ID   Q7Z2V5_HUMAN            Unreviewed;       406 AA.
AC   Q7Z2V5;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   Flags: Fragment;
GN   Name=DKFZp686J01190 {ECO:0000313|EMBL:CAE11890.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:CAE11890.1};
RN   [1] {ECO:0000313|EMBL:CAE11890.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Human esophagus tumor {ECO:0000313|EMBL:CAE11890.1};
RG   The German Human cDNA Consortium;
RA   Lauber J., Bahr A., Mewes H.W., Weil B., Amid C., Osanger A., Fobo G.,
RA   Han M., Wiemann S.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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DR   EMBL; BX571764; CAE11890.1; -; mRNA.
DR   AlphaFoldDB; Q7Z2V5; -.
DR   SMR; Q7Z2V5; -.
DR   IntAct; Q7Z2V5; 2.
DR   PeptideAtlas; Q7Z2V5; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd18049; DEADc_DDX5; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF90; ATP-DEPENDENT RNA HELICASE DDX5-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT   DOMAIN          94..122
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          125..300
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          328..406
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           94..122
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         406
FT                   /evidence="ECO:0000313|EMBL:CAE11890.1"
SQ   SEQUENCE   406 AA;  45997 MW;  42163AD6A38D2E0E CRC64;
     MSGYSSDRDR GRDRGFGAPR FGGSRAGPLS GKKFGNPGEK LVKKKWNLDE LPKFEKNFYQ
     EHPDLARRTA QEVETYRRGK EITVRGHNCP KPVLNFYEAN FPANVMDVIA RQNFTEPTAI
     QAQGWPVALS GLDMVGVAQT GSGKTLSYLL PAIVHINHQP FLERGDGPIC LVLAPTRELA
     QQVQQVAAEY CRACRLKSTC IYGGAPKGPQ IRDLERGVEI CIATPGRLID FLECGKTNLR
     RTTYLVLDEA DRMLDMGFEP QIRKIVDQIR PDRQTLMWSA TWPKEVRQLA EDFLKDYIHI
     NIGALELSAN HNILQIVDVC HDVEKDEKLI RLMEEIMSEK ENKTIVFVET KRRCDELTRK
     MRRDGWPAMG IHGDKSQQER DWVLNEFKHG KAPILIATDV ASRGLG
//