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Database: UniProt
Entry: A0A319C1X1_9EURO
LinkDB: A0A319C1X1_9EURO
Original site: A0A319C1X1_9EURO 
ID   A0A319C1X1_9EURO        Unreviewed;       589 AA.
AC   A0A319C1X1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=TOG domain-containing protein {ECO:0000259|SMART:SM01349};
GN   ORFNames=BO82DRAFT_385322 {ECO:0000313|EMBL:PYH79084.1};
OS   Aspergillus uvarum CBS 121591.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH79084.1, ECO:0000313|Proteomes:UP000248340};
RN   [1] {ECO:0000313|EMBL:PYH79084.1, ECO:0000313|Proteomes:UP000248340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH79084.1,
RC   ECO:0000313|Proteomes:UP000248340};
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}.
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DR   EMBL; KZ821722; PYH79084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319C1X1; -.
DR   STRING; 1448315.A0A319C1X1; -.
DR   VEuPathDB; FungiDB:BO82DRAFT_385322; -.
DR   OrthoDB; 1369289at2759; -.
DR   Proteomes; UP000248340; 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:UP000248340};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          58..301
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REPEAT          162..196
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   DOMAIN          366..589
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          301..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   589 AA;  65707 MW;  0C6D5BD080F15F9D CRC64;
     MDDRHWKAVV TAAVLTSILH IGDILPFLGE FLIKLFWILR TSAVTFCVLF TVLTLSGDEV
     RRLFTILLNI MEAKALELVE IARNNYLSLD AKTGALVAYK SEIKQRNVPE AAVPPSFEAA
     RIFISSPHGN IITPAFNMLS HLTRRLFIQR QPHLIANYSR NLQPLLLEKL GDNRERVRAQ
     AAQAFTELWP AASAEVEHYV LDTALVGRNP RAKEMALIWL SNMSRTHGLR FRQYVAKLVN
     CLEDADPAVR DAAKLTVVEL FGTASGASAR AKADLMNQLS IRSVRKTIVN AILTQIDLDP
     ADLEPNRGPM HRADRITQRP HSSLEAHPRP MSRADGHKHP LPQHSSEATP LTPSDGDSVE
     PLNVSSSREI EDIIRAMVPH FDGRESEENW AKREKNVMLL RRLVRGNAPV AHSNTLITAL
     KSILDGIFKV VNSLRTTMAT NGCLFMQDMA IYCGPKIDPM MEIIMQNLIK LCAGMKKITA
     QNGKMTVETV IQHVSFTPRI LQHVFGASQD KNAQLRLFSA DWFKIILNKQ AANRSSIEHG
     GGLELLEKAF KKGLADANPA VRQAMRGTFW VFFGMWPNQG NEASQLAPP
//
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