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Database: UniProt
Entry: A0A0V1CLW4_TRIBR
LinkDB: A0A0V1CLW4_TRIBR
Original site: A0A0V1CLW4_TRIBR 
ID   A0A0V1CLW4_TRIBR        Unreviewed;       786 AA.
AC   A0A0V1CLW4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=Ddx54 {ECO:0000313|EMBL:KRY50293.1};
GN   ORFNames=T03_17070 {ECO:0000313|EMBL:KRY50293.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY50293.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY50293.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY50293.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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. DDX54/DBP10
CC       subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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:KRY50293.1}.
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DR   EMBL; JYDI01000153; KRY50293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1CLW4; -.
DR   STRING; 45882.A0A0V1CLW4; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0043186; C:P granule; IEA:UniProt.
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; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17959; DEADc_DDX54; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR012541; DBP10_C.
DR   InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
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; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR   Pfam; PF08147; DBP10CT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01123; DBP10CT; 1.
DR   SMART; SM00487; DEXDc; 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.
DR   PROSITE; PS51195; Q_MOTIF; 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:UP000054653};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          26..54
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          57..230
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          254..409
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          590..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           26..54
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        745..773
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  89767 MW;  3FF922E38B304B4C CRC64;
     MESADEVEID YAKLLIAQNR KNKSAGGFQA MGLDHNVFKG IMKRGYKIPT PIQRKTIPII
     LNGKDVVAMA RTGSGKTAAF LIPMFVKLKI RDPSAGVRAM IISPTRELAL QTFKFLKEVL
     GKFTGLRASV IIGGDSMEDQ FAAIHENPDV VIATPGRLLH LIVEMNLSLK SVNYVVFDEA
     DRLFEMGFEE QLREVLKRLP PDRQTLLFSA TLPKSLVDFT RAGLRHPTLI RLDVDSKLSD
     KLKLTHLFCR REDKLGILLS ILGDRSLVEE NSLTLIFCAT KHYVEFLHAI LEYFKFKCAC
     LYSSMDSEAR RVNVEKFHRK EINILIVTDL AARGVDIPLL DNVINFHFPA KAKLFVHRVG
     RAARAGRHGH AISFISTDEY AYLLDLYLFL GRSLQFSTSG TCADVGDLIG TVPQRRVDDE
     NRTIALLLNT TSLDLESLQK VAENSYKHYT RSRPTSSAES VRRAKAETRL NNLPNHPAMA
     AVGFGCEKLE QEKDILLANI KCFRPQTTVF ELNAKSSDLQ WQVMKAKRRV HQKKIDQSKA
     ATVAEMNAAS NEEDHPLQQH VDAHANDPVD FTGVFSEKIE SKFSERATES VLSHKKKKKK
     TQNQKMTVKE EEKKEQFFIP YVPSDLHSEQ GLSVENNFTS ELGSAVIDFM DDEMEKMQRR
     NQKTKWDRKR KKFVNACDED NKKRSSKKIK TESGVWIPAS YKTDLYDSWK KKLRMKAVQG
     DVDQQENTEK RLKFFRRNRH AKGRKGPVKS ELKSKMQIIK QRVESEHRRK RNAKQLTNEK
     KQKKKK
//
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