ID R9XIW1_ASHAC Unreviewed; 955 AA.
AC R9XIW1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Protein STU1 {ECO:0000256|ARBA:ARBA00016012};
GN ORFNames=AACERI_AaceriACL132C {ECO:0000313|EMBL:AGO13467.1};
OS Ashbya aceri (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO13467.1, ECO:0000313|Proteomes:UP000016920};
RN [1] {ECO:0000313|Proteomes:UP000016920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}.
CC -!- SIMILARITY: Belongs to the CLASP family.
CC {ECO:0000256|ARBA:ARBA00009549}.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC {ECO:0000256|ARBA:ARBA00025722}.
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DR EMBL; CP006025; AGO13467.1; -; Genomic_DNA.
DR AlphaFoldDB; R9XIW1; -.
DR HOGENOM; CLU_008401_1_1_1; -.
DR OrthoDB; 5477703at2759; -.
DR Proteomes; UP000016920; Chromosome VI.
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:0061863; F:microtubule plus end polymerase; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:InterPro.
DR GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR GO; GO:0007051; P:spindle organization; IEA:InterPro.
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; IPR048492; Stu2_CTS.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR PANTHER; PTHR12609:SF0; CYTOSKELETON-ASSOCIATED PROTEIN 5; 1.
DR PANTHER; PTHR12609; MICROTUBULE ASSOCIATED PROTEIN XMAP215; 1.
DR Pfam; PF12348; CLASP_N; 1.
DR Pfam; PF21042; Stu2_CTS; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 2..243
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 298..542
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 479..517
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REGION 263..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 714..797
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 549..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 106081 MW; 2BB11A39C732A450 CRC64;
MTEDEDFTKL GLKQRLGHKS WKARQHGYQE LERMFERSSV LDVASEVSAW WEAPEHFGRF
ITDSNVVAQE SAVGAMQRML ELMGQLERVP ETGALRAQWV PALVEKGVSS SRAGTKAKAM
ECILMLASFD TSVRQTMELM LPFAGNKLPR LVSSLMAAMG QLVCSFGFVN MKNDFWSEVL
APLPRLAGHA DRSVRAETMN FILEVYKWTG KPFLQDMLLE KLKPIQQKDL DKLFGNYDGT
IPPTEQPRLF HWQVLQRQRE AAAGVDDDGD TMMGEGQGGA QPGGESGAAP AVLADPFTLL
KPSSIVKNFP ADFEKNVKSV KWKERVEALQ QVYDDLLKPA KKLDQTDDYS FYARSLAQIL
SKDANLQAAT LAANSVAHMT TALREGIAPY GHMLLEGLLD RTKEKKPSVS EAVVEALDLL
AQYYGVDNCL EPTIEHMKHK IPQVKMESTN FLTRMLQKQW KPTAARLKDE VIMRMMPDIV
PIIVKIVNDT QPSLRDAGFE CFATVMKLFG EREFTDELEK LGSLKKKKIY EHFEKIEVKV
PPPVQKPQQT RAPQTQRQPQ HSPHYSQRSL QNQQSPQQHQ LQHPHSPQAQ RSNNHQNSAS
NFSKTLPHIV KTPRAAASSL SPSVDVRHFD SPPQTLRTPT ASTIPTKRGP SSPLKDKNIL
NNGGLNTKPR LVNRSQTHST VRASHFNPMS SLPPSSNNSV AAPSVVPPAV LAELDELKGA
KAKWNKERQE LMAKLTSFQT QTSQLNSENQ MLQDQLNDVQ LALNEKTMLL RSKDLQITKL
KNRLATLESE LDTALNSKHS PDTPAKSVLE GIHAISPSHG SAQSAGVYGG SNHSDPCISI
QPHNPQQIRK TSGGSFRSNA GLTSRFSPLT SSVRVATSSE SSDDLPRRVH SLHIMDTTNA
VAGSTTTNGS SASLLSEESW KRAAEVTNQL KARIERMRAK TRGLTMDAED SYRQN
//
