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Database: UniProt
Entry: E4X3D3_OIKDI
LinkDB: E4X3D3_OIKDI
Original site: E4X3D3_OIKDI 
ID   E4X3D3_OIKDI            Unreviewed;       451 AA.
AC   E4X3D3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, 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=GSOID_T00017774001 {ECO:0000313|EMBL:CBY18137.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY18137.1};
RN   [1] {ECO:0000313|EMBL:CBY18137.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000256|ARBA:ARBA00024350}.
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DR   EMBL; FN653023; CBY18137.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4X3D3; -.
DR   InParanoid; E4X3D3; -.
DR   Proteomes; UP000001307; Unassembled WGS sequence.
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; cd17954; DEADc_DDX47; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR044765; DDX47/Rrp3_DEADc.
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:SF21; 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; 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:UP000001307}.
FT   DOMAIN          24..52
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          55..228
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          255..399
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          418..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           24..52
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        418..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   451 AA;  50605 MW;  554DC05579C841B7 CRC64;
     MSSSESDHEQ DDNQEEEFTL EGLEAWQSLG VCDEVAQTCV DLKWSKPTPI QQKSIPIAIE
     GKDVIGLAET GSGKTAAFAI PVLQTLLKTP GGGRLSCLVM TPTRELAFQI REQFQALGSS
     IGLSCACIVG GIEMMSQQLA LAKKPHVIVA TPGRLVDHLE KTRGFNLKAL KFLIMDEADR
     ILNLDFEAEV DKILRAIPRE RQTMLFSATM TAKVKKLQRA ALKNPVKISI NSKYKTVDKN
     IQKYMFIPEA HKECYLVSLL NELQGSSFMI FTSTCAKTSL IARLVKRLGY DSVPLHGQMS
     QQKRLGALAR FKGKSRSILV CTDVASRGLD VPHVDCVINY DVPTNTKDYI HRVGRTARAG
     RAGKSVTFVS QYDVELYQKI EAHIGKKLDQ WPCEKDEVMA LKERVDEAKR IAVQEIKEEE
     GKRKSKKKRQ FDEEQSIKDR IGKVKHKKRR K
//
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