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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//