STU1_PHANO
ID STU1_PHANO Reviewed; 1207 AA.
AC Q0UQJ8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Protein STU1;
GN Name=STU1; ORFNames=SNOG_05966;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Microtubule binding protein that promotes the stabilization
CC of dynamic microtubules. Required for mitotic spindle formation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with microtubules. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT87030.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445332; EAT87030.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001796355.1; XM_001796303.1.
DR AlphaFoldDB; Q0UQJ8; -.
DR STRING; 13684.SNOT_05966; -.
DR GeneID; 5973232; -.
DR KEGG; pno:SNOG_05966; -.
DR eggNOG; ENOG502QT5T; Eukaryota.
DR InParanoid; Q0UQJ8; -.
DR OMA; TMSTNGC; -.
DR OrthoDB; 149571at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0060172; P:astral microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR034085; TOG.
DR Pfam; PF12348; CLASP_N; 2.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1207
FT /note="Protein STU1"
FT /id="PRO_0000272293"
FT REGION 504..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 131501 MW; 122699ADB55D1F77 CRC64;
MPDMLEQTNA LLAALKKPST NVDQRLQLFS NVKSNIKHNR VPEECQAPIF ECIRIAISAT
TSATLVSTGF STLSHFIKRL QLQRETAVIT SQSSKLCALL LEKLGDARES HRSASLQILA
DLHPLCPLEV ETLIHNAMKG TNARAKDTSM TWVVKMNQTE NLPFRAYSAQ MIANLEDADA
GVRDTAKHAV VDLFTSAPEH AKANLKKQLV STNVRKAIAT YITAHLDGAA TGGAHEEMPP
PPPAVRERPL PTQRAQTLQP DHGIADALAA EQPPPTEAVT MDPIHIYTQR ELEDIFRDMA
PPFEGRESEG NWLARDKNTT KLRRILMGNA PAEFPGAFVA GIKSLLEGIL KVANTLRTTM
STNGCQLVQE LAKTLRHAID PWVEILLQCF IKMCAATKNI AAQNGNVTVE AIISNVSYNN
RILQHVSFAA TNALRASWVK TLIRKHKAHV EHSGGLDTLE KIIRKGVTDA NPKVREAYRS
TYWTFALVWP QRAEAMFETL EKREKTALEK DPNNPNASLA SSQSSAVSSF SKSVGAGAAR
NALKEKIAEQ RRAKMAASKV PERPMSAAAT YSPVKSASTK SLSARTASTA STASNGPARP
PSAMSGESTK SALKNSSGTG SLMSGTVRRP IRRPELNRPA TADPYAVRRA GNGKTTPSMT
PEKTPAVTTT KKSVAPKSSV RPRAQTQNSP NVSPIRSRSR LGQSTTVQKT ASASSRQASP
APSASKDEDL ELTIVKPFVR SQSHHDPGTI PFRQRNGLDK SAVFDNETVL SGDEDNFTMV
IPNLARPTAQ SIHHTPPKTH SPSHLSAPSP RASMLRSPKS MGDINGFGFR SSTRSPRVRS
PDRPSTRGTD AQEGVQVFED PFVGDEPAAV EHEVEKPVLG ELPINEKNIE RRPSNESISS
DTVMGNASED RPRGHHKTTS TGSVLYSESN DTNNAEVLKN RQLLASGIKK IESRTVESHM
FRRMQDMIRS NHEIWGANDE NFGCLLLACL DFLEVPTEEL KTTPIKVANL KVQALATIRA
MLSLYRKETA KYFSRVLCTV LQTKAQYENT SHIAIDLETT AEEIVRYGQT SDCLNAVLAL
IEDLPSSTPT SSPSSKSSLT SLPGAGQTRT ATMALSTLAA LIQISGAKNI TLSPDQTSRL
GKLAVRCMDD QDADVRKSNI EFCIALHERI AAPAGEQEND GFWRAVAGAR EQHLNLLTYY
LAKRRAA
