ID A0A218VD46_9PASE Unreviewed; 765 AA.
AC A0A218VD46;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=DHX15 {ECO:0000313|EMBL:OWK63660.1};
GN ORFNames=RLOC_00013999 {ECO:0000313|EMBL:OWK63660.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK63660.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK63660.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK63660.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) 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. DEAH subfamily.
CC DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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:OWK63660.1}.
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DR EMBL; MUZQ01000010; OWK63660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218VD46; -.
DR STRING; 299123.ENSLSDP00000010218; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
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; cd17973; DEXHc_DHX15; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044756; DHX15_DEXHc.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF95; ATP-DEPENDENT RNA HELICASE DHX15; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OWK63660.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619}.
FT DOMAIN 117..283
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 308..488
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 88059 MW; C8C41441B8809833 CRC64;
MSKRHRLDLG DDYSSSKKRT TDGKDRDRDR DRDDRSKDRD RDRDRDRDRD RERDKEKDLR
PTSNSTYYAA AGLPAIKPAM IPHSINPFTN LPHTPRYYDI LKKRLQLPVW EYKERFTDIL
IRHQSFVLVG ETGSGKTTQI PQWCVDYMRS LPGPKRGVAC TQPRRVAAMS VAQRVADEMD
VMLGQEVGYS IRFEDCSSAK TILKYMTDGM LLREAMNDPL LERYGVIILD EAHERTLATD
ILMGVLKEVV RQRSDLKVIV MSATLDAGKF QIYFDNCPLL TIPGRTHPVE IFYTPEPERD
YLEAAIRTVI QIHMCEEEEG DLLLFLTGQE EIDEACKRIK REIDDLGPEV GDIKIIPLYS
TLPPQQQQRI FEPPPPKKQN GAIGRKVVVS TNIAETSLTI DGVVFVIDPG FAKQKVYNPR
IRVESLLVTA ISKASAQQRA GRAGRTRPGK CFRLYTEKAY KTEMQDNTYP EILRSNLGSV
VLQLKKLGID DLVHFDFMDP PAPETLMRAL ELLNYLAALN DDGDLTELGS MMAEFPLDPQ
LAKMVIASCD YNCSNEVLSI TAMLSVPQCF VRPTEAKKAA DEAKMRFAHI DGDHLTLLNV
YHAFKQNHES VQWCYDNFIN YRSLMSADNV RQQLSRIMDR FNLPRRSTDF TSRDYYINIR
KALVTGYFMQ VAHLERTGHY LTVKDNQVVQ LHPSTVLDHK PEWVLYNEFV LTTKNYIRTC
TDIKPEWLVK IAPQYYDMSN FPQCEAKRQL DRIIAKLQSK EYSQY
//
