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Database: UniProt
Entry: A0A2B4SVS7_STYPI
LinkDB: A0A2B4SVS7_STYPI
Original site: A0A2B4SVS7_STYPI 
ID   A0A2B4SVS7_STYPI        Unreviewed;       962 AA.
AC   A0A2B4SVS7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=ddx4 {ECO:0000313|EMBL:PFX32567.1};
GN   ORFNames=AWC38_SpisGene2606 {ECO:0000313|EMBL:PFX32567.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX32567.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
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. DDX4/VASA
CC       subfamily. {ECO:0000256|ARBA:ARBA00010132}.
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:PFX32567.1}.
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DR   EMBL; LSMT01000021; PFX32567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4SVS7; -.
DR   STRING; 50429.A0A2B4SVS7; -.
DR   Proteomes; UP000225706; 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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00590; RRM_SF; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF11; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00098; zf-CCHC; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 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.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50158; ZF_CCHC; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PFX32567.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          40..117
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          399..414
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          422..436
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          499..527
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          530..715
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          727..888
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          117..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           499..527
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        131..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..928
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..954
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   962 AA;  105333 MW;  E8C99B0B0A9B3413 CRC64;
     MQGYTQEPSP QPLAIVTDET ARYNESSHSN FSKPFQREEY KVCVKNVPID MSKESLEALF
     RSCGNVTSVN ILPPKPERNS TIGFVAFSSE DELSKAIDAV NGTLLGGHSL RVEQAIPRDR
     NTGASGKDFQ HPGGYQNTQS FYQRRTDQQP GRGQHEQAGG RGQYNQHVGR GQYGEVGVRG
     QLEQPRGRGH YEQPGGRGTY QQPGGMVPHQ HPGGWGPYGK PVIRGQHEQP GGWEPYQQPE
     GWGQHEQPGG RKPYEQSGGR GMYELPGRRG QYQHPRGRGP YHGHQSGVMM RSFQNMGVSV
     EQAIFNPSGP GRGVGMMQSF GTSSEVVPGG ASSVLNGVTN SYPHEAEALQ TNGVQHMWDE
     TSSPEVQELT GRLPQNSVTQ GNATNLQPHA PVHNGGQSCY KCGGTGHFAK QCESSGALDK
     SCHGCGEEGH FARECPAVAN SQRQKGTGNK VGPVTYIPPE LPSDISELFQ DAPHSGLNFD
     KYDDIPVKVS GKGSVSPISS FEEAGILEQC LKNIKRAEFT KPTPIQKYAI PIALEGRDLM
     ACAQTGSGKT VAFVVPVLTA MIKQDHLSGG SLTGEIPAPS ALCIVPTREL AVQIFKEVCK
     FADGTVVCPA VCYGGVSVPH QLAKIRKGSH FLIATPGRLE DFVSKNEVSL EKVRYLILDE
     ADRMLDMGFE QTVRKLVENF GMPDKVQRQT LMFSATFPDD IQRLAADFLK EDYLFVIVGR
     IGGSNLDISQ TVISVPGDDK QEKLFNILLN SGTDRTLIFV ELKRVADFLA CLLSQNNFPT
     TSISGDRTQQ EREAALQDFR SGRAPVLVAT SVAARGLDIP DVKHVINYDL PQDIEEYVHR
     IGRTGRIGNK GRATSFFQPG KDDRLARSLV KVLSEAYQEV PDWLEHVAEE AIGSSYGPAG
     GRFASKDRRE REHLRGSGSR DLMGEVNRRM EQLDVQSQNR PHPGEANSLT DQSGYPDEEE
     WD
//
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