ID X0CPL1_FUSOX Unreviewed; 1133 AA.
AC X0CPL1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protein STU1 {ECO:0000313|EMBL:EXK92769.1};
GN ORFNames=FOQG_05801 {ECO:0000313|EMBL:EXK92769.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK92769.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK92769.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK92769.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXK92769.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=54005 {ECO:0000313|EMBL:EXK92769.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (MAY-2012) 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}.
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DR EMBL; JH658370; EXK92769.1; -; Genomic_DNA.
DR EMBL; JH658370; EXK92770.1; -; Genomic_DNA.
DR eggNOG; ENOG502QT5T; Eukaryota.
DR HOGENOM; CLU_004060_0_0_1; -.
DR Proteomes; UP000030663; 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; 3.
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:UP000030663}.
FT DOMAIN 10..228
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 285..516
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 878..1129
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 226..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 123326 MW; 34C41AE75D43FDEB CRC64;
MADTKLTDQQ VADLNTILRG DGSLDSKVQY VTIIKSGIKQ HNVPESSVSQ LFDGLRAATT
SQHAALVNAG FTALNHLLTR LSRQDPKLLS KEAARTLPIV VEKLGDHKDK FRSLASHSLV
TLYAVAPADV ERFVRNSAMN GKNPRAKETS MSWLLQMHKE NGLPFRGYVP VLMELLEDAD
GMVRDAAKNT VIELFRSAPN AAKSDLKRQL KNFKVRPAIE QAIVKELAPT SGRPETPAAE
ATAPAPRPAL SASTSSVAAA ERPITPGIET KPETLEPLYV NTNRELDDVF KEMAWFFEGK
ESEQNWLKRE NSVNKLRRLN VGNVPSDFPD TFLVGVKSML DGIIKAITSL RTSLCKEGCA
LIQEMANTFG PAMDPMVELL MQCFVKLAAG TKKISSQLAN VTVDTILSKV SYTPRLMQHI
WMACQDKNVA PRIYATGWLK TILKKEAQHK HHIEHTGGVE LIEKCIKKGL TDANPAVREK
MRSTYWAFWG IWPAKADAIM ADLDGTAQKL LNKDPSNPHS PKKGETAARP GLGLSKSTMG
TSKPSIREAM MAQKKANAAK NLPARPGSAM AHLSPVKTTT SSTATAASKP SGTRTRPETG
GMSGAPMRPA RRRPEMAARP ATAGPYSVRD MDAGSPESIR SKTPKPRETT PKRTAPRPRP
GHASHASESS LASPTSVRSG TKPAASPRTS PTKLKQSQSA MLPMSSPSRA NEDFTLVVPN
MANLRAMQKP APEPHQRAPQ ANQEIPSELT TPVLEDSPHI VPEAIKEAAP VSEPETAPEP
AAEAETQSAD QPMEEVAEPP VAVSEPVVEP TPQPSETMQA EPVSGAPGST LQVYEDPFTD
EQPSPKPTFN VPVLEDKPIN ADAANLPNAR AQSPVTQDVE SSERTKQSSR LLESGITRVK
AKTLDVHGFR KLQSLLRDTK GIFTDDKFEA LLIGLFQYLE DPLSGVSTEK AQDIKAQILA
TIRLLLRKER DNFQPHVSRG LESLLETRSA YDIRAHIVSG VEVLADELVT IGDGSEIVVV
LTNRLQNVDS STPEGSRMLS TGMHVLRSLL DKRPNFVPTD TELGQLASLA GRCLVSTDSG
VRMDAVQLCV ALHSRVGEQV FWNALKDVQD DPKSLITYYI VKRQREQTPT IAA
//
