ID   RH7_SPIOL               Reviewed;         685 AA.
AC   Q41382;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 7;
DE            EC=3.6.4.13;
GN   Name=RH7; Synonyms=PRH75;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Seedling;
RX   PubMed=9121476; DOI=10.1128/mcb.17.4.2257;
RA   Lorkovic Z.J., Herrmann R.G., Oelmueller R.;
RT   "PRH 75, a new nuclear-localized member of the DEAD-box protein family from
RT   higher plants.";
RL   Mol. Cell. Biol. 17:2257-2265(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9121476}.
CC   -!- DEVELOPMENTAL STAGE: Mainly expressed in young and rapidly developing
CC       tissues. {ECO:0000269|PubMed:9121476}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X99937; CAA68193.1; -; mRNA.
DR   PIR; T09159; T09159.
DR   AlphaFoldDB; Q41382; -.
DR   SMR; Q41382; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR012562; GUCT.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08152; GUCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; RNA-binding.
FT   CHAIN           1..685
FT                   /note="DEAD-box ATP-dependent RNA helicase 7"
FT                   /id="PRO_0000239149"
FT   DOMAIN          138..320
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          349..491
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           107..135
FT                   /note="Q motif"
FT   MOTIF           266..269
FT                   /note="DEAD box"
FT   COMPBIAS        13..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         151..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   685 AA;  73085 MW;  F7717C666CBF87F7 CRC64;
     MPSISMMSDA ITPETLKKEK KMKSETLDSD DTVVKKEKSS SKKKEKSSSS GKKDKEEKEK
     KKKRKAVDLD DSSDKSDNSS ELVQADDLKP KKAKVMEEAV VEAEDPNSLS NFRISKPLKD
     VLISKGIKAL FPIQAMTFDN VIDGCDLVGR ARTGQGKTLA FVLPIVESLV NGRTKDLRRS
     GHGRLPSVLV LLPTRELATQ VLADFQVYGG AVGLTACSVY GGAPFHSQIS SLTRGVDIVV
     GTPGRVKDLL EKGVLKLGSL LFRVLDEADE MLKMGFVDDV ELILGKVDHV SKVQTLLFSA
     TLPSWVKQIS TRFLKSAKKT VDLVSDQKMK ASISVRHIVI PCSASARPDL IPDIIRCYGS
     GGRSIIFTET KESASQLAGL LTGARPLHGD IQQTQREVTL KGFRTGKFMT LVATNVAARG
     LDINDVQLII QCEPPRDVED YIHRSGRTGR AGNTGVAVML YDPKRSSVTK IERESGVKFE
     HLSAPQPVDV AKAVGIEAAA AILQISDSVI PAFKDAAEEL LSTSGLSAVD ILSKALAKAA
     GYSDIKERSL LTGMEGYVTL LLDAGRPFYG QSFAYTVLKR FLPATKADSI MGVALTADKS
     GAVFDVPVDD LETFLVGAEN AAGVNLDVVK ALPPLEEKVQ ISRRFGGGGR GGRGGGYGGR
     GGGYGGGGYG GGGGYGGRGG GYGRR