ID A0A2G5C843_AQUCA Unreviewed; 747 AA.
AC A0A2G5C843;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=AQUCO_07700010v1 {ECO:0000313|EMBL:PIA27449.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA27449.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA27449.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
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 {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC subfamily. {ECO:0000256|ARBA:ARBA00038084}.
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DR EMBL; KZ305094; PIA27449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5C843; -.
DR STRING; 218851.A0A2G5C843; -.
DR InParanoid; A0A2G5C843; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17941; DEADc_DDX10; 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; IPR025313; DUF4217.
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 PANTHER; PTHR24031:SF54; ATP-DEPENDENT RNA HELICASE DDX10-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 106..281
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 303..455
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 674..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 84181 MW; 387D48CF210BE2EC CRC64;
MKPKSKNPKF TRKKKWVSEV EEIELLESWI EYGKPDSGSN PLSIKPLSKD APIGKLEDND
DENSLLLFSS YGGCKKFVQY PISQKTKDGL AEGKFKVTTD IQRASLPHTL CGRDILGAAK
TGSGKTLAFI IPVLEKLYRA RWGPEDGVGC IIITPTRELA GQIFDVLNLV GKRHGFSAGL
LIGGRKDVEV EKESVNDLNI LVCTPGRLLQ HMDETQNFDC SQLQILVLDE ADRILDVGFK
QALNAIISQL PKKRQTLLFS ATQTKSIQDL ARLSLKDPEY ISVHKEHVTA TPSRLQQTAM
IVPLDQKLDM LWSFIKAHLN SKILVFLSTC KQVKFVFEAF KKLRPGIPLT CLHGRMKQEV
RMVIYSQFCE KRTVLFSTDV ASRGLDFNKA VDWVVQVDCP DDTASYIHRV GRTARYHSGG
RSVLFLTPSE EVILQKLQSA KVPVQLIKAN TKRLQSVSGL LGSLLVKYPS MQALAERAFI
TYLRSIHKQR DKEVFDVMKL PIEEFSASLG LPMTPKVRFL DRKSRAGTVS EKAPQPKIAV
ENIEAKTSIE LADPNQSKEE MEKAFLFEKE TEIDEERIGA ENGLTAVPAT RILKKKKLKI
NVHRPVGTRV VFDEEGNTLP PLAAFANTDN TGCGKDLVEH DIVQDRYEKL REDMKNRDKE
DKELHKKRLE KMRLKEKMKR RRAAEVLSGS DDEETEDRST KKSKIYFDSD NEDGEKENKY
EPGIKADSIS LAEQEALALN LLSSMHS
//
