; -.
DR   KEGG; cfj:CFIO01_07040; -.
DR   eggNOG; ENOG502QT5T; Eukaryota.
DR   HOGENOM; CLU_004060_0_0_1; -.
DR   OrthoDB; 1369289at2759; -.
DR   Proteomes; UP000020467; 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; 3.
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:UP000020467}.
FT   DOMAIN          3..232
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          283..518
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          902..1153
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          226..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1155 AA;  125455 MW;  4DF78671037B3978 CRC64;
     MADKITEEQV DDLLKILRSE ASVDQKVQHV TGIKSGIKQH NVPDVLVPQV FDGLRTASTS
     PHAVLVNAGF TALNHLLTRL SRQEPKYIAK DAKHTLPLVI DKLGDPKDKF RSLASQALTT
     IYTAAPMDVE RSVKNVAMVG KNPRAKEASM HWLLYMHQEH GTQFRAYVPT LMELLEDADG
     MVRDVAKSTV IELFRNAPNA AKSDLKRQLK NFNVRPAIEQ AIVKELAPTA ADRPKTPGLD
     APAPAPRPKL AASVSSVASE RPVTPAPETR SEVEPSYANT QRELDDIFRE MMTYFEGRES
     EQNWLKREES MTKLRRLIAG NVPEDFPDAF MLGLKGLLDG IIKAITSLRT SLSKEGCNLV
     QDIAMTFGPG MDPLVELLMQ TFIKLAAATK KIASQQADTT VNIIIGKVTY NSRIMQHIWG
     ACQDKNVQPR TYATGWLKTI LTKEAHHKSH IEHGGGLDLV EKCIKKGLND ANPGVRERMR
     ATFWVFAKIW PSRADMLKDT LEPTAQKLLD KDPNNPNAPK REVEATRARP GLGLSKSTMG
     TGKPTLRETM MAQKKATMAA SQKLPPRPGS AMANLSPARP QQATSSSSSG PAPSAKPTAS
     GGMSVRPMRP TKRRPEMAAR PATAGPYSVR THDGPSAEAS SPENPKSRST TTRPKTEASP
     RRAQSRPRAA TSHASPGAKS TLSKSVSSPR DSPRTSPAKP KRMQTTIPTS SPSRDNEDLT
     LVVPSLGSLK STPTLDRRQR AATEEPTVPD FEADAPAEVS ADIPLPKAEP VQEASPEPVS
     EPTPEPAEQS QAEPEDEGTV EAPSETSPEA PAAETEEAPV EEILEAPAEA AAGGLAPSPV
     IEEMAKAEPE PVPTNGLKVF EDPFVDDGTT AGPDITTPVL EDKPVNEVAV PAPSNGFEAN
     GTPETPEKAR QTSRLLDSGV TRVKAKSLDV HGFRKLQSII RDNKAVFTDE KFEALLRGLF
     EYLESPLETL APERVQDVKA QIVARIKLLL KKERDNFQPH VSRGLESLVS TRSAYDSRTR
     IVSGLELLAE ELVALGDPPE IVVVMTKLLQ SKQDTTIEGS RCLATGLHVL KELLDKRTGF
     TPSDNELAQL AGLAGRCLES TDSGVRMGAV QLCVALHARI GDAPFWELIK GAKDDPKNLI
     TYYIAKHQRE SSVGA
//
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