ID A0A395NUP1_TRIAR Unreviewed; 1088 AA.
AC A0A395NUP1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Heat repeat containing {ECO:0000313|EMBL:RFU79842.1};
GN ORFNames=TARUN_2369 {ECO:0000313|EMBL:RFU79842.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU79842.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU79842.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU79842.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFU79842.1}.
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DR EMBL; PXOA01000137; RFU79842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NUP1; -.
DR STRING; 490622.A0A395NUP1; -.
DR Proteomes; UP000266272; Unassembled WGS sequence.
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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
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; 3.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000266272}.
FT DOMAIN 4..229
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 285..526
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 831..1087
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 256..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 118458 MW; 810978483E4523C4 CRC64;
MADTKLTDDQ VANLTTVLRN DNVHFDVKVQ YVNTIKSGIK QHNVPETCIP QLFEGLRSAS
ASQHVALATA GFTALNHLFT RMSRQEPKHL VKEAARTLPL VVEKLGDSKD KPRALALQSL
NTLYSVAPAD VERAIRITAM GGKNSRAKEA SMQWLLETHQ QHGLPFRGYV PSLMELLEDA
DGMVRDTAKS TVIELFKNAP GAAKSDLKKQ LKNFKVRPAI EQAIVKALAP TGPRSDAPSE
AAPAAAAAAA RPALSAPSSF APSERPITPA VDSPADSVEP QYVNTHRELD DIIKDMTPYF
EGKESEQNWM KREQSIVTLR RLVAGNAPAE FLDTFTAGLK TLLDGIIKAV NSLRTSLSKE
GCSLVQEMAI AFGPAIDPLV ELLMQTFMKL SANTKKISSQ MANSAVDVIL SRVTYTPRIM
QHIWGVCQDK NVQPRTYASG WLITILKKEA HHKNHIEHTG GVDLMEKCIK KALGDANPGV
REKMRAAYWT FWSVWPARAD AIMADLDPTA QKLLNKDPHN PNAGKKVEAP VAAKPGSGFS
KSTNAASSKP SLRETMMAQK KATLSARNMP TRPGSAMSSF STASPSNSST QLNPSVPKPP
ARPRGEAGTI SVNAGGMSVA PMRPARRRPD VARPATAGPY SVRDQPSSVE AHSPEGGKSK
AASSSSSKSE KLRESTPKRP SSRAHHGHAS HASESSIVSP TTVRPTGIPS PRASPARLRH
SQTMIHTMSP TRATDDLTLV VPTLSSIQSA SPRIESPRQP IFTPSSPPSV LPSEIPLSPR
TELPSRTLKV YEDPFTDDQP TPRPSLPTAP VLEEKPINED AANIQRPTQP PLSDESEAPE
KNGQNARLLD SGITKIKAKT LEVHGFRKLQ SLIRDTKTVF TDQRFEALLI GLFQYLEDPL
TDLPADKAQD VKAQILTTIK LLLKKERRNF QPHVSRGLES LLQTRGRYDT RAHVVSGLEL
LADELVTLSD GSETAVVLTK RLQSCSDSTT EGCRTLSMGL HVLREMLDKR PEYVPTSKEL
LQLTGLAGRC LESTDSGVRL DAVKFCVALH SRVGEVAFWE AMAGIKDDPK SLITYYIVKK
QREDGVAS
//
