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Database: UniProt
Entry: A0A087W1Z5_ECHMU
LinkDB: A0A087W1Z5_ECHMU
Original site: A0A087W1Z5_ECHMU 
ID   A0A087W1Z5_ECHMU        Unreviewed;      1326 AA.
AC   A0A087W1Z5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=EmuJ_000242500 {ECO:0000313|EMBL:CDI98560.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CDI98560.1};
RN   [1] {ECO:0000313|EMBL:CDI98560.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [2] {ECO:0000313|EMBL:CDI98560.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000256|ARBA:ARBA00008792}.
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DR   EMBL; LN902844; CDI98560.1; -; Genomic_DNA.
DR   STRING; 6211.A0A087W1Z5; -.
DR   eggNOG; KOG0921; Eukaryota.
DR   OMA; RFKCELR; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd19854; DSRM_DHX9_rpt1; 1.
DR   CDD; cd19855; DSRM_DHX9_rpt2; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.30.160.20; -; 2.
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; IPR044445; DHX9_DSRM_1.
DR   InterPro; IPR044446; DHX9_DSRM_2.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014720; dsRBD_dom.
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:SF119; ATP-DEPENDENT RNA HELICASE A; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00035; dsrm; 2.
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; SM00358; DSRM; 2.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT   DOMAIN          6..76
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          171..244
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          401..567
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          646..817
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1262..1326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1326 AA;  150165 MW;  DB015DE824E99D81 CRC64;
     MSDAEGIKTF VYTWLHKSQR KVPEYTFQQR SMGRGRLRFI CELRVDGFAY IGVGNSVNKK
     DAQTNAARDF ASFLVREGYL KESEVPTIRA EEYRHLADED RHCAAMYPST SSSGAMHPSY
     HPPHLQVNET DVPGRGPNDS YINRIMDRIK LEEAEGIDLT ADIHGGWSME NSKARLNEYL
     QASRQPPVQI KFTSIGPDHN KSFLAEATVW ARRVNKTLYA RENGSNKTMA SRACCLSLVR
     QLFHVGEIEA YCGERKRKRS DDLPPLAVKL NPDLENRLHA LLERLHLVPN LSPPVPPLKT
     GRTAVGSSEE EHNMIMNYQV ADFEPRPRQS AQLISWCPPI ENWNPWTAYN IDEGPEALMS
     LAQLSQTYKE QYERRINSRA YEVIREERNS LPVAAFSQQI LDTIAGNQVT LIKGETGCGK
     TTQIPQFILD SYLASSRGAE CSVLVTQPRR ICAISLAERV ASERCETVGI SVGYSVRFET
     ILPRPYGSIL FCTIGTFCRK MEAGIRGVSH IIVDEIHERD VNTDFVMILM RDLVRANPSL
     RVILMSATID TTTFTEYFDN TATVELEGRT YPVSCFYLED CINMTNYVPP PIYNEKKNKK
     PRLEEELTMD TEENCNFICP PGYPPSVAER MRQIPEKEVP FTLIGGLLEY ICRMNIDGAV
     LIFLPGWNTI SMLRKYLQTH PCFSNPNEFL ILPLHSQVPR EDQRLVFRPA PPGIRKIVLS
     TNIAESSITI NDVVFVIDTC LARVKMFTAR NNLTSYSTMW ASLTNLEQRR GRAGRVRAGF
     AYHLCSRARL SRLEHYATPE ILRTPLHELA LMIKLLRLGD IQTFLRKALQ SPPLDAVIEA
     EYTLREMKAL DSNDELTPLG HILARLPIEP RLGRMLVFSC AFRLGGAMAL VAAHSSFGCD
     VLAMPPDRRR LSWEQLRFAA TTNSDHLAML NAFQVWSTKR AQDGDQAANY FCDVRELNAF
     SLRIIDEAAH QICNILMGLG FPESVLSDRL INFNNRSCST FDYVAAMLTN GLYPNIAYHV
     EKRKLLTAEG KCALVHKGSV NCTKNPTFTF PLFAFTEKIR TQAISCKTLT MVTPIQLLLF
     GCRRGVWKPK STGLESARSD ERRVALMEEE GVVLLDDWLP FRMRYSTAAR IFALRPALEA
     LLVRVCLRPA CLENLSPEDR SVIELTKELC RHTALRDAAT LDEATHSTCA RFNADSRCPL
     PTDTRRQIGP PEMSATSFDW DESQSLGWGY REWQDEWSHT SSNAGNPPPY CVHAGVHGTK
     RDYPWPNRET YIPQNYGDRS GSLPQSAGHY AEPPLRHEKL DYGYEPTLSR PPGPRSLRKP
     RPPYPY
//
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