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Database: UniProt
Entry: Q4SWK6_TETNG
LinkDB: Q4SWK6_TETNG
Original site: Q4SWK6_TETNG 
ID   Q4SWK6_TETNG            Unreviewed;      1027 AA.
AC   Q4SWK6;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=GSTENG00011441001 {ECO:0000313|EMBL:CAF94976.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|EMBL:CAF94976.1};
RN   [1] {ECO:0000313|EMBL:CAF94976.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|EMBL:CAF94976.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU365068}.
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:CAF94976.1}.
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DR   EMBL; CAAE01013614; CAF94976.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4SWK6; -.
DR   KEGG; tng:GSTEN00011441G001; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17949; DEADc_DDX31; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   PANTHER; PTHR24031:SF89; ATP-DEPENDENT RNA HELICASE DDX31-RELATED; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU365068};
KW   Helicase {ECO:0000256|RuleBase:RU365068};
KW   Hydrolase {ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU365068};
KW   RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          111..270
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          966..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        6..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..437
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..579
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..749
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1027 AA;  111050 MW;  F5D50235F11999C5 CRC64;
     MKQRGEKRRL TPTEEASSSK RSRLQHGGEE LPAAQAPQKK KATEKSGPKT SSLFRNNPEI
     PQVHRATVSQ VEEEIFTSDT FTQMSLHPHL VTTLNNVFNV STVTSVQRQT IPVLLSGRDA
     LVRSQTGSGK TLSYAIPVVQ SLQALQPKVS RGDGPLALIL VPTRELAQQT FVTFQKLLKP
     FTWVVPGVLM GGEKRKAEKA RLRKGINILV STPGRLVDHI RNTLSISFSA VRWLVLDEAD
     RTLDLGFEKD LSVILNSVNS AASSRQNVLL VSPLSHRRLC SSLWWWFPAK SDWCVWLLSS
     WANASFLRTT KSSSSSPAAR RPSSSTCCSP PSSGGPRPIR TLESASCVSM ATCSRRQERG
     SGADRCVPAL RCVRLRSPAV HGQSGRRQQP RPTPLAANRC SPCVSGCSGS RSGPAAGHLD
     PAVHAPHDGR RVRAPRRADG ASGPGGQQPH LPHASRDGLR GGTGQSQHQP IRNQAAGHPL
     QLDDGRHLQG AGQVPQQEPR HTFQSAVGGA RRQWLGAGQS HPRWCRPAAP AQLLLGPASA
     VLVGQQVRQR GRGPGGHRRQ PPSAEPPPAG EPPSPPAPQS KRSLGRRPGC LGFGAVALLN
     DHAHLGPHVF TSSPALAGGG APALAESHGR AVAGSGLRAC RRQPVHGRGP AGHPEQRQPE
     EQRHQLLVGL AAPVLLLLVR TLYPVLQHVE GPGRGRQRLA GCDRRLGVGL RSGREPRDLP
     GVWDPAVPNN QGRPSRRRPS RRRPRRRRSA AVTLPSASGQ FFHAHSPETD RGTPFRGANR
     QVQTVRQVMV DILQNHTKLD WPDRCPRLEP YRYPAAFFSL NIHPSSRNPE EILVFSTQRL
     FRPQLRGPAP PVRSEVRGLH RHRGGGARLL RGTRGELSAA DGGAAGLIRI FSGSGDPGPA
     DVLRRAGEES AELGAPPGGG SWALQSFLRA YTTYPARLKH IFHIRSLHLG HTAKSFALRE
     APQALGAARL PPGGGAKSRK RRSQNRPESQ VTPPGPRSVM ERVCVCCISA SSLLITTHTH
     THTHSCL
//
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