ID A7E7P8_SCLS1 Unreviewed; 1085 AA.
AC A7E7P8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=TOG domain-containing protein {ECO:0000259|SMART:SM01349};
GN ORFNames=SS1G_01326 {ECO:0000313|EMBL:EDN96400.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN96400.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476622; EDN96400.1; -; Genomic_DNA.
DR RefSeq; XP_001597132.1; XM_001597082.1.
DR AlphaFoldDB; A7E7P8; -.
DR STRING; 665079.A7E7P8; -.
DR EnsemblFungi; EDN96400; EDN96400; SS1G_01326.
DR GeneID; 5494055; -.
DR KEGG; ssl:SS1G_01326; -.
DR eggNOG; ENOG502QT5T; Eukaryota.
DR HOGENOM; CLU_004060_0_0_1; -.
DR InParanoid; A7E7P8; -.
DR OMA; GNAPHDF; -.
DR OrthoDB; 1369289at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0060172; P:astral microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
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; 2.
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:UP000001312}.
FT DOMAIN 3..223
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 281..521
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 508..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 119402 MW; F54744B7A2D108D1 CRC64;
MGEKITEDQV ANLLAILRTD GSVDAKVNQI NNIKSSIKQH NVPEPCILSL FEALRIALSS
QHAALVNAGF STLNHLLTRL SRQEPKYITK EAARTLPMIN DKMGDQREKY RQLAAQCLTT
FWKNAPMDVE RIVKNAGLVG KNSRMKETSM NWIVQMHQEH GMPFKSFVTT LMELLEDADG
MVRDTARNTV ITLFHRNAPN GAKSDLKKQL KNFNVRPAIV SAITSQLIQA GPPVVVEQER
PEAPMRNPLA TSASAMNISR PATPEVRVEQ VEPAYVNTQR ELEETFQEMQ QWFQDKESEA
NWLKREQSCT KLRRLNAGNA PSDYHDAFLA GIKSLLDGIL KAVNSLRTSL SKEGCSLVQE
VARTAGPGLD PMVEILLQNL IKLCGGTKKI SSQNGNATVD IIISGVTYNH RIMQHIWLAC
QDKNVQPRTY ATGWLKTLLK KEAQHKSHVE HSGGLELIEK CLKKGLADAN PGVRENMRST
YWTFAQIWPA RAEIIIEDLE PTQKRLLENS ADNPNAPKKA AAVSTRPGLG FSKSSTGPPR
PSLRETMLAQ KKAQMANKNI PSRPGSAMST FSPTRTVPTK SSSEAAPTRP YLEANASRGG
LSVAPMRPSK SKRPELAPRP ATAGPYSVRR TNQASSEANA SPSSSTTARP PRSKTPVATS
SPQARRAPVP RPNTSHTSHP TQSSQPTQST YTSPAKTVPG KVTTASPRLA ASPHISSPVR
TRTKSVPGAP LSSPTRADED FTMVVPTITG LERIQSEKSH QVFDSSNREE IKAPVNQPMK
VYEDPFSSTD DTTTPRPTVT ASVLEEVPVN EDAMNLSRNS IGELDGEGIK NPPMSPDKLK
QTTKLLDSGI AKIRGKTLDV HGFRKLQTMI KDNKAVWGDG RFPALVMGLF EYLEEPLTNL
SPAKVQDVKA QILATIKVLY KNYREYFRPH IAKGFHSILV TRSCYDARTH IVSGLELLAD
ELVTLANPKD TISTILRSLS DEEMSLEGCR KLSMGLHILK QTLDVKSEVE LDDAEIDSIL
ALAAKCLESK ESGVRLDAVV LCVSTHARIG EARFWSGIGG RVSGDPKSLI TYYIVKRQRE
LEMGN
//
