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Database: UniProt
Entry: A0A0V1BZD7_TRISP
LinkDB: A0A0V1BZD7_TRISP
Original site: A0A0V1BZD7_TRISP 
ID   A0A0V1BZD7_TRISP        Unreviewed;      1115 AA.
AC   A0A0V1BZD7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=DHX37 {ECO:0000313|EMBL:KRY42156.1};
GN   ORFNames=T01_11025 {ECO:0000313|EMBL:KRY42156.1};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY42156.1, ECO:0000313|Proteomes:UP000054776};
RN   [1] {ECO:0000313|EMBL:KRY42156.1, ECO:0000313|Proteomes:UP000054776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS3 {ECO:0000313|EMBL:KRY42156.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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. DEAH subfamily.
CC       {ECO:0000256|ARBA:ARBA00008792}.
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:KRY42156.1}.
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DR   EMBL; JYDH01000005; KRY42156.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1BZD7; -.
DR   STRING; 6334.A0A0V1BZD7; -.
DR   eggNOG; KOG0926; Eukaryota.
DR   InParanoid; A0A0V1BZD7; -.
DR   Proteomes; UP000054776; 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   GO; GO:0022414; P:reproductive process; IEA:UniProt.
DR   CDD; cd17982; DEXHc_DHX37; 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; 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:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:KRY42156.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054776}.
FT   DOMAIN          241..408
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          511..685
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1115 AA;  127338 MW;  E4A76D82A100935B CRC64;
     MSRQISFNIG EIMSEEPTYI LAHDTSNAFV LEPRKKQVNK SNKDASIKGV NISTKKKLKA
     KCISKKKAKE LKKILSRKRK NVDRNVIYEK LSRWKISDEE MKLLNSVSGL HEKLKRRKSD
     LKFDEKIQSE ELNYPAENGN FVNNNLIQYF ETETSAENEK SEHDNHEYVQ NNISNADISV
     QEQSVKLAVS AESTVSSVIE NKQSLKLVNN KTATYVPIYR QPDIEKQRLK LPVVAEEQVI
     MEAIKECPVV IICGETGSGK TTQVPQFLYE AGMALNGKII GITEPRRVAA ISMSKRVAEE
     MNVGVDVVSY QIRFEGNTTE HTKVKFMTDG VLLREIQKDF LLSNYSAILI DEAHERSMYS
     DILIGLLSRI ILLRQKRNDK LHLVIMSATL RVEDFLSPKL FKQTPRVIHV SSRQYPVTVY
     FNRHTDEDYL AAAFRKVCQV HRLLPEGAIL VFVSGQQEVY TLVSWLKKTF PMEGIVKIDN
     NSSEKFQRRN FSMKSKRKRE NYRPRNDTVI NLDDYIIPAD DKVDLNEMDA PDLDLFDTVE
     PKDDIILSDL KNEEIPLYCL PLYSLMESKK QARIFEPIPE GCRLCIISTN VAETSITIPN
     VRYVVDTGKE KVRLYDPVTG ISKFVVHWIS KASADQRAGR AGRVAPGHCY RLYSSAVYNE
     FEKYSTPEIL TKPPDDLVLQ MKSMNILRVQ NFPFPSPLSV EALQASEERL LKLDLLERQV
     DCKGKEVTKI TNLGRSVALF PLAPRYGKML SLACQRNLLA HAVCLVAALS VREVLINPSS
     ISAPNVEEKK KRIKACLNCR RDLAGQGQSL LMGDFGVMLQ SVLLAEKSNN LSGVCKSYSI
     RMKALLEIRK LRRQLTNMIN LIFPGIDLTL DQKLEIPNSE RMILLRQLLL IGLCDNVARR
     NDAVSNNNRI AYSSSVIKDH LWIHPSSTLV KLQPEWVVYQ EVIDGCNEKK CMINVLAIEP
     DWLPKLAKGY CHFGEPLKTI QPHYSAEQDC ITCIVDCTYG VSGWFLSRLQ VKHAENLDYY
     RYLAVEFLNG NVFSKLQAYK KYLVTSPSII FKPWAKIQTR TDRFLRALVN GKISSKADLI
     RVWSTEKKFL RSEYLEWLIE AKHAEVMSIW PPLDK
//
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