ID A0A0V1CVA6_TRIBR Unreviewed; 1125 AA.
AC A0A0V1CVA6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:KRY53233.1};
GN ORFNames=T03_16121 {ECO:0000313|EMBL:KRY53233.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53233.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY53233.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY53233.1};
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:KRY53233.1}.
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DR EMBL; JYDI01000090; KRY53233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CVA6; -.
DR STRING; 45882.A0A0V1CVA6; -.
DR Proteomes; UP000054653; 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:KRY53233.1};
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:UP000054653}.
FT DOMAIN 337..505
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 543..725
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1125 AA; 129274 MW; 86CA7D9E7A78FAD5 CRC64;
MSYIKCSVKS KLERCGVEAA FAKNPKATLL SFFQAMRWKM PSILTERTGL SHEAIWHCRI
SFLLPESDNL LTFNSCVDSK SKSEAESWAA YSACKFLSEK YDHFPSRKKS ITPEKIKADE
LLESQKWSQL GRHPKSVVHE FYQARGFDKL PLENGKITVS LTAEVPLVFS TVISRNTRKH
AVAVAYWEFL LKLKEAKYVD DNFNVIFHSK QEIMEFKRNQ RLPTFIDISE SLFRRIDCLV
KEFHLFSKDF MQSVQRLRIK QAVDKLINSN GCSVNLNKEE DEDGSIDECL ELDMILKRNH
SLYTSAQRLR NSFDPAVINL RSFRQQLPIF VIKDELLSTL EHHQVVIIAG DTGCGKTTQI
PQFIFDDYVT KFRGAECNII VTQPRRISAI AMANRLAAER QEAVGETVGF NVRLNCCIPR
NKGSILFLTP GTFLRSAMFT EQIENISHVI IDEVHERDVL TDLMLVFLKR KLVILPKLKL
ILMSASINPY KFSSYFNNCP VLSAAGRIFD VAEYFLDDVY RFLGREMPSE EIVDHDYETD
ANLVAELLCW IHKNRPVRSN SFFNNFNYPN ENGDVLCFLP SWNDICRVSG LLDARKCSEE
QMVVLPCHSS LPISEQKRIF EPMSCGKRKI VLATNIAETS LTIDNIRYVV NTGTRKIGRL
ISSKNWLSHH QSWASKSSQI QRKGRAGRQM EGECYHLFSK EVYQNMPEYD VPTIQAAPLE
RLALMTKSLF KNSDPFQVLS EALDPPSKEG CKSNLRFTIE ILVVAFFPVD AARHLLQDLK
IFDKENRLTE LGKNVALFGC HPFLGIALLY SIIFRCTEPI LSIVACLESD ENFFDLSFSN
KGQIIKMLDY LIGRSFSLHS SAVNLCRFGC DLMWQHSSET DEWKSNIFSK NFISLRSVVF
ILELRKQFAE EVVRSNLVDE WKDLFSLDHP LNLSSNNFEI IKAVIMAGLF QNVAKGIHGI
LSKRGKIEPD AVTICESNLK PVRPRRYGNY ILKESDNWWS DWFIYYKKIW SEKSRSFAVE
GLSMINPLIA VLFSGFTPEI LQSDNATVIA LVPAKHFQLQ VSSARNAELL IRLRSCIHDF
FNLYINHHEY IMKLAENDPI KKWHNDLLTL ITDLLNMEQN YNSKQ
//
