ID   A0A2K5XPL2_MANLE        Unreviewed;      1168 AA.
AC   A0A2K5XPL2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
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|Ensembl:ENSMLEP00000005254.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000005254.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000005254.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A2K5XPL2; -.
DR   Ensembl; ENSMLET00000025675.1; ENSMLEP00000005254.1; ENSMLEG00000023203.1.
DR   GeneTree; ENSGT00940000158279; -.
DR   Proteomes; UP000233140; Unplaced.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17976; DEXHc_DHX30; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.30.160.20; -; 2.
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: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   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:0000256|ARBA:ARBA00022806};
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:UP000233140}.
FT   DOMAIN          418..586
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          628..801
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          124..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1168 AA;  130854 MW;  68BFECC4AE9A7B4D CRC64;
     CPCSEKAPQV ISVHPASRDL LKEFPQPKNL LNSVIGRALG ISHAKDKLVY VHTNGPKKKK
     VTLHIKWPKS VEVEGYGSKK IDAERQAAAA ACQLFKGWGL LGPRNELFDA AKYRVLADRF
     GSPADSWWRP EPTMPPTSWR QLNPESIRPG GPGGLSRSLG REEEEDEEEE LEEGTIDVTD
     FLSMTQQDSH TPLRDSRGSS FEMTDDDSAI RALTQFPLPK NLLAKVIQIA TSSSTAKNLM
     QFHTVGTKTK LSTLNLLWPC PMTFVAKGRR KAEAENKAAA LACKKLKSLG LVDRNNEPLT
     HAMYNLASLR ELGETQRRPC TIQVPEPILR KIETFLNHYP VESSWIAPEL RLQSEDILPL
     GKDSGPLSDP ITGKPYVPLL EAEEVRLSQS LLELWRRRGP VWQEAPQLPV DPHRDTILNA
     IEQHPVVVIS GDTGCGKTTR IPQLLLERYV TEGRGARCNV IITQPRRISA VSVAQRVSHE
     LGPSLRRNVG FQVRLESKPP ARGGALLFCT VGILLRKLQS NPSLEGVSHV IVDEVHERDV
     NTDFLLILLK GLQRLNPALR LVLMSATGDN ERFSRYFGGC PVIKVPGFMY PVKEHYLEDI
     LAKLGKHQYL HRHRHHESED ECALDLDLVT DLVLHIDARG EPGGILCFLP GWQEIKGVQQ
     RLQEALGMHE SKYLILPVHS NIPMMDQKAI FQQPPVGVRK IVLATNIAET SITINDIVHV
     VDSGLHKEER YDLKTKVSCL ETVWVSRANV IQRRGRAGRC QSGFAYHLFP RSRLEKMVPF
     QVPEILRTPL ENLVLQAKIH MPEKTAVEFL SKAVDSPNIK AVDEAVILLQ EIGVLDQREY
     LTTLGQRLAH ISTDPRLAKA IVLAAIFRCL HPLLVVVSCL TRDPFSSSLQ NRAEVDKVKA
     LLSHDSGSDH LAFVRAVAGW EEVLRWQDRS SRENYLEENL LYAPSLRFIH GLIKQFSENI
     YEAFLVGKPS DCTLASAQCN EYSEEEELVK GVLMAGLYPN LIQVRQGKVT RQGKFKPNSV
     TYRTKSGNIL LHKSTINREA TRLRSRWLTY FMAVKSNGSV FVRDSSQVHP LAVLLLTDGD
     VHIRDDGRRA TISLSDSDLL RLEGDSRTVQ LLRELRRALG RMVERSLRSE LAALPPSVQE
     EHGQLLALLA ELLRGPCGSF DVRKTADD
//