STU1_NEUCR
ID STU1_NEUCR Reviewed; 1136 AA.
AC Q7S9L2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Protein stu-1;
GN Name=stu-1; ORFNames=NCU07693;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; CM002239; EAA33043.1; -; Genomic_DNA.
DR RefSeq; XP_962279.1; XM_957186.2.
DR AlphaFoldDB; Q7S9L2; -.
DR STRING; 5141.EFNCRP00000008032; -.
DR EnsemblFungi; EAA33043; EAA33043; NCU07693.
DR GeneID; 3878427; -.
DR KEGG; ncr:NCU07693; -.
DR VEuPathDB; FungiDB:NCU07693; -.
DR HOGENOM; CLU_004060_0_0_1; -.
DR InParanoid; Q7S9L2; -.
DR OMA; TMSTNGC; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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; 2.
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..1136
FT /note="Protein stu-1"
FT /id="PRO_0000272292"
FT REPEAT 95..133
FT /note="HEAT 1"
FT REPEAT 167..205
FT /note="HEAT 2"
FT REGION 524..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 123636 MW; D550B5E2D5219A29 CRC64;
MAERITDEQV ADLLAILRTD ASVDAKANRI TAVKTSIKQH NVPATCFAPL FEALHIASTA
QHPVLVNAGF TTLNHLLARL ARQDPKFLAK EAPHTLPVVV DKLGDQKDKF RQIAVQALTT
LYKVAPVDVE RSVRNIAMVG KNPRAKEMSM HWLLQTHQEQ GLQFRAYVPT LMELLEDADG
SVRDVAKTTV IELFKNAPNT AKSDLKRQLK NFKVRPAIEQ VIVKELNNPS SSVSSHQNDM
MDLDEPVMPT RAPAPASIRT NLSASVPTLA SERPLTPGLD SRPEPVEPQF VNTQRELDDI
FRDMHMFFDG RETEQNWLKR EESMTKLRRL IAGNAVSDFH DSFLAALRAL LDGIIKAVTS
LRTSLSKEGC ALVQDIATAY GPGMDPMVEI LMQTFVKLCA ATKKISSAQA NATINTILGK
VSYTNRLMQH IWMACQDKNV QPRLYATEWL TTMLTKMAHH KNQVEHTGGL DLIEKCIKKG
LADANPGVRE KMRATYWTFS GIWPARATHI MNELDLTAQK LLQKDPHNPN AHSRTETGGA
RPGMGLSKSV MGAPKPSVRD AIIAQKRAMA SSKNQPPRPG SAMAHFSPVG TTRNVSSTSQ
ASVASASTAS AVPAPTKSAF GASSGGLSGA PMRPGKRRPE VAARPATAGP YSVRNEVPPA
EPASPPSKPR IKTVTSPKTQ TLVISPKKAI PRPQQGHSTN SSESGIPIPV SGISSPTKPT
SAFGLRSPRS PLAPELPPSS VIASPSRVMP DPAQIPLPES SPSKDEELSL VVPGSVLPTQ
KTPSPTEESQ QPQIAIVPIE AVEIVPDSPY RSVQVYEDPY TAGQTQPQST YTSPVLEPKP
VNEGAATSPP PQPSYDGENG HDMGEIPIPS SPERTRQNSR LLDSGISKVE TKSLDVHGFR
KLQGIIRDPK GGAIFTDDKF NALLSGLFEF LEAHPSEIPH VPAEKQQDVK AQILATIKLL
LKKMRENFRP HVSRGLDSLL RARAAYDSRS HIVSGMELLA DELITLGDPT EITLVLANTL
REALLDKDQQ HNTAARSLSM GMHVLKEVVE SSANSSTPFT PTEQELDTLA GLAAKCLESA
DSAVRMDAVQ LCVALHAKVG DQRFWDAVKR EGVRDDPKSL ITYYIVRRQR EVGTNA
