ID A0A2C5ZRQ6_9HYPO Unreviewed; 915 AA.
AC A0A2C5ZRQ6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=TOG domain-containing protein {ECO:0000259|SMART:SM01349};
GN ORFNames=CDD83_3387 {ECO:0000313|EMBL:PHH82011.1};
OS Cordyceps sp. RAO-2017.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH82011.1, ECO:0000313|Proteomes:UP000221130};
RN [1] {ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|Proteomes:UP000221130};
RA de Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHH82011.1, ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|EMBL:PHH82011.1,
RC ECO:0000313|Proteomes:UP000221130};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (OCT-2017) 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:PHH82011.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NJEV01001888; PHH82011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5ZRQ6; -.
DR STRING; 2004951.A0A2C5ZRQ6; -.
DR OrthoDB; 1369289at2759; -.
DR Proteomes; UP000221130; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:UniProt.
DR GO; GO:1902903; P:regulation of supramolecular fiber organization; IEA:UniProt.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
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.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000221130};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 8..237
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 172..210
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 288..529
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 515..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 98646 MW; ED9C4BD0534328C6 CRC64;
MADNNNNNKV TDQQVAELVA LLRGDAGLDA KVQHVTAVKS GIKQHNVPEA AVPQLFDALR
TAASSQHAAL VNAGFTALNH LFTRLSRQEP RLLAKEAPRC LPAVVDKLGD HKDKFRALAS
QALVTLYAAA PADVERAVRN QAMAAKNPRA KEASMQWLLQ MHKEHGLQFR SYVPLLMELL
EDADGMVRDA AKSTVIELFK TAPNAAKSDL KRQLKNFKVR PAIEQAIVKA LGPSAAAAAR
PDTPSDAPLP ARANNLAASV SSLASERPTT PMVADSPAEP IEPMYVNTHR ELDDLFRDMA
WHFDGKETEQ NWMKREQSVA TLRKLNAGNA PSDYPDAYVA GLRAMLDGII KAINSLRTSV
SKEGCGLIQD MAATLGPAMD PMVELLMQTL VKLSAGTKKI SSQLANVTVD TLIGRVTYTA
RLMQHVWGAC QDKNVQPRLY ATGWLKTLFR KEAHHKSHVE HTGGVDLMEK CIKRGLGDAN
PGVREKMRST YWAFWAVWPA RADAIMADLD PTAQKLLNKD PSNPNSPKKS ADPPRPGLGL
SRSTMASSKP SLREAMMAQK KATMAGRNLP ARPGSAMAHI SPVRTASNSS NHSATAAAKA
AVGARARQEP TISVNAGGMS VAPMRPARRR PDVAARPATA GPYSVRDQPG SLEMGSPESI
RSRGGTPKHG ATPPQRRTAP RPRPGHASHA SESGPISPTV ARAASRIPSP RGSPVTARHA
QDALLSPSPS KSNEEITLVV PVMPSIESTL SSSSSQRQEP PEPPEPPTEP PTEPQPSSAP
EEPDEEHVRP ASESPPRASL QVYEDPFTEE EQAAAKATTM TVPVLEEKPV NEDAAQLQRA
ANGDEAAAAA SASEQVSSPE KTRQNSRLLD SGINKIKAKS LEVHGFRKLQ SLLRDSRTVL
DSERFEVLLL GLFRR
//
