ID L1I405_GUITC Unreviewed; 1041 AA.
AC L1I405;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=GUITHDRAFT_149568 {ECO:0000313|EMBL:EKX30993.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX30993.1};
RN [1] {ECO:0000313|EMBL:EKX30993.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX30993.1,
RC ECO:0000313|Proteomes:UP000011087};
RX PubMed=23201678; DOI=10.1038/nature11681;
RG DOE Joint Genome Institute;
RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT "Algal genomes reveal evolutionary mosaicism and the fate of
RT nucleomorphs.";
RL Nature 492:59-65(2012).
RN [2] {ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:EKX30993}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; JH993408; EKX30993.1; -; Genomic_DNA.
DR RefSeq; XP_005817973.1; XM_005817916.1.
DR AlphaFoldDB; L1I405; -.
DR STRING; 905079.L1I405; -.
DR PaxDb; 55529-EKX30993; -.
DR EnsemblProtists; EKX30993; EKX30993; GUITHDRAFT_149568.
DR GeneID; 17287713; -.
DR KEGG; gtt:GUITHDRAFT_149568; -.
DR eggNOG; KOG0383; Eukaryota.
DR HOGENOM; CLU_292676_0_0_1; -.
DR Proteomes; UP000011087; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032001; SAWADEE_dom.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF16719; SAWADEE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 2.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011087}.
FT DOMAIN 378..435
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 474..645
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKX30993.1"
SQ SEQUENCE 1041 AA; 119053 MW; AD981A72AB7EEFD3 CRC64;
SANLDRSDEV RPYKTRSARA RDETSSEEEE ISDSSIEPRQ IEEDFMDEDV QPSPVKKARV
GAGASQPDCL LLEAYDEATR AWYDVQILEL RRSKARVLFE NVEPVEKTWI PIHYLRVRSD
PCEMNLTRPL RVGAKVLAFR VRKDDALYFD AVIERIKRKK DKMAAGKENR CKAGAKAEDN
EDEEIPVDGN MYKVKYQDGP VKGRSEWLLV HQLLKRNFSP VINYSILCKR LPDTHHVCLH
PLIFVGLSFQ VISDASNDES DFDLFKGWMA ANTETLPSTV ARKLTAISHS GDEQVSNLFA
CRLVHDGLQV VDEILSFRVA EKNPKKGDGK ADVNAREYFV ILCRSGMTVA IVKLNGSVAR
RVTRMIARLK KFAVGGLNHG EVLLIVLLSK YLVKWCGCSY EKCTWEDESS LDSPGDREKV
KEFQAAQARY VKRSKQQKGS EKKPVTAYHE IFESPSYLNG ALHDYQIRGL NWLRKKRFDG
ENVILADEMG LGKTIQIASL IASVMVEEKR TCGPFLIVVP LSTIANWKRE IQKWCPDVNF
AVLHDSQKGR QVMIDHEFDP LKLGVMRFEV LCTSYEVAVS AFSALSKVRW DTLIVDEGHR
LKNDESILYA QLQKLQTKNK ILLTGTPLQN NLNELFNLMI RMIHKLFEPY ILRRLKKDVK
IHLKAKVEKT VPISLTDIQK TFYAAILAKN LDVLNGRNKD NRHVSLNNVL MELRKCCNHA
YLFDSAVKHH KNPDDTLAHL VQASGKFELL HLLLPKLKER GSKVLIFSQF KIMLDILETY
LELFNNPESE YFIFLLSTRA GGQALSRAHR IGQKNNVLVL RLVTINTVEE KVISQARKKL
MLESLVVGAN QECKFSRKET ELWLMSVLLL MDYQEILLYG AKQIVSDDQK LKSTKCSRVL
TSELRALECE TADDTSRSQR GACGLPEPDQ AKKQAYAKTQ QVVRALARQA SVKYSDTFVD
QLLQIENTEN GDSFEDYNES LKFDFESRDG QDEGKVDEQM VQSRMYWNEL LKDYAEQEKE
DDVLGRGKRK RSHVSYCEQQ M
//
