ID A0A1V6SFF4_9EURO Unreviewed; 1310 AA.
AC A0A1V6SFF4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=TOG domain-containing protein {ECO:0000259|SMART:SM01349};
GN ORFNames=PENFLA_c064G10072 {ECO:0000313|EMBL:OQE12741.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE12741.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE12741.1}.
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DR EMBL; MLQL01000064; OQE12741.1; -; Genomic_DNA.
DR STRING; 254877.A0A1V6SFF4; -.
DR OrthoDB; 1369289at2759; -.
DR Proteomes; UP000191342; 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:UP000191342};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..215
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 92..126
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 317..563
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 227..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1310 AA; 143140 MW; E9AE99F97CC73D9F CRC64;
MEAKAAELLA AFKNPNLSVD SKIAYLSSVK SDIKQKNVPE GAIRPIFETL RLAVGSQHYS
VLGAGFSTLG HLLKRLAIQE QQQWIVHQAH SLYPILLERL NDPKERIRAQ AASIFTELWP
FAGNEVEYHV LEVALVGKNH RAKEMSMLWL ANMTKNHGLL FRQYVPSLVS CLEDADSAVR
DTAKLVVIDL FRNGPARAKS DLQKQMAARS VRKSIANAIL SGIGLGSVEP ETASSTRPIS
RAERSISVMS SRSHAMEQTD DEMEPAKSRP ASRAHRERPT ASSAPAEPPI VNRPRTPAPT
PAPQQSLPDE GGLEPFDVAS ARDVDDLVRD MLPWFEGKES EDNWLKREKN VILFRRLTRG
NAPHDFSQTY INAVKTLLDG ILKVLNSLRT TMSTNACLLV QDIARTCGPR IDSMVEIIMQ
NLLKLCSALK KIAAQNGNAT VEVVIQNVSF SIRILQHVSF AVQDKNVGVR LFATGWLKAL
IIRQAHHKSA VEHNGGLDLI EKSITKGLGD ANPGVREASR STFWTFYGVW PERANVIADT
LDPKSRNLLE KDSSNPNPPS KGAPALPAKS PAKSRSALQE AIAARKRAQM PSRPESAQPT
FAEAKQPAPS SKSTRSVPTG APLSSLSSAP MRPGMKPRRA EISRPATADP YARRPESRAQ
SSSTQSTRQA TTSPRAVRSK PSTPTSQAPL TAPRTRPREP AQAATTKGRP KKLDLSKSKS
HNDLLAAASR ARSDSNESLA NQPSARTPRH GNYLSASEDQ HSPASTELES PPFNASQPLL
YSAPHGPHAD SVPLEESEPI MLEEPVITVP SPSIPEPDLA VSPAPVSPVH QHPDLEFGSG
PVSAVKPRPE SMVIYEDPTT PTGDINETLG HAASVGNPTP SKPSPSRSDQ PEHGQAETQP
IPEDISAPVV ASARKPTPDL APTQESGLNF EVRTPSPTRR APLQPSPSPT RGRVQPAASN
ILDIDVVLPQ EPHAGTNGTD GNNENATPRL TKTVDLPPAP RYPAKPSALE EVTVNEATPR
SPEARQRSFE SIPQSLSQST LSQSTMSDDS TRRTRKWADR HRSPSPRSKD PVNAKEMIRK
GLARIVSRTM EPSGYRKLQG LIQYHGDEIV SQTQDYNTLL EALIAELEAI PSNRKDHDVK
TQVLATIRSM LLRTREHFHP YDTRAMAAII RVRCHYESTS HFVTCLEEVA DKLVFLTLPQ
TAIIGVLQGL DLGADAENDE TYRSTIMGLS TIQQSLSRPG IDIDDELLAR IGAVVMQQLG
HPRPGVRKNA TELCTFLNIT FGSERVQKVT QPPREGSLNL LTYFMARRTQ
//
