STU1_COCIM
ID STU1_COCIM Reviewed; 1244 AA.
AC Q1DS65; J3K9S6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein STU1;
GN Name=STU1; ORFNames=CIMG_06848;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704912; EAS31369.3; -; Genomic_DNA.
DR RefSeq; XP_001242952.2; XM_001242951.2.
DR AlphaFoldDB; Q1DS65; -.
DR STRING; 246410.Q1DS65; -.
DR PRIDE; Q1DS65; -.
DR EnsemblFungi; EAS31369; EAS31369; CIMG_06848.
DR GeneID; 4562036; -.
DR KEGG; cim:CIMG_06848; -.
DR VEuPathDB; FungiDB:CIMG_06848; -.
DR InParanoid; Q1DS65; -.
DR OMA; TMSTNGC; -.
DR OrthoDB; 149571at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
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; -; 3.
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; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1244
FT /note="Protein STU1"
FT /id="PRO_0000272286"
FT REPEAT 87..124
FT /note="HEAT 1"
FT REPEAT 159..196
FT /note="HEAT 2"
FT REPEAT 1038..1075
FT /note="HEAT 3"
FT REPEAT 1126..1163
FT /note="HEAT 4"
FT REGION 232..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1244 AA; 137113 MW; 3B2E2DC3D27D1288 CRC64;
MDARATELLA TLRNGNVSVD VKTTSLAKLK SEIKQKHVPD AAISPLFESF RLAIASQHYS
LSSAGFSALG HLLKRLTLQE QHEAIALQGR ATYQLLLERL GDHKERIRSQ AAQAFTDFWP
AASADVEHHV LGAALIGKNA RAKETSMVWL AKMTREYGLL FRIYVPALVT CLEDADGVVR
DTAKSTVIEL FQSAPPRAIS DLKKQLIQNN VRKSIATSIL SSLGANIVAD SETSSSFQSQ
SRSDITRPAT SFSHRREEVP RSQSVLSMRS HSNADVHNIP KIDAAFKSQS KPTRSGHSSK
DPTLSHTASS ESLPAPRQDT TDGEGVEPLY INSHREFDDT IREMLPHFEG KESEQNWILR
EKSIMTLRRL TKGNAPHDYQ QYYLAGIKSV LDGILKTANS LRTTLSAAGC YLLQDIARTC
GPAIDPMVEI LLQSLIKLSA ALKKITAQNG NVTVDVIIGN VSYTARILQH IWGACQDKNV
QPRQFATGWI KTIIIRQGKH KGSIEHSGGL DLIEKCIKKG LGDPNPGVRE GMRGTFWAFY
SVWPERADVI MSALEPKSKN LLERDPNNTH RGVASQSFDG SRGSQPHSTK SSLKEAINAQ
KKARLAASSN VPSRPESAQS SFPDPKSGRP APRRPTGTST IRVPTGEKLS QSASLSSAPM
RPASRPRRPE LVRPATADPY SSRRSAAPTA QSKASSPSDS PQKSKSKLMT TPRSRNPLAR
PKSRMDNAAN VTNDKQRADP AATLAPKMRR RGPSEPDVVS AAARARIAIL SPSRTEGDFS
VASSQVKIDQ KAEEAFQGTP TRGIENGTPL PASPLRSPLK GAFSTPTRNR KSSDGAPPSR
IPISPSYSSR RSSEEPMLPR TPLDSRRSRG ESDEAASQIP APVDQSPIID AINSQSPGIL
KVYEDPQSPH SKHSIVLGDT VPKTPGSQAK VMPLEELPLN ESTTVPNRKH NQLPEHTPLL
QPSPILTPSS ENSHRRWKKV EGSERRRSLS PRSKDPVKAQ DMITRGLARI RTGALDVHGY
RKFQNLIKYH ESISKDDTKY EDILMALLEA LEKPDGDKGA PSGRSLDLKT QVLVTIRLML
VINREAFAAF YPRVMTAIIT ARKQYELTNH IVSGLEETAE DIVSACNPPQ VIDAILDLLE
TEERSFESYR MVAMGSYILS GLLRRLNNQK LYLSQAELER LGKFANENLR STQPDVRRAI
IDFCPELYDM VQSEDAFWSM VNSSVEDFRP LLTYYIMRRP EKIG