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Database: UniProt
Entry: A0A175W880_9PEZI
LinkDB: A0A175W880_9PEZI
Original site: A0A175W880_9PEZI 
ID   A0A175W880_9PEZI        Unreviewed;      1139 AA.
AC   A0A175W880;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Protein STU1 {ECO:0000313|EMBL:KXX79775.1};
GN   ORFNames=MMYC01_204384 {ECO:0000313|EMBL:KXX79775.1};
OS   Madurella mycetomatis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX   NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX79775.1, ECO:0000313|Proteomes:UP000078237};
RN   [1] {ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   van de Sande W.W.J.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXX79775.1, ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   Van De Sande W.;
RT   "Madurella mycetomatis genome sequencing.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXX79775.1}.
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DR   EMBL; LCTW02000077; KXX79775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A175W880; -.
DR   STRING; 100816.A0A175W880; -.
DR   VEuPathDB; FungiDB:MMYC01_204384; -.
DR   OrthoDB; 1369289at2759; -.
DR   Proteomes; UP000078237; 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; 2.
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:UP000078237}.
FT   DOMAIN          1..218
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          283..521
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          224..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1139 AA;  123325 MW;  030749DB1108310C CRC64;
     MAEKITDKQV ADLIAILRTD ASIDAKVQQV TLIKSGIKQQ NVPEPCILPL FEALRTASSS
     QHAVLVNAGF SALNHLLTRL SRQEPKYLAK EAPRTLPLVI ERLGDQKEKF RQLAIQCLIT
     LYKVAPQDVE RFVRNTAMAG KNARAKEASL HWLLQMHQEH GLQFRVYVPT LMELLEDADG
     MVREAAKSTV IELFRNGPNA AKSDLKKQLK NFKVRPGIEQ AIIKELNPTS SAPVSQSDSL
     DEPPATRPTL AASVSSLVER PVTPMLDGRP DQVEPTYVNT QRELEEMFRE MHLYFDGKET
     EQNWMKREES ITKLRRLIAG NAATDFGEHF LSGLRALLDG IIKAVVSLRT SLSKEGCSLV
     QDIARAYGPG MDPMVELLMQ TFIKLTAATK KISSQLANAT VDTIISRVTY NARIMQHIWF
     ACQDKNVQPR LYASGWLKTL LHKEAHHKNH LEHTGGLDMI EKCIKKGLGD ANPGVREKMR
     ATYWTFAGIW PARAEAIMSG LDPTAAKLLH NDPHNPNPTA KRPEGGARPG LGLSKSTMGT
     SKPSVRDAML AQKKAMSSKA LPARPGSAMS HFSPVRTVST SSQASGTTTS SARTRPESVI
     GSTGGLTGAP VRPGRRRPEM AARPATAGPY SVRSHDQPST EQSSPPQNHK PKAVTPKSIT
     ASPKRTVPKT ARQVVPANES QHPTPTRAGT PKSIASPRAT PSRIAQPPVA PVSSSPSKAD
     EDFTLVVPTV HVIQSTPYEK RPSSPAETAS TAPSPSNTPS RTARLASAAP AAPATVPEAI
     ARPSVTAQSL LGSPLQPVQP VLAAPTKPPQ SLEVYEDPFT ADDQATPRPS FTGPVLEDKP
     INEDAATLQQ TSQAEHHNGD ANEDTCSPDR TRQNSRLLDS GISKVQQKSL DVHGFRKLQG
     IIRDSKATSL IPDDKFDALL LGLFQFLESP LSHVSPEKSQ DVKAQILATI KLLLKKMREN
     FRPHVSRGLE SLVRARATYE GRTHIVSGLE LLAGELVALG DASEIVMVLT RMLRSMDVDG
     GAGTDDGATD AGAGGAEARS LSMGLHVLKE TMESKGGLAG YVPAEGELAA LAGLAARCLE
     SLESAVRMDA VLLCVAIHAR VGDARFWEAV KGVREDPKSL ITYYIVRRQR EMGVVGQAA
//
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