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Database: UniProt
Entry: Q54TF8
LinkDB: Q54TF8
Original site: Q54TF8 
ID   DDX19_DICDI             Reviewed;         465 AA.
AC   Q54TF8; O00898;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=ATP-dependent RNA helicase ddx19;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase helC;
DE   AltName: Full=DEAD box protein 19;
GN   Name=helC; Synonyms=ddx19; ORFNames=DDB_G0281553;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=AX3;
RX   PubMed=9601648; DOI=10.1016/s0960-9822(98)70233-7;
RA   Machesky L.M., Insall R.H., Kay R.R.;
RT   "The helC gene encodes a putative DEAD-box RNA helicase required for
RT   development in Dictyostelium discoideum.";
RL   Curr. Biol. 8:607-610(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: ATP-binding RNA helicase required for normal differentiation
CC       and development. {ECO:0000269|PubMed:9601648}.
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   -!- 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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB60938.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF002677; AAB60938.1; ALT_FRAME; mRNA.
DR   EMBL; AAFI02000042; EAL66538.1; -; Genomic_DNA.
DR   RefSeq; XP_640633.1; XM_635541.1.
DR   AlphaFoldDB; Q54TF8; -.
DR   SMR; Q54TF8; -.
DR   STRING; 44689.Q54TF8; -.
DR   PaxDb; 44689-DDB0215338; -.
DR   EnsemblProtists; EAL66538; EAL66538; DDB_G0281553.
DR   GeneID; 8623244; -.
DR   KEGG; ddi:DDB_G0281553; -.
DR   dictyBase; DDB_G0281553; helC.
DR   eggNOG; KOG0332; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q54TF8; -.
DR   OMA; DFKNLCM; -.
DR   PhylomeDB; Q54TF8; -.
DR   PRO; PR:Q54TF8; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   CDD; cd17963; DEADc_DDX19_DDX25; 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; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF31; 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; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Developmental protein; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; RNA-binding.
FT   CHAIN           1..465
FT                   /note="ATP-dependent RNA helicase ddx19"
FT                   /id="PRO_0000327407"
FT   DOMAIN          102..268
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          297..449
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           70..98
FT                   /note="Q motif"
FT   MOTIF           215..218
FT                   /note="DEAD box"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         115..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        52..53
FT                   /note="GI -> EF (in Ref. 1; AAB60938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="V -> W (in Ref. 1; AAB60938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="A -> T (in Ref. 1; AAB60938)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   465 AA;  51720 MW;  B6756CA7D0B8B689 CRC64;
     MSEKETNTTS TENKEKEKQE QTNTNSTTES TNNQVDEEYE RPGRSEGLDE FGIQLDIQQS
     DPNSPLYSVK TFEELGLKPE LLKGVYAMGY NKPSKIQEAA LPIIIQSPNN LIAQSQSGTG
     KTAAFTLGML NCVDPSINAP QAICISPTKE LALQTFEVIS KIGQFSNIKP LLYISEIEVP
     KNVTNQVIIG TPGKILENVI KKQLSVKFLK MVVLDEADFI VKMKNVPNQI AMINRLLPSN
     VKVCLFSATF SMGVEELIKK IVQDPYTSIR LKRQELSVEK IHQYFIDCGS EDNKALILSD
     IYGFISVGQS IVFVHTIATA KSVHQKMVDE GHSVSLLYGK DLTTEERFKQ IKDFKDGKSK
     VLITTNVLAR GIDIPQVSLV INYDVPLDEM GKPDPVHYLH RIGRVGRFGR SGVALSFVYD
     QQSTNKLMNI STHLGVPLKE LKSSEIESLD GILKGIRNQL TPLNN
//
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