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Database: UniProt
Entry: W5L5F2_ASTMX
LinkDB: W5L5F2_ASTMX
Original site: W5L5F2_ASTMX 
ID   W5L5F2_ASTMX            Unreviewed;       857 AA.
AC   W5L5F2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   Name=DDX24 {ECO:0000313|Ensembl:ENSAMXP00000015064.2};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000015064.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000015064.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00001556,
CC         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. DDX24/MAK5
CC       subfamily. {ECO:0000256|ARBA:ARBA00038457}.
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DR   RefSeq; XP_007257440.1; XM_007257378.2.
DR   AlphaFoldDB; W5L5F2; -.
DR   STRING; 7994.ENSAMXP00000015064; -.
DR   Ensembl; ENSAMXT00000015064.2; ENSAMXP00000015064.2; ENSAMXG00000014635.2.
DR   GeneID; 103042633; -.
DR   KEGG; amex:103042633; -.
DR   CTD; 57062; -.
DR   eggNOG; KOG0347; Eukaryota.
DR   GeneTree; ENSGT00550000074847; -.
DR   HOGENOM; CLU_003041_13_1_1; -.
DR   InParanoid; W5L5F2; -.
DR   OrthoDB; 56712at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000014635; Expressed in zone of skin and 14 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17946; DEADc_DDX24; 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; PTHR24031:SF91; ATP-DEPENDENT RNA HELICASE DDX24; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 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, ECO:0000256|RuleBase:RU365068};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          229..257
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          261..539
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          572..733
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          69..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           229..257
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        89..110
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..369
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  96394 MW;  631E47AC38761366 CRC64;
     MKTKMLSKKR PGSGKKRGIL VKGQWKTVKI DPSIFADEAM GEVVVFEELT DYSLVESNKT
     VAVSKLLQES VGKKKRKSNK RTAREIEDEE GLLNEEFAEQ SSDDDDDVEK LDIVEKPAKK
     RKKKKKKTKG NTVAGIESQD TSEGLSNLTK EGEDQTQEQS EGSCSVTILT SGKKKKTKKQ
     KSATEQAMSS SQVIETDAQV NPVGKSKRKG KNWTDAALSN SAAQDSDVSA WKDLFVPELV
     LKALSKLGFS APTPIQALAL PPAIRDHMDI LGAAETGSGK TLSFGIPMIH RILEWKKSVH
     AKNAGLSTGK STESGLDQAD EEMPDIETDS IAQEDGKNDE DEGIILEAAE DGEEMAGEEE
     DDDEEEQQSR DDGLATNDEG VLDIETKGTE KQDSEKRPLL GLVLTPTREL AVQVQHHIDA
     VAQFTGIKTA ILVGGMAPQK QDRVLKRRPE IVIATPGRLW EMIQDRHPHL RNLRQLRCLV
     IDEADRMVEK GHFAELEKLL EMLSTSQFNP KRQTFVFSAT LTMVHSLPSR LARKKGKQLE
     QRSKLELLME KVGIKNKPKI IDLSRKEATV ETLTETKIHC EKEEKDFYLY YFLLQYPGRT
     MVFANSIDCI KRLTSLLTIL DCNPLPLHAN MHQKQRLKNL ERFAERESCV LLTTDVAARG
     LDIPDVQHVL HYQVPRTSET YVHRSGRTAR AAKEGLSLLL IGPDDMINFK KIYKTLGKDE
     DLPVFPIQNK CMAAIKERVN VARGIEKIEY HNSRAKQHNS WLRQAAEEMD IDVDDDLLMG
     GGRDEREDRD QQKLVKGMKK HLKHLLSQPV FKPHMQTKYP TQMGRLQLPE LPLASETALS
     SLTNQQRKQK QQQKRKL
//
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