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ATP-dependent RNA helicase vasa, isoform A (EC 3.6.4.13) (Antigen Mab46F11)

 VASA1_DROME             Reviewed;         661 AA.
P09052; Q24582; Q8SXU8; Q9V3Q8;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 3.
30-AUG-2017, entry version 181.
RecName: Full=ATP-dependent RNA helicase vasa, isoform A {ECO:0000303|PubMed:3052853};
EC=3.6.4.13 {ECO:0000269|PubMed:8026330};
AltName: Full=Antigen Mab46F11;
Name=vas {ECO:0000312|FlyBase:FBgn0283442};
Synonyms=vasa {ECO:0000303|PubMed:3140040};
ORFNames=CG46283 {ECO:0000312|FlyBase:FBgn0283442};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=3140040; DOI=10.1038/335611a0;
Lasko P.F., Ashburner M.;
"The product of the Drosophila gene vasa is very similar to eukaryotic
initiation factor-4A.";
Nature 335:611-617(1988).
[2]
SEQUENCE REVISION.
Lasko P.F.;
Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=3052853; DOI=10.1016/0092-8674(88)90216-4;
Hay B., Jan L.Y., Jan Y.N.;
"A protein component of Drosophila polar granules is encoded by vasa
and has extensive sequence similarity to ATP-dependent helicases.";
Cell 55:577-587(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10471707;
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G.,
Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G.,
Martin C., Moshrefi A.R., Palazzolo M., Reese M.G., Spradling A.C.,
Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.;
"An exploration of the sequence of a 2.9-Mb region of the genome of
Drosophila melanogaster: the Adh region.";
Genetics 153:179-219(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[6]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[8]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ILE-256; ILE-271 AND GLY-552.
PubMed=8026330;
Liang L., Diehl-Jones W., Lasko P.;
"Localization of vasa protein to the Drosophila pole plasm is
independent of its RNA-binding and helicase activities.";
Development 120:1201-1211(1994).
[9]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=9521895;
Styhler S., Nakamura A., Swan A., Suter B., Lasko P.;
"vasa is required for GURKEN accumulation in the oocyte, and is
involved in oocyte differentiation and germline cyst development.";
Development 125:1569-1578(1998).
[10]
FUNCTION, INTERACTION WITH EIF5B, AND DISRUPTION PHENOTYPE.
PubMed=10678180; DOI=10.1016/S1097-2765(00)80414-1;
Carrera P., Johnstone O., Nakamura A., Casanova J., Jackle H.,
Lasko P.;
"VASA mediates translation through interaction with a Drosophila yIF2
homolog.";
Mol. Cell 5:181-187(2000).
[11]
FUNCTION.
PubMed=11526087;
Harris A.N., Macdonald P.M.;
"Aubergine encodes a Drosophila polar granule component required for
pole cell formation and related to eIF2C.";
Development 128:2823-2832(2001).
[12]
FUNCTION, INTERACTION WITH GUS, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12479811; DOI=10.1016/S1534-5807(02)00361-1;
Styhler S., Nakamura A., Lasko P.;
"VASA localization requires the SPRY-domain and SOCS-box containing
protein, GUSTAVUS.";
Dev. Cell 3:865-876(2002).
[13]
FUNCTION, INTERACTION WITH FAF, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND UBIQUITINATION.
PubMed=14588248; DOI=10.1016/j.cub.2003.10.026;
Liu N., Dansereau D.A., Lasko P.;
"Fat facets interacts with vasa in the Drosophila pole plasm and
protects it from degradation.";
Curr. Biol. 13:1905-1909(2003).
[14]
INTERACTION WITH PIWI; DCR-1 AND FMR1, AND SUBCELLULAR LOCATION.
PubMed=16949822; DOI=10.1016/j.cub.2006.08.051;
Megosh H.B., Cox D.N., Campbell C., Lin H.;
"The role of PIWI and the miRNA machinery in Drosophila germline
determination.";
Curr. Biol. 16:1884-1894(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND THR-27, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[16]
FUNCTION, AND INTERACTION WITH AUB; ME31B; EIF-4A AND TER94.
PubMed=18590813; DOI=10.1016/j.mod.2008.06.005;
Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.;
"Isolation of new polar granule components in Drosophila reveals P
body and ER associated proteins.";
Mech. Dev. 125:865-873(2008).
[17]
FUNCTION, INTERACTION WITH GUS AND FSN, SUBCELLULAR LOCATION,
MUTAGENESIS OF 184-ASP--ASN-188; ASP-184; ASN-187; ASN-188 AND
ASN-189, AND MOTIF.
PubMed=20123973; DOI=10.1128/MCB.01100-09;
Kugler J.M., Woo J.S., Oh B.H., Lasko P.;
"Regulation of Drosophila vasa in vivo through paralogous cullin-RING
E3 ligase specificity receptors.";
Mol. Cell. Biol. 30:1769-1782(2010).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 200-623 IN COMPLEX WITH SSRNA
AND ATP, FUNCTION, AND MUTAGENESIS OF ARG-328; GLU-329; GLN-333;
ARG-378; ASP-381; GLN-525; ARG-528; THR-546; ARG-551 AND ASP-554.
PubMed=16630817; DOI=10.1016/j.cell.2006.01.054;
Sengoku T., Nureki O., Nakamura A., Kobayashi S., Yokoyama S.;
"Structural basis for RNA unwinding by the DEAD-box protein Drosophila
Vasa.";
Cell 125:287-300(2006).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 184-203 IN COMPLEX WITH GUS,
AND MUTAGENESIS OF ASP-184; ILE-185; 186-ASN--ASN-189;
186-ASN--ASN-188; ASN-187; ASN-188 AND ASN-189.
PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
"Structural basis for protein recognition by B30.2/SPRY domains.";
Mol. Cell 24:967-976(2006).
[20]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 184-203.
Structural genomics consortium (SGC);
"Crystal structure of human spla/ryanodine receptor domain and socs
box containing 1 (spsb1) in complex with a 20-residue vasa peptide.";
Submitted (DEC-2008) to the PDB data bank.
[21] {ECO:0000244|PDB:3EMW, ECO:0000244|PDB:3F2O}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 184-203 IN COMPLEX WITH
HUMAN SPSB1 AND SPSB2, AND MOTIF.
PubMed=20561531; DOI=10.1016/j.jmb.2010.06.017;
Filippakopoulos P., Low A., Sharpe T.D., Uppenberg J., Yao S.,
Kuang Z., Savitsky P., Lewis R.S., Nicholson S.E., Norton R.S.,
Bullock A.N.;
"Structural basis for Par-4 recognition by the SPRY domain- and SOCS
box-containing proteins SPSB1, SPSB2, and SPSB4.";
J. Mol. Biol. 401:389-402(2010).
-!- FUNCTION: Involved in translational control mechanisms operating
in early stages of oogenesis. Required maternally in many stages
of oogenesis, including cystocyte differentiation, oocyte
differentiation, and specification of anterior-posterior polarity
in the developing cysts. Essential for the formation and/or
structural integrity of perinuclear nuage particles during germ
cell formation. Required for gus, Fsn and aub accumulation at the
posterior pole of the embryo. Required for the localization of vas
to the perinuclear region of nurse cells.
{ECO:0000269|PubMed:10678180, ECO:0000269|PubMed:11526087,
ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:14588248,
ECO:0000269|PubMed:16630817, ECO:0000269|PubMed:18590813,
ECO:0000269|PubMed:20123973, ECO:0000269|PubMed:3052853,
ECO:0000269|PubMed:3140040, ECO:0000269|PubMed:8026330,
ECO:0000269|PubMed:9521895}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:8026330}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:8026330};
-!- SUBUNIT: Interacts with eIF5B and faf. Interacts with gus (via
B30.2/SPRY domain) and Fsn (via B30.2/SPRY domain). Interacts with
aub, me31B, eIF-4a and TER94. Interacts with piwi; this
interaction is RNA independent. Interacts with Dcr-1 and Fmr1;
these interactions occur in the polar granules.
{ECO:0000269|PubMed:10678180, ECO:0000269|PubMed:12479811,
ECO:0000269|PubMed:14588248, ECO:0000269|PubMed:16630817,
ECO:0000269|PubMed:16949822, ECO:0000269|PubMed:17189197,
ECO:0000269|PubMed:18590813, ECO:0000269|PubMed:20123973}.
-!- INTERACTION:
Q9V6L9:Fsn; NbExp=2; IntAct=EBI-134067, EBI-126933;
A1Z6E0:gus; NbExp=5; IntAct=EBI-134067, EBI-75338;
Q96BD6:SPSB1 (xeno); NbExp=2; IntAct=EBI-134067, EBI-2659201;
Q99619:SPSB2 (xeno); NbExp=2; IntAct=EBI-134067, EBI-2323209;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12479811,
ECO:0000269|PubMed:14588248, ECO:0000269|PubMed:16949822,
ECO:0000269|PubMed:20123973, ECO:0000269|PubMed:8026330}.
Note=Component of the meiotic nuage, also named P granule, a germ-
cell-specific organelle required to repress transposon activity
during meiosis. Later seen in the pole plasm at the posterior end
of the oocyte as a component of polar granules.
{ECO:0000269|PubMed:14588248, ECO:0000269|PubMed:8026330}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=P09052-1; Sequence=Displayed;
Name=solo;
IsoId=B6JUP5-1; Sequence=External;
-!- TISSUE SPECIFICITY: Abundantly expressed in the female germline.
Gus and faf are required for vas expression in the posterior pole
of the oocyte. {ECO:0000269|PubMed:12479811,
ECO:0000269|PubMed:14588248, ECO:0000269|PubMed:3052853,
ECO:0000269|PubMed:3140040, ECO:0000269|PubMed:9521895}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:3052853,
ECO:0000269|PubMed:3140040}.
-!- DOMAIN: The B30.2/SPRY domain-binding motif mediates recognition
by proteins containing a B30.2/SPRY domain.
{ECO:0000269|PubMed:20123973, ECO:0000269|PubMed:20561531}.
-!- PTM: Ubiquitinated during oogenesis. Deubiquitinated by faf, which
protects this protein from proteasome-mediated degradation.
{ECO:0000269|PubMed:14588248}.
-!- DISRUPTION PHENOTYPE: Defective growth of germline cysts. Fails to
efficiently accumulate many localized RNAs, such as Bic-D, orb,
osk and nos, but still accumulates grk RNA.
{ECO:0000269|PubMed:10678180, ECO:0000269|PubMed:3140040,
ECO:0000269|PubMed:9521895}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL89864.1; Type=Frameshift; Positions=50; Evidence={ECO:0000305};
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EMBL; X12945; CAA31405.1; -; Genomic_DNA.
EMBL; X12946; CAA31405.1; JOINED; Genomic_DNA.
EMBL; M23560; AAA29013.1; -; mRNA.
EMBL; AE014134; AAF53438.1; -; Genomic_DNA.
EMBL; AY084126; AAL89864.1; ALT_FRAME; mRNA.
PIR; A58768; A58768.
RefSeq; NP_001260458.1; NM_001273529.2. [P09052-1]
RefSeq; NP_001303322.1; NM_001316393.1. [P09052-1]
RefSeq; NP_723899.1; NM_165103.3. [P09052-1]
UniGene; Dm.4715; -.
PDB; 2DB3; X-ray; 2.20 A; A/B/C/D=200-623.
PDB; 2IHS; X-ray; 2.20 A; C/D=184-203.
PDB; 3EMW; X-ray; 1.80 A; B=184-203.
PDB; 3F2O; X-ray; 2.05 A; C/D=184-203.
PDB; 5NT7; X-ray; 1.40 A; B/D=463-623.
PDBsum; 2DB3; -.
PDBsum; 2IHS; -.
PDBsum; 3EMW; -.
PDBsum; 3F2O; -.
PDBsum; 5NT7; -.
ProteinModelPortal; P09052; -.
SMR; P09052; -.
BioGrid; 60902; 12.
DIP; DIP-20604N; -.
ELM; P09052; -.
IntAct; P09052; 9.
MINT; MINT-970294; -.
iPTMnet; P09052; -.
PRIDE; P09052; -.
EnsemblMetazoa; FBtr0304854; FBpp0293394; FBgn0262526. [P09052-1]
EnsemblMetazoa; FBtr0332472; FBpp0304748; FBgn0262526. [P09052-1]
GeneID; 26067080; -.
KEGG; dme:Dmel_CG46283; -.
CTD; 26067080; -.
FlyBase; FBgn0283442; vas.
KO; K13982; -.
OMA; FRGCRGG; -.
OrthoDB; EOG091G03JV; -.
PhylomeDB; P09052; -.
ChiTaRS; vas; fly.
EvolutionaryTrace; P09052; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0262526; -.
ExpressionAtlas; P09052; differential.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0043186; C:P granule; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Developmental protein; Differentiation; Helicase;
Hydrolase; Magnesium; Nucleotide-binding; Oogenesis; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Ubl conjugation.
CHAIN 1 661 ATP-dependent RNA helicase vasa, isoform
A.
/FTId=PRO_0000054976.
REPEAT 93 99 1.
REPEAT 100 106 2.
REPEAT 107 113 3.
REPEAT 114 120 4.
REPEAT 121 127 5.
DOMAIN 276 453 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 477 624 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 289 296 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 93 127 5 X 7 AA tandem repeats of [FS]-R-G-G-
[EQ]-G-G.
REGION 184 203 Required for posterior localization in
oocyte.
MOTIF 184 188 B30.2/SPRY domain-binding motif.
{ECO:0000269|PubMed:20123973,
ECO:0000269|PubMed:20561531}.
MOTIF 245 273 Q motif.
MOTIF 399 402 DEAD box.
MOD_RES 22 22 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 27 27 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 184 188 DINNN->AAAAA: Enhances protein stability.
Does not affect protein distribution in
the oocyte.
{ECO:0000269|PubMed:20123973}.
MUTAGEN 184 184 D->A: Decreases interaction with gus.
{ECO:0000269|PubMed:17189197,
ECO:0000269|PubMed:20123973}.
MUTAGEN 185 185 I->A: Decreases interaction with gus.
{ECO:0000269|PubMed:17189197}.
MUTAGEN 186 189 NNNN->ANNA: Strongly decreases
interaction with gus.
{ECO:0000269|PubMed:17189197}.
MUTAGEN 186 188 NNN->AAA: Abolishes interaction with gus.
{ECO:0000269|PubMed:17189197}.
MUTAGEN 187 187 N->A: Strongly decreases interaction with
gus. {ECO:0000269|PubMed:17189197,
ECO:0000269|PubMed:20123973}.
MUTAGEN 188 188 N->A: Strongly decreases interaction with
gus. {ECO:0000269|PubMed:17189197,
ECO:0000269|PubMed:20123973}.
MUTAGEN 189 189 N->A: Does not affect interaction with
gus. {ECO:0000269|PubMed:17189197,
ECO:0000269|PubMed:20123973}.
MUTAGEN 256 256 I->N: Fails to bind and unwind RNA.
{ECO:0000269|PubMed:8026330}.
MUTAGEN 271 271 I->M: Fails to bind and unwind RNA.
{ECO:0000269|PubMed:8026330}.
MUTAGEN 328 328 R->A: Reduction in RNA-binding, reduced
RNA-dependent ATPase and unwinding
activities.
{ECO:0000269|PubMed:16630817}.
MUTAGEN 329 329 E->A: Increase in RNA-binding and no
significant change to RNA-dependent
ATPase or unwinding activities.
{ECO:0000269|PubMed:16630817}.
MUTAGEN 333 333 Q->A: Reduction in RNA-binding, drastic
reduction in unwinding activities, no
significant change to RNA-dependent
ATPase activity.
{ECO:0000269|PubMed:16630817}.
MUTAGEN 378 378 R->A: Reduction in RNA-binding,
significantly reduced RNA-dependent
ATPase and unwinding activities.
{ECO:0000269|PubMed:16630817}.
MUTAGEN 381 381 D->A: Increase in RNA-binding.
{ECO:0000269|PubMed:16630817}.
MUTAGEN 525 525 Q->A: Reduction in RNA-binding, abolished
unwinding activities and no significant
change to RNA-dependent ATPase activity.
{ECO:0000269|PubMed:16630817}.
MUTAGEN 528 528 R->A: Reduction in RNA-binding, barely
detectable RNA-dependent ATPase activity
and completely defective unwinding
activity. {ECO:0000269|PubMed:16630817}.
MUTAGEN 546 546 T->A: Moderately decreased the RNA
binding, abolished both the RNA-dependent
ATPase and unwinding activities.
{ECO:0000269|PubMed:16630817}.
MUTAGEN 551 551 R->A: Reduction in RNA-binding, drastic
reduction in unwinding activities and no
significant change to RNA-dependent
ATPase activity.
{ECO:0000269|PubMed:16630817}.
MUTAGEN 552 552 G->E: Fails to unwind RNA.
{ECO:0000269|PubMed:8026330}.
MUTAGEN 554 554 D->A: No change to RNA-binding, abolished
unwinding activities and no significant
change to RNA-dependent ATPase activity.
{ECO:0000269|PubMed:16630817}.
CONFLICT 35 35 A -> R (in Ref. 3; AAA29013).
{ECO:0000305}.
CONFLICT 153 165 Missing (in Ref. 3; AAA29013).
{ECO:0000305}.
CONFLICT 192 192 V -> A (in Ref. 1; CAA31405 and 3;
AAA29013). {ECO:0000305}.
CONFLICT 265 265 Y -> F (in Ref. 1; CAA31405).
{ECO:0000305}.
CONFLICT 322 322 V -> C (in Ref. 3; AAA29013).
{ECO:0000305}.
CONFLICT 452 452 F -> S (in Ref. 1; CAA31405).
{ECO:0000305}.
CONFLICT 582 582 R -> C (in Ref. 1; CAA31405).
{ECO:0000305}.
CONFLICT 594 594 D -> H (in Ref. 3; AAA29013).
{ECO:0000305}.
STRAND 189 192 {ECO:0000244|PDB:3F2O}.
HELIX 195 199 {ECO:0000244|PDB:3F2O}.
HELIX 211 214 {ECO:0000244|PDB:2DB3}.
HELIX 225 230 {ECO:0000244|PDB:2DB3}.
STRAND 233 239 {ECO:0000244|PDB:2DB3}.
HELIX 247 249 {ECO:0000244|PDB:2DB3}.
HELIX 254 262 {ECO:0000244|PDB:2DB3}.
HELIX 270 280 {ECO:0000244|PDB:2DB3}.
STRAND 285 288 {ECO:0000244|PDB:2DB3}.
HELIX 295 309 {ECO:0000244|PDB:2DB3}.
STRAND 320 324 {ECO:0000244|PDB:2DB3}.
HELIX 328 341 {ECO:0000244|PDB:2DB3}.
TURN 342 344 {ECO:0000244|PDB:2DB3}.
HELIX 358 365 {ECO:0000244|PDB:2DB3}.
STRAND 370 374 {ECO:0000244|PDB:2DB3}.
HELIX 376 384 {ECO:0000244|PDB:2DB3}.
STRAND 395 399 {ECO:0000244|PDB:2DB3}.
HELIX 401 404 {ECO:0000244|PDB:2DB3}.
TURN 407 409 {ECO:0000244|PDB:2DB3}.
HELIX 410 418 {ECO:0000244|PDB:2DB3}.
STRAND 427 433 {ECO:0000244|PDB:2DB3}.
HELIX 437 444 {ECO:0000244|PDB:2DB3}.
STRAND 451 457 {ECO:0000244|PDB:2DB3}.
STRAND 465 471 {ECO:0000244|PDB:2DB3}.
HELIX 474 476 {ECO:0000244|PDB:2DB3}.
HELIX 477 487 {ECO:0000244|PDB:2DB3}.
STRAND 492 495 {ECO:0000244|PDB:2DB3}.
HELIX 499 511 {ECO:0000244|PDB:2DB3}.
STRAND 516 520 {ECO:0000244|PDB:2DB3}.
HELIX 525 536 {ECO:0000244|PDB:2DB3}.
STRAND 541 545 {ECO:0000244|PDB:2DB3}.
HELIX 547 549 {ECO:0000244|PDB:2DB3}.
STRAND 560 565 {ECO:0000244|PDB:2DB3}.
HELIX 570 577 {ECO:0000244|PDB:2DB3}.
STRAND 587 593 {ECO:0000244|PDB:2DB3}.
TURN 595 597 {ECO:0000244|PDB:2DB3}.
HELIX 599 601 {ECO:0000244|PDB:2DB3}.
HELIX 602 611 {ECO:0000244|PDB:2DB3}.
HELIX 618 620 {ECO:0000244|PDB:2DB3}.
SEQUENCE 661 AA; 72331 MW; 8617C25CCB3130B9 CRC64;
MSDDWDDEPI VDTRGARGGD WSDDEDTAKS FSGEAEGDGV GGSGGEGGGY QGGNRDVFGR
IGGGRGGGAG GYRGGNRDGG GFHGGRREGE RDFRGGEGGF RGGQGGSRGG QGGSRGGQGG
FRGGEGGFRG RLYENEDGDE RRGRLDREER GGERRGRLDR EERGGERGER GDGGFARRRR
NEDDINNNNN IVEDVERKRE FYIPPEPSND AIEIFSSGIA SGIHFSKYNN IPVKVTGSDV
PQPIQHFTSA DLRDIIIDNV NKSGYKIPTP IQKCSIPVIS SGRDLMACAQ TGSGKTAAFL
LPILSKLLED PHELELGRPQ VVIVSPTREL AIQIFNEARK FAFESYLKIG IVYGGTSFRH
QNECITRGCH VVIATPGRLL DFVDRTFITF EDTRFVVLDE ADRMLDMGFS EDMRRIMTHV
TMRPEHQTLM FSATFPEEIQ RMAGEFLKNY VFVAIGIVGG ACSDVKQTIY EVNKYAKRSK
LIEILSEQAD GTIVFVETKR GADFLASFLS EKEFPTTSIH GDRLQSQREQ ALRDFKNGSM
KVLIATSVAS RGLDIKNIKH VINYDMPSKI DDYVHRIGRT GRVGNNGRAT SFFDPEKDRA
IAADLVKILE GSGQTVPDFL RTCGAGGDGG YSNQNFGGVD VRGRGNYVGD ATNVEEEEQW
D


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