ID A0A0V0WV97_9BILA Unreviewed; 1066 AA.
AC A0A0V0WV97;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP-dependent RNA helicase DHX30 {ECO:0000256|ARBA:ARBA00039388};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=DEAH box protein 30 {ECO:0000256|ARBA:ARBA00042917};
GN Name=DHX30 {ECO:0000313|EMBL:KRX79219.1};
GN ORFNames=T06_6690 {ECO:0000313|EMBL:KRX79219.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX79219.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX79219.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX79219.1};
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000256|ARBA:ARBA00004436}.
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:KRX79219.1}.
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DR EMBL; JYDK01000056; KRX79219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WV97; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
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; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd00048; DSRM_SF; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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:SF229; ATP-DEPENDENT RNA HELICASE DHX30; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 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:KRX79219.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00023271};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT DOMAIN 337..505
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 543..710
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1066 AA; 122297 MW; 3C4ACFF8816308DA CRC64;
MSYIKCSVKS KLERCGVEAA FAKNPKATLL SFFQAMRWKM PSILTERTGL SHEAIWHCRI
SFLLPESDNL LTFNSCVDSK SKSEAESWAA YSACKFLSEK YDHFPSRKKS ITPEKIKADE
LLESQKWSQL GRHPKSVVHE FYQARGFDKL PLENGKITVS LTAEVPLVFS SVISRNTRKH
AVAVAYWEFL LKLKEAKYVD DNFNVIFHSK QEIMEFKRNQ RLPTFIDISE SLFCRIDCLV
KEFHLFSKDF MQSVQRLRIK QAVDKLINSN GCSVNLNEEE DEDGSVDECL ELDMILKRNH
SLYTSAQRLR NSFDPAVINL RSFRQQLPIF VIKDELLSTL QHHQVVIIAG DTGCGKTTHI
PQFIFDDYVT KFRGAECNII VTQPRRISAI AMANRLAAER QEAVGETVGF NVRLNCCIPR
NKGSILFLTP GTFLRSAMFT EQIENISHVI IDEVHERDVL TDLMLVFLKR KLVILPKLKL
ILMSASINPY KFSSYFNNCP VLSAAGRIFD VAEYFLDDVY RFLGREMPSE EIVDHDYETD
ANLVAELLCW IHKNRPNGDV LCFLPSWNDI CRVSGLLDAR KCSEEQMVVL PCHSSLPISE
QKRIFEPMSC GKRKIVLATN IAETSLTIDN IRYVVNTGTR KIGRLISSKN WLSHHQSWAS
KSSQIQRKGR AGRQMEGECY HLFSKEVYQN MPEYDVPTIQ AAPLERLALM TKSLFKNSDP
FQVLSEALDP PSKEGLDAAR HLLQDLKIFD KENRLTELGK NVALFGCHPF LGIALLYSII
FRCTEPILSI VACLESDENF FDLSFSNKDQ IIKLLDYLIG RSFSLHCSAV NLCRFGCDLM
RHHKLRKQFA EEVVRSNLVD EWKDLFSLDH PLNLSSNNFE IIKAVIMAGV FQNVAKGIHG
ILSKRGKIEP DAVTICESNL KPVRPRRYGN YILKESDNWW SDWFIYYKKI WSEKSRSFAV
EGLSMINPLI AVLFSGFTPE ILQSDNATVI ALVPAKHFQL QVSSARNAEL LIRLRSCIHD
FFDLYINHHE YIMKLAENDP IKKWHNDLLT LITDLLNMEQ NYNSKQ
//
