ID A0A162RIX2_9CRUS Unreviewed; 826 AA.
AC A0A162RIX2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=APZ42_012733 {ECO:0000313|EMBL:KZS20545.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS20545.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS20545.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS20545.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS20545.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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:KZS20545.1}.
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DR EMBL; LRGB01000158; KZS20545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162RIX2; -.
DR STRING; 35525.A0A162RIX2; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
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:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
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; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KZS20545.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 35..63
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 66..237
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 268..410
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 584..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..63
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 586..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..826
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 92749 MW; EB98261AAA1678DA CRC64;
MPELEGFGDG GYQSEAELDT RTLVQEQNRK KKKSGGFQSM GLSYNVYRGV IKCGYKIPTP
IQRKCIPLIM EKKDVVAMAR TGSGKTACFL IPLFERLQAH STIGTRALIM SPTRELALQT
LKFTRELGKY TGLKAATILG GDSMEAQFAA MHEIPDIIIA TPGRFAHLCV EMELKLKEIE
YVVFDEADRL FEMGFGEQLL EILNRLPESR QTLLFSATLP KLLVDFTKAG LTDPVLVRLD
VDSKLPEALK LAFVFCPCES KASILLHLLR NAIKAGELTL VFAATMHHVE YLHLLLDKAG
ISNTYIYSSL DQAARKIHAA KFQTKQTNVM ITTDVAARGI DIPLLDNVIN YNFPAKAKLF
VHRVGRVARA GRSGTAYSLV ALDEIPALVD LHLFLGRLVK QIPQDGLKKG EDWDGYLGRV
GQSVIDDGSS AMQLWHQESV ELQNMIKVYT SAYKQYKRSC PPPSHESIKK GKEIKLELLG
PHPVFVAESG ELESDRLNLL EQMKCYRPHH TIFEIGVTAN SIKAKVMLEK RIKHQRIIIK
QKKAAIKSAA EAASSDEPEN VGVPQEEADE EMVQEAFSTV IAQKKRASRK PFDPNQAKKK
RLQTQTTKDE ENYINYVAKD HQTESGLALG CDFGRAAADA VLDLTGDDDQ ELRKQRSLMK
WDRKKKKFIG QEDVKKRKIR TESGVWIPAT YKTDRYERWK GKSKIDQNDP ASEDSGDDEK
GGNRNVSSRF GGGFPRRGVP MGMNLEGKLG GLPMNHPAMK KAWSEVKRGG QRVGDEVKLP
EQIEKARKLK EKARLRGNKE IRIKLQMKQK KPTLKTKQKK GGKRRR
//
