STU1_DEBHA
ID STU1_DEBHA Reviewed; 1529 AA.
AC Q6BK07;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein STU1;
GN Name=STU1; OrderedLocusNames=DEHA2F25872g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR382138; CAG89883.2; -; Genomic_DNA.
DR RefSeq; XP_461464.2; XM_461464.1.
DR AlphaFoldDB; Q6BK07; -.
DR STRING; 4959.XP_461464.2; -.
DR EnsemblFungi; CAG89883; CAG89883; DEHA2F25872g.
DR GeneID; 2904218; -.
DR KEGG; dha:DEHA2F25872g; -.
DR VEuPathDB; FungiDB:DEHA2F25872g; -.
DR eggNOG; ENOG502QT5T; Eukaryota.
DR HOGENOM; CLU_261691_0_0_1; -.
DR InParanoid; Q6BK07; -.
DR OMA; RNYQPRS; -.
DR OrthoDB; 513064at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 2.
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; 2.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..1529
FT /note="Protein STU1"
FT /id="PRO_0000272288"
FT REGION 266..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1529 AA; 172469 MW; 94B0BB494BE2A620 CRC64;
MSSQVISASR LYQIVASPTS DNDAKSRSIN ELKTHVKKDF VDIKQVPKYV EALSIAVDIS
DTGISTSSFS VLSHLVKRVS MQDSSGEVLK SQSYLVLPII INRLGDIKAS ARISAKKALE
AYWFSAPKEV EDSIIDIAFS HKNSKVINES IIWLDHIITN VNPHFKINLF LPHIVKLLRL
NSDSDEVLIE NIKTLFKDYY SLKHNRLYKF DLSKEFDTQK IPSNVHESII SQIGTSSSIL
MKQATPDIGL DHNFISAGTT RVTVNSMGRD KGTISSNSST PASLSSSTMS RPKSRTNFHN
YTKSISPSQE DEQITKPSVH NSAFNKYNTN QMSAPAKPVA MVNENSNEIN SEISPEIEKI
IAKTFTYKID SSILPLDVKD VDDLCGTINE LLPIFEGKET EFNWGMREKN IIKLRSIIRG
NSSRLFTNEL TSYLKESSES ICKAVTSLRT TLSSHGCHFL KECAIILKEH FDPLVDSYVP
HLMKLCSATK HIASSNANMA LCAIFINVPY NYRLLHKILV SANEKNVQPR SYSGIWLQVV
LVRFHDTSSF SYRGSNSISG LDTSIKILTK LLADPNPNVR QVAKDTYWCF WDKFPSEAES
LLTRLDTNVV KAIERSKPRT ITSRNQPSTL SSLTARKARP SIKESIIARN KELRKQKDQT
SISRPSSRIN STSSPCPPDN DYLQKHDKPQ FSTLDSGKFS RLGVAKRTPS TSSLSRVESN
QDAITRKVSD SVSSNAKKHN DSQGINADAQ IQNIETMKST YSVDDNSSNR TNMEQTNKFE
SFDKQSDPIL KFLSSNQKEF ITEGINLLKY AIMGEEDLSS EVNGLLKKIS VRNQDLLKPL
FLSTDNLFKK TYQFFSFEDF FRVCCILIHT IDTRLVDLIV SIAGVDDIYE SAIKLISYTT
NLGNIIDDSD LTMQIIRFKS IIVRSIIEFL NQGLDKIPIS DSYFSKLVTN LFELVSLVKS
TGLYKSFCEL LIKLYSINPT LFTSELQMIA TSTREEVEYV VGIDDVLDLN RGHAINFTTQ
YELTRVVPGN NLRKMSPLKA PSDLTMVVPV EKELFEDDNI DIDSKIQSES ANDTGFRTPP
KLAGNHTSPI HSERSTIIET DGNISDNVEE YVNDAMDVDQ NPSEEIVNGL KNDIEMHNDD
NKVKEKTSND MSDSLPLIDE SDNIFVEIDS DSASRKPDLF TKFAQHDNSS ELVENFAQVK
ITELSKQRLR NNDPIKKFID KVDPLNKISL KNKPISIYED VNFKGSPQKV KDYSYTELNW
FNFQLAKLAM DKEDNQEIDY CIEDFKSLCD NLSSKKIEGK EFVSVLNYLQ NIQISNAEFS
RYFQSSGHSL IENSLWNFFD NHINLPVSKK LSGLILLKQL LINRLRVSLD RLWNLLVGLS
SESSSSVDEL SLAISEAFDE MLAGLFSSEI IFARILTTLE NAVLERESFS LPFILECLSK
VLSTNAVSLL IDEKLIMRID NVLSGFMNDE EVEIRRCVIS SYGKLLKASR ISSSIETNED
IRSEYSVMDD ILKKLSIPQK KLIEYYSQS
