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Database: UniProt
Entry: G3Q122_GASAC
LinkDB: G3Q122_GASAC
Original site: G3Q122_GASAC 
ID   G3Q122_GASAC            Unreviewed;       753 AA.
AC   G3Q122;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023570.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000023570.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000023570.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; G3Q122; -.
DR   STRING; 69293.ENSGACP00000023570; -.
DR   Ensembl; ENSGACT00000023616.1; ENSGACP00000023570.1; ENSGACG00000017826.1.
DR   eggNOG; KOG0925; Eukaryota.
DR   GeneTree; ENSGT00940000155800; -.
DR   InParanoid; G3Q122; -.
DR   OMA; MKVYPLY; -.
DR   TreeFam; TF105735; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000017826; Expressed in embryo and 13 other cell types or tissues.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT   DOMAIN          105..271
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          296..476
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  86465 MW;  2AEABB60C509718F CRC64;
     MSKRHRLDLG EDYSTKKRSE GRDRDRDRED RSRDRERDRD RDRDPKPTNV PSNSTVPLPC
     LAPIKQLAMQ QQINPFTNLP HTPRFYEILK KRLQLPVWEY KERFGDIITR HQSFVLVGET
     GSGKTTQIPQ WCVDMVRGLP GPKRAVACTQ PRRVAAMSVA QRVADEMDVM LGQEVGYSIR
     FEDCSSAKTI LKYMTDGMLL REAMNDPLLE RYGVIILDEA HERTLATDIL MGVLKEVVRQ
     RGDLKVIVMS ATLDAGKFQV YFDNCPLLTI PGRTHPVEIF YTPEPERDYL EAAIRTVIQI
     HMCEEDEGDC LLFLTGQEEI DEACKRIKRE VDDLGPDVGD IKIIPLYSTL PPQQQQRIFE
     PPPPRKPNGA IGRKVVVSTN IAETSLTIDG VVFVIDPGFA KQKVYNPRIR VESLLVTAIS
     KASAQQRAGR AGRTRPGKCF RLYTEKAYKT EMQDNTYPEI LRSNLGSVVL QLKKLGIDDL
     VHFDFMDPPA PETLMRALEL LNYLAALNDD GDLTELGSMM AEFPLDPQLA KMVIASCEFN
     CSNEILSITA MLSVPQCFVR PTEAKKAADE SKMRFAHIDG DHLTLLNVYH AFKQNHEANQ
     WCYDNFVNYR SLMSADNVRQ QLSRIMDRFN LPRRSTEFTS RDYYTNIRRA LCTGFFMQVA
     HLERTGHYLT VKDNQVVQLH PSTVLDHKPE WVLYNEFVLT TKNYIRTCTD IKPEWLVKIA
     PQYYEMSNFP QCEAKRQLER IVAKLESKEY SQY
//
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