ID A0A317VV09_9EURO Unreviewed; 1189 AA.
AC A0A317VV09;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=TOG domain-containing protein {ECO:0000259|SMART:SM01349};
GN ORFNames=BO70DRAFT_372194 {ECO:0000313|EMBL:PWY77449.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY77449.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY77449.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY77449.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY77449.1}.
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DR EMBL; MSFL01000018; PWY77449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VV09; -.
DR STRING; 1448321.A0A317VV09; -.
DR VEuPathDB; FungiDB:BO70DRAFT_372194; -.
DR OrthoDB; 1369289at2759; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..288
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 148..182
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 454..685
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 285..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 130705 MW; 60AD3A7D0C1C02D2 CRC64;
MFSFTSDESL RAYLAFVIAF AVLIVPFKFY LFCFCFVFFY ALLGVTDAEA KILLQNMESK
AAELVSALKN SNLSIDAKIF HLNGVKSDIK QKNVPEDAVP AIFESSRLSI ASQHSSLLSA
GFSTLGHLLK RLFIQDQAYL ISVQARILYP ILLERLGDHK ERVRAQAAQA FTDLWPAASA
DVEHYVLETA LVGKNPRAKE MSMIWLSNMT KNHGLLFRSY VSSLVACLED ADSVVRDTAK
LTVVELFQNA SARAKADLST KFAEQNVRKS IVNAIIAGIG STLVEAGPSS RPASRVQMSS
SRADDAFRPA SRTQKSTVEA GPSSRPASRV QLPSSRADDT ILPVSRAQKS TVEPEQPLRP
VSRVQKRIVE PEQPLRPVSR AQKPAVESEQ PLRPASRAHK PALESEQPSR PVSRVQKRPA
SRADGNTAQA EAASRPSSSD SEKVVPINVT SSRHIDDMVR TMSPHFEGRE TEENWLHREK
SVIDLRRLTH GNAPQAFPQA FIAAMKTLLD GIFKVVNSLR TTMSTNGCLL IQDLAKICSS
KIDPMMEIIM QNLLKVCANM KKITAQNGNT TVDIVIGHVS FTHRILQHVS SASLDKNVQL
RLYSTGWLRT LINRQAHHKS SIEHGGGLDL IDKGIKKCLS DANPAVREAV RSTFWTYHRV
WPGRADSILS TLDAKTRVML EKAPANPNID YLPSTKTSTT TRQGPAVNTP AIAGRSALKE
AIAARKKAYL APANARPDTP PTASTSSLSS APLRSDAPPT ASTSSLSSAP LRSDAPPTAP
TSLSSAPLRP GVKARRVESQ IYEDPVVPPV PTTPTAKDED FVVPPAPTTP KAKDEDLVPP
APTTPTANDE DPVVPLAPTT PTTVFHIDTP VRSVSPAHST IYRPIKAVEP LLPAGATNVN
GSPSPKRTRI PVLHRSGPKN ALQELSKNEP AHRDNRPRLP SLPRMPSLHI ERTRRNSGAG
TSVDDSRHCK RFENAQKKFE QRKRSISPRS KDPAKGREML EKGVHRIRSK SMDILGYRKM
QGLIEYHDSF LREGSQCEDL LDALLDELTS TPDATHQSAG RALDLKTQVL QTVRYLLRNI
HTRHAPRVLL AILQATYFYE PSAHIFTEIS ATAEYIITAY FSEELALLRE QALASSVFLT
APEPGTRRQA TQMCVQLHAM AANEEDFWRL VGCPGGNTKN LLMYYIARQ
//
