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Database: UniProt
Entry: A0A090N492_OSTTA
LinkDB: A0A090N492_OSTTA
Original site: A0A090N492_OSTTA 
ID   A0A090N492_OSTTA        Unreviewed;      1158 AA.
AC   A0A090N492;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=SNF2-related {ECO:0000313|EMBL:CEF99463.1};
GN   ORFNames=OT_ostta10g03000 {ECO:0000313|EMBL:CEF99463.1};
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448 {ECO:0000313|EMBL:CEF99463.1, ECO:0000313|Proteomes:UP000009170};
RN   [1] {ECO:0000313|Proteomes:UP000009170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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:CEF99463.1}.
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DR   EMBL; CAID01000010; CEF99463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090N492; -.
DR   STRING; 70448.A0A090N492; -.
DR   InParanoid; A0A090N492; -.
DR   OrthoDB; 318617at2759; -.
DR   Proteomes; UP000009170; Chromosome 10.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18010; DEXHc_HARP_SMARCAL1; 1.
DR   CDD; cd00085; HNHc; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.30.50; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR002711; HNH.
DR   InterPro; IPR003615; HNH_nuc.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45766:SF5; SNF2 DOMAIN-CONTAINING PROTEIN _ HELICASE DOMAIN-CONTAINING PROTEIN _ HNH ENDONUCLEASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF01844; HNH; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 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   Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT   DOMAIN          210..390
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          530..703
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          31..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1077..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1158 AA;  127482 MW;  4A0EBA1856E68D87 CRC64;
     MDDVLDVDDD AFDVELADVE VDLIARQRRE SNAFSRPESS SPHSNPVTNP STTTTTKRPR
     ARPHVWMDVV RDNVVRVSCS HERLRAGFAG KLYAAVDGFA VATPATPDDA EAGAAWDVPM
     RLAKKVRDAL CAMNAFERGY SRALRKNVAM GAPPARTAEY ASAPPGYCGV TKRGGEEDEE
     KARVEVDRRF GTIAGNIRRA LYPFQETGVK FAIRRNGRAL IADQMGVGKT LQAIAVADAY
     RDAGPLLVIV PAAMRFVWAD EIERWLTDVT PRQLSVIFGS GDKFLLEKLA KESREANSAA
     ATTGRRVVVS SYHMLAPLFD EFLEVKWGCV IADESHNMHV SKSFNGSETK MTETAWKLIK
     KAKYAVLTTG TPSLTKPFDM FYQIDALRPG MLGQTKWEFA EYYCDVKFDM KGRSDVSGGS
     RLLELRSLLT HTTMIRRLKK DVMGDLPPKR RQVVPIDIDQ SIARVGGPKI WAKIAKAARA
     PRDEMSYGEE DDNILDEDER DDVEYVLNAK LCNLEKGRRV SVSQIVGMLK IAPIIDWLES
     DLLRDDSMQF VIFAHHQAVL DAIERDVCMC LEKQNRGTYV RIDGSTPSDE RKVLVDKFRE
     GAAVGADGVV SVRIALLSVK AAGTGLDFST ASCVVFAELP DDASLLEQAE ARVHRRGNDS
     GVNVYFLCAR GGACSHDEDR WQRLESQLDV CKEAIDGDDA RVGLDVSAYG ASIELEATKK
     SVFSKSVVVE SSTVKDPTLS PSRVETKQAT PLQLWFEVSA TSGRLHAHAS ADGSEPLHVS
     VSRSQLTRAL ASAKYAKELP EPFSSNPAAV AAALDFSNTW NAMTARDRNS ILARQQPCRA
     NELNEVAEAL NSKAATAATG STSRHSRLVP LPKDADWCTV LVSDIAQRNR ANYEMRVPCR
     FVPGTTRRAL LCVNCVDELD RVFSDRIRRV DLFCGEECLR AYDQGMSSSA LRRALFEIER
     GVCVECGLDC EKLVKHVRVF KSRMKRVKEI LRLAPAFEKR GNKALLSRLA EKPSGGRAWE
     CDHKVAVFEG GGGCTVENAQ TLCVICHSKK TKEQAKQRAA KRKRDAELAA ARNARPITAL
     VDSDDSEDDV SIDNLAPPPT SRKPQAPAQT DIRDFTVVRP LASDSDDDDD DDDSLAELIV
     PAFSSKRPIV GHGLALPP
//
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