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
//