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Database: UniProt
Entry: A0A1X7VTM7_AMPQE
LinkDB: A0A1X7VTM7_AMPQE
Original site: A0A1X7VTM7_AMPQE 
ID   A0A1X7VTM7_AMPQE        Unreviewed;      1049 AA.
AC   A0A1X7VTM7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=100637149 {ECO:0000313|EnsemblMetazoa:Aqu2.1.43696_001};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.43696_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20686567; DOI=10.1038/nature09201;
RA   Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA   Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA   Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA   Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA   Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA   Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The Amphimedon queenslandica genome and the evolution of animal
RT   complexity.";
RL   Nature 466:720-726(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.43696_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2017) to UniProtKB.
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};
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DR   RefSeq; XP_011402843.1; XM_011404541.2.
DR   AlphaFoldDB; A0A1X7VTM7; -.
DR   STRING; 400682.A0A1X7VTM7; -.
DR   EnsemblMetazoa; Aqu2.1.43696_001; Aqu2.1.43696_001; Aqu2.1.43696.
DR   GeneID; 100637149; -.
DR   KEGG; aqu:100637149; -.
DR   eggNOG; KOG0923; Eukaryota.
DR   InParanoid; A0A1X7VTM7; -.
DR   OrthoDB; 5488182at2759; -.
DR   Proteomes; UP000007879; 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; cd17974; DEXHc_DHX16; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
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; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007879}.
FT   DOMAIN          414..578
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          596..776
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          108..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1049
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          913..940
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        128..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1049 AA;  120259 MW;  A5333767EE206C75 CRC64;
     MADVVAWVGD QLYEILGLSD RYTAEFLVGL AKKSSSLDGF VSQLESTGAL TIDHKTREFA
     SELWARVPHK AVVEKPARAK EREAKLQTQR NKSYQILYDS GDEEEEAIMK KRRSSLSSGK
     GIKNSKRNIR KDKSSQWESD SSSSEEEKEM KAKRVRVEEP KEEEEDEWDA MEKEREKDLL
     ERDALNERIK KKDKEKTRKI VEKSDKKGYE EARKRLQVAE KDQKKLIPEL RKKSRIRYLG
     DRAQDKLAEL DADIIDNEYL FSDTKLTKRE EAEHLRKKKL KELADEHRNA KDMEKIERYH
     IPSEKEKPSA RYEEPRKEEL LGPNADLRKW EDEQLGIALV RFGAKDAKEK NKQKEYDLVM
     DDEVAFVLAE TVAGSKGENE EEMPEGPSVE ERRKMNLEET RRSLPIFPYR EPLLEAVENH
     QILIIEGETG SGKTTQIPQY LYEAGYCSNK MKIGCTQPRR VAAMSVAARV SAEMGVKLGN
     EVGYSIRFED CTSERTVIKY MTDGMLLREF LGEPDLESYS VMIIDEAHER TLHTDVLFGL
     VKDIARFRPD LKLLVSSATM DTKKFSEFFD DAPIFRIPGR RYPVDLYYTK APEADYLDAA
     VVSVLQIHLT QPRGDILVFL TGQEEIETTY EMLKERTAKL GSRIGELVIL PIYANLPSDM
     QAKIFEPTPP GARKVVLATN IAETSLTIDG IIFVIDPGFC KQKSYNPRTG MESLVVVPCS
     KASSNQRAGR AGRVAAGKCF RLFTSWAYHN EMEDTTIPEI QRTNLGNVVL LLKSLGINDL
     INFDFMDPPP PETLMLALEQ LYALGALNHM GELTKLGRRM AEFPVDPAMS KMLIVSEKYG
     CSEEILTITA MLSVNNAIFY RPKDRVVHAD TARQSFFRPG GDHLTLLAVY NDWVSTDYST
     QWCFDNFIQH RSMKRARDVR DQLEGLMERV EIDLASSEDV VAIRKAITAG YFYHAARLSK
     GGYRTAKHQQ VVHIHPNSSL FEDQPRWVIY FELVFTSKEY MRQVIEIDNQ WLLEVAPHYY
     KAKDIQDENR KMPKGAGASR DDTRFDNQF
//
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