DHX30_BOVIN
ID DHX30_BOVIN Reviewed; 1220 AA.
AC Q2NKY8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=ATP-dependent RNA helicase DHX30 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q7L2E3};
DE AltName: Full=DEAH box protein 30;
GN Name=DHX30;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA dependent helicase. Plays an important role in the
CC assembly of the mitochondrial large ribosomal subunit. Required for
CC optimal function of the zinc-finger antiviral protein ZC3HAV1.
CC Associates with mitochondrial DNA. Involved in nervous system
CC development and differentiation through its involvement in the up-
CC regulation of a number of genes which are required for neurogenesis,
CC including GSC, NCAM1, neurogenin, and NEUROD.
CC {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000250|UniProtKB:Q7L2E3,
CC ECO:0000250|UniProtKB:Q99PU8}.
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:0000250|UniProtKB:Q7L2E3};
CC -!- SUBUNIT: Identified in a complex with TFAM and SSBP1. Interacts with
CC AGO1 and AGO2 (By similarity). Interacts (via N-terminus) with ZC3HAV1
CC (via N-terminal domain) in an RNA-independent manner. Found in a
CC complex with GRSF1, DDX28, FASTKD2 and FASTKD5.
CC {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000250|UniProtKB:Q7L2E3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L2E3}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q7L2E3}. Mitochondrion matrix,
CC mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L2E3}. Note=Localizes
CC to mitochondrial RNA granules found in close proximity to the
CC mitochondrial nucleoids. Relocalizes to stress granules upon heat
CC stress. {ECO:0000250|UniProtKB:Q7L2E3}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; BC111349; AAI11350.1; -; mRNA.
DR RefSeq; NP_001070003.1; NM_001076535.2.
DR AlphaFoldDB; Q2NKY8; -.
DR SMR; Q2NKY8; -.
DR STRING; 9913.ENSBTAP00000030598; -.
DR PaxDb; Q2NKY8; -.
DR PRIDE; Q2NKY8; -.
DR GeneID; 767607; -.
DR KEGG; bta:767607; -.
DR CTD; 22907; -.
DR eggNOG; KOG0920; Eukaryota.
DR InParanoid; Q2NKY8; -.
DR OrthoDB; 278674at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 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; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Mitochondrion;
KW Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..1220
FT /note="ATP-dependent RNA helicase DHX30"
FT /id="PRO_0000245537"
FT DOMAIN 79..147
FT /note="DRBM"
FT DOMAIN 470..638
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 680..853
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 12..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 585..588
FT /note="DEAH box"
FT BINDING 483..490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PU8"
SQ SEQUENCE 1220 AA; 135946 MW; DF762DBFF8C3128C CRC64;
MATARRLMAL AAGVSPRLRP LGPRAIGRQG GPRGLSTGCS RPDRTQEAAE AEAAPGEPGE
GDGSVVNASR DLLKEFPQPK NLLNSVIGRA LGISHAKDKL VYVHTNGPKK KKVTLHIKWP
KSVEVEGYGS KKIDAERQAA AAACQLFKGW GLLGPRNELF DAAKYRVLAD RFGSPADSWW
RPEPTMPPTS WRQLNPESIR PGGPGGLSRS LGREEEEDEE EELEEGTIDV TEFLSMTQQD
SHAPLRDSRG GSFEMTDDDS AIRALTQFPL PKNLLAKVIQ IATSSSTAKN LMQFHTVGTK
TKLSTLTLLW PCPMTFVAKG RRKAEAENKA AALACNKLKS LGLVDRNNEP LTHAMYNLAS
LRELGETQRR PCTIQVPEPI LRKIETFLNH YPVESSWISS ELRLQGEDIL PLGKDSGPLS
DPITGKPYVP LSEAEELRLS QSLLELWRRR GPVWQEAPQL PVDPHRDTIL NAIEQHPVVV
IAGDTGCGKT TRIPQLLLER YVTEGRGARC NVIITQPRRI SAVSVAQRVS HELGPTLRRN
VGFQVRLESK PPARGGALLF CTVGILLRKL QSNPSLEGVS HVVVDEEHER DVNTDFLLIL
LKGLQRLNPA LRLVLMSATG DNERFSRYFG GCPVIKVPGF MYPVKEHYLE DILAKLGKHQ
YPHRHRHHES EDECALDLDL VTDLVLHIDA RGEPGGILCF LPGWQEIKGV QQRLQEALGM
HESKYLILPV HSNIPMMDQK AIFQQPPIGV RKIVLATNIA ETSITINDIV HVVDSGLHKE
ERYDLKTKVS CLETVWVSRA NVIQRRGRAG RCQSGFAYHL FPRSRLEKMA PFQVPEILRT
PLENLVLQAK IHMPEKTAVE FLSKAVDSPN IKAVDEAVIL LQEIGVLDQR EYLTTLGQRL
AHISTDPRLA KAIVLAAIFR CLHPLLVVVS CLTRDPFSSS LQNRAEVDKV KALLSHDSGS
DHLAFVRAVS GWEEVLRWQD RSSRENYLEE NLLYAPSLRF IHGLIKQFSE NIYEAFLVGK
PSDCTLASAQ CNEYSEEEEL VKGVLMAGLY PNLIQVRQGK VTRQGKFKPN SVTYRTKSGN
ILLHKSTINR EATRLRSRWL TYFMAVKSNG SVFVRDSSQV HPLAVLLLTD GDVHIRDDGR
RATISLSDSD LLRLEGDSRT VRLLRELRRA LGRMVERSLR SELAALPPCV QEEHGQLLAL
LAELLRGPCG SFDVRKTADD
