ID A0A1S3G6H5_DIPOR Unreviewed; 1220 AA.
AC A0A1S3G6H5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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_012883617.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012883617.1};
RN [1] {ECO:0000313|RefSeq:XP_012883617.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012883617.1};
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_012883617.1; XM_013028163.1.
DR AlphaFoldDB; A0A1S3G6H5; -.
DR GeneID; 105994583; -.
DR KEGG; dord:105994583; -.
DR CTD; 22907; -.
DR InParanoid; A0A1S3G6H5; -.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000081671; 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 ECO:0000313|RefSeq:XP_012883617.1};
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:UP000081671}.
FT DOMAIN 470..638
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 680..853
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1220 AA; 136714 MW; 8905B5E10403B4A3 CRC64;
MDLKDSAPGF QLPLLARHVQ LGLIQKRSGP AQTTSVQTPP TPPSTHVCQP RPWRDHLSRL
NVNISNMAAS RDLLKEFPQP KNLLNSVIGR ALGISHAKDK LVYVHTNGPK KKKVTLHIKW
PKSVEVEGYG SKKIDAERQA AAAACQLFKG WGLLGPRNEL FDAAKYRVLA DRFGSPADSW
WRPEPTMPPT SWRQLNPESI RPGGPGLPRT LGREEEEDEE EELEEGTIDV SEFLSLTQQD
SHNPLRDSRG GSFEMTDDDS AVRALTQFPL PKNLLAKVIQ IATSSSTAKN LMQFHTVGTK
TKLSTLTLLW PCPMTFVAKG RRKAEAENKA AALACKKLKS LGLVDRNNEP LTHAMYNLAS
LRELGETQRR PCTIQVPEPI LRKIETFLNH YPVDSSWISP ELRLQSDDIL PLGKDSGPLS
DPITGKPYVP LSEAEEVRLS QSLLELWRRR GPVWQEAPQL PVDPHRDTIL NAIEQHPVVV
ISGDTGCGKT TRIPQLLLER YVTEGRGARC NVIITQPRRI SAVSVAQRVS HELGPSLRRN
VGFQVRLESK PPARGGALLF CTVGILLRKL QSNPSLEGVS HVIVDEVHER DVNTDFLLIL
LKGLQRLNPA LRLVLMSATG DNERFSRYFG GCPVIKVPGF MYPVKEHYLE DILAKLGKHQ
YPHRHRHHES EDECALDLDL VTDLVLHIDA RGEPGGILCF LPGWQEIKGV QQRLQEALGM
HESKYLILPV HSNIPMMDQK AIFQQPPVGV RKIVLATNIA ETSITVNDIV HVVDSGLHKE
ERYDLKTKVS CLETVWVSRA NVIQRRGRAG RCQSGFAYHL FPRSRLEKMV PFQVPEILRT
PLENLVLQAK IHMPEKTAVE FLSKAVDSPN IKAVDEAVIL LQEIGVLDQR EYLTTLGQRL
AHISTDPRLA KAIVLAAIFR CLHPLLVVVS CLTRDPFSSS LQNRAEVDKV KALLSHDSGS
DHLAFVRAVA GWEEVLRWQD RTSRENYLEE NLLYAPSLRF IHGLIKQFSE NIYEAFLVGK
PSDCTLPSAQ CNEYSEEEEL VKGVLMAGLY PNLIQVRQGK VTRQGKFKPN SVTYRTKSGN
ILLHKSTINR EATRLRSRWL TYFMAVKSNG SVFVRDSSQV HPLAVLLLTD GDVHIRDDGR
RATISLSDSD LLRLEGDSRT VRLLRELRRA LGRMVERSLR SELAALPPMV QQEHGQLLAL
LAELLRGPCG SFDVRKTADD
//
