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Database: UniProt
Entry: A0A150GNQ5_GONPE
LinkDB: A0A150GNQ5_GONPE
Original site: A0A150GNQ5_GONPE 
ID   A0A150GNQ5_GONPE        Unreviewed;      1154 AA.
AC   A0A150GNQ5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=CLASP protein {ECO:0000313|EMBL:KXZ51447.1};
GN   ORFNames=GPECTOR_12g410 {ECO:0000313|EMBL:KXZ51447.1};
OS   Gonium pectorale (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX   NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ51447.1, ECO:0000313|Proteomes:UP000075714};
RN   [1] {ECO:0000313|Proteomes:UP000075714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX   PubMed=27102219; DOI=10.1038/ncomms11370;
RA   Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA   Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA   Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA   Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT   "The Gonium pectorale genome demonstrates co-option of cell cycle
RT   regulation during the evolution of multicellularity.";
RL   Nat. Commun. 7:11370-11370(2016).
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:KXZ51447.1}.
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DR   EMBL; LSYV01000013; KXZ51447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150GNQ5; -.
DR   STRING; 33097.A0A150GNQ5; -.
DR   OrthoDB; 5478662at2759; -.
DR   Proteomes; UP000075714; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProt.
DR   GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:UniProt.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:UniProt.
DR   GO; GO:1902903; P:regulation of supramolecular fiber organization; IEA:UniProt.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
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; IPR034085; TOG.
DR   InterPro; IPR048491; XMAP215_CLASP_TOG.
DR   PANTHER; PTHR21567; CLASP; 1.
DR   PANTHER; PTHR21567:SF87; CRESCERIN-LIKE PROTEIN CHE-12; 1.
DR   Pfam; PF12348; CLASP_N; 1.
DR   Pfam; PF21041; XMAP215_CLASP_TOG; 1.
DR   SMART; SM01349; TOG; 3.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          6..226
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REPEAT          82..120
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   DOMAIN          345..577
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          701..933
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          218..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1154 AA;  122389 MW;  F9C2D44DADFEF666 CRC64;
     MSGWSDIKED LQVTSKQRLG LEGLEALLQQ TTLSKAELSE VVNLAPGLLS SSNPKVAQQT
     LEALNAVVRR ADTQLAPFAS TLIPCVAERL GDSRQPVRAQ ALDVLVSLFK TVKPELVLDK
     LSPFWHHKSW KVKHGLLEVV AEVVSTTGAS FLRGRDQNNA VLKQIVCMMD EPELAVREAA
     ADCLDELYRA APAAVVSTVQ ASNLRPAQQT ELLTRLGVPS ASTGAAPISD TGSKRASSGY
     TAVDVAASLE AGASQGLYTA GDFTSTARGR ISGSGQAGTS APAPASDAML SRPVEARRPT
     SNSSAGPSQA SAATGKRGGF KDGGGVTLDG ELPAPAPIPI ASERELREEL EAAVATLSLA
     PNTEWQARMT AMQRVEGLVL GGAVEYECFH EALKGLAQVL TQQFKERRST IARQTCHLIG
     VLARALGPRF EQHALTLLPT LFGVLVITVA VMAESADVGV RNILRHCHAT RVLQTIADGV
     CKEKNPKTRQ FCATYLNVIL EDWDVGVWSR QLEGVEAAIK AAVQDPTGDT RQSGRTAMAL
     YSSALPERAQ AFLKRLDGGL QDKLSAAVSG GKPAKPAPTT HSRQALSAAL AAKKMAARRA
     QEAADADAGI VVMVPTAVKS QQPAEVLSAA TARNRSAGRT SSAAFLAPAP SSSQQGGSGD
     GSEGASRLMT GTVGRNSRKS LCLPPGRIPG GSADLTGLLG DSASTSAIVA AAPSASVRSS
     GQFQSDRGSG AAESGAAASS APGLVPLSRV VSTILGGPRT WSDKVLAAAL TLLGNLVKYY
     GRVLEGQLDR LLPLLLNKGA EGKEQSRALC TDIMHACGQV YRADALVPAL SKCLDIVKLP
     RSKQMALEFF RAHVGTWSGI NATQLKHWLV RLAPLLDDRT PDLRKRAGEV LDCLLAVPWA
     REPINYVAYQ HNNADVVAVM AQLLDTAREV LSAAAAAADG SMPFAMGRHT AAMENLADAV
     ERCSKEAWVR TFPPLMVELN SWVQHPFGAV RSMSYSLLRE LLLHQPHLFT DNNLESQLGL
     LLHGCGDASR EVSTPASQTL SVLLSSCNAQ QAIVLMQELM PREREAHRRG QDKGARLVAV
     MEGVRQLAAR LSPDQLHRLT FQPHPTTGNT LLEPLVANLM DVETCVRRGA VVTLAELWYR
     LGSSSDMMFV TITT
//
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