ID A0A2U4C9V9_TURTR Unreviewed; 1262 AA.
AC A0A2U4C9V9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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|RefSeq:XP_019802235.1,
GN ECO:0000313|RefSeq:XP_019802237.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019802237.1};
RN [1] {ECO:0000313|RefSeq:XP_019802235.1, ECO:0000313|RefSeq:XP_019802237.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019802235.1,
RC ECO:0000313|RefSeq:XP_019802237.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_019802235.1; XM_019946676.2.
DR RefSeq; XP_019802237.1; XM_019946678.2.
DR RefSeq; XP_019802238.1; XM_019946679.1.
DR GeneID; 101323418; -.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000245320; Chromosome 10.
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 ECO:0000313|RefSeq:XP_019802235.1};
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:UP000245320}.
FT DOMAIN 471..639
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 681..895
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1262 AA; 140865 MW; A971D1D3F1CBE47C CRC64;
MDLKDSSPGF QLSLLARNVQ PGLIQKRSGP AQAASVQTSP TPSSTHVCQP CPWRDHFSRL
NVNISNMAAS RDLLKEFPQP KNLLNSVIGR ALGISHAKDK LVYVHTNGPK KKKVTLHIKW
PKSVEVEGYG SKKIDAERQA AAAACQLFKG WGLLGPRNEL FDAAKYRVLA DRFGSPADSW
WRPEPTMPPT SWRQLNPESI RPGGPGGLSR SLGREEEEDE EEELEEGTID VTEFLSMAQQ
DSHTPLRDSR GGSFEMTDDD SAIRALTQFP LPKNLLAKVI QIATSSSTAK NLMQFHTVGT
KTKLSTLTLL WPCPMTFVAK GRRKAEAENK AAALACKKLK SLGLVDRNNE PLTHAMYNLA
SLRELGETQR RPCTIQVPEP ILRKIETFLN HYPMDSSWIS PELRLQSDDI LPLGKDSGPL
GDPITGKPYM PLSETEELRL SQSLLELWRR RGPVWQEAPQ LPVDPHRDTI LSAIEQHPVV
VIAGDTGCGK TTRIPQLLLE RYVTEGRGAR CNVIITQPRR ISAVSVAQRV SHELGPSLRR
NVGFQVRLES KPPARGGALL FCTVGILLRK LQSNPSLEGV SHVIVDEVHE RDVNTDFLLI
LLKGLQRLNP ALRLVLMSAT GDNERFSRYF GGCPVIKVPG FMYPVKEHYL EDILAKLGKH
QYPHRHRHHE SEDECALDLD LVTDLVLHID ARGEPGGILC FLPGWQEIKG VQQRLQEALG
MHESKYLILP VHSNIPMMDQ KAIFQQPPVG VRKIVLATNI AETSITINDI VHVVDSGLHK
EERYDLKTKV APISWPCPSP DLPWACVSGE GHTCGISLSL LWGAVEELSE VSCLETVWVS
RANVIQRRGR AGRCQSGFAY HLFPRSRLEK MAPFQVPEIL RTPLENLVLQ AKIHMPEKTA
VEFLSKAVDS PNIKAVDEAV ILLQEIGVLD QREYLTTLGQ RLAHISTDPR LAKAIVLAAI
FRCLHPLLVV VSCLTRDPFS SSLQNRAEVD KVKALLSHDS GSDHLAFVRA VSGWEEVLRW
QDRSSRENYL EENLLYAPSL RFIHGLIKQF SENIYEAFLV GKPSDCTLAS AQCNEYSEEE
ELVKGVLMAG LYPNLIQVRQ GKVTRQGKFK PNSVTYRTKS GNILLHKSTI NREATRLRSR
WLTYFMAVKS NGSVFVRDSS QVHPLAVLLL TDGDVHIRDD GRRATISLSD SDLLRLEGDS
RTVRLLRELR RALGRMVERS LRSELAALPP CVQEEHGQLL ALLAELLRGP CGSFDVRKTA
DD
//
