ID   DHX30_CHICK             Reviewed;        1231 AA.
AC   Q5ZI74;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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; ORFNames=RCJMB04_29l1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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   -!- 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; AJ720910; CAG32569.1; -; mRNA.
DR   RefSeq; NP_001012869.1; NM_001012851.1.
DR   AlphaFoldDB; Q5ZI74; -.
DR   SMR; Q5ZI74; -.
DR   STRING; 9031.ENSGALP00000008031; -.
DR   PaxDb; Q5ZI74; -.
DR   GeneID; 420376; -.
DR   KEGG; gga:420376; -.
DR   CTD; 22907; -.
DR   VEuPathDB; HostDB:geneid_420376; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   InParanoid; Q5ZI74; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; Q5ZI74; -.
DR   PRO; PR:Q5ZI74; -.
DR   Proteomes; UP000000539; 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: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:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
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; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014720; dsRBD_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; PF00035; dsrm; 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; PS00690; DEAH_ATP_HELICASE; 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; Reference proteome; Repeat;
KW   Ribosome biogenesis; RNA-binding.
FT   CHAIN           1..1231
FT                   /note="ATP-dependent RNA helicase DHX30"
FT                   /id="PRO_0000245542"
FT   DOMAIN          80..148
FT                   /note="DRBM 1"
FT   DOMAIN          292..359
FT                   /note="DRBM 2"
FT   DOMAIN          488..656
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          697..870
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          39..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           603..606
FT                   /note="DEAH box"
FT   BINDING         501..508
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1231 AA;  137703 MW;  BBCD730FC2D98A83 CRC64;
     MAALGLLLQA AAACGSAGPL RLGRCYRGAR GLCTRLAEPD GLEGARQEDE EEQPPPPGAE
     EQSTAMVKDS RDLLKEFPQP KNLLNSVIGR ALGISHARDK LVYIHTNGPR KKKVTLHIKW
     PKNVEVEGYG TKKIDAERQA AAAACQLFKG WGLLGPRNEL FDAAKYRLLA DQLGCPDERW
     CSEGKWRSKS GPSLADLSTC WRRMEPDDPI QPMEQGRMPK AMRREELEEG ELEEGELEEG
     ELEEEAIDVS DYLPMAHQDA RTPGRDASRG GSSIEMTDDN TAIRALTQFP LPKNLLAQVI
     QIATSSSTVK EYMQFRTVGT KTKICKLTLR WPCPMTFAAK GRRKVEAENK AAALACQKLK
     SLGLVDKNNN PLSHAMYNMT SLRELGENQR KPCHIKVPEA TLRKIENYLN HYPVDIRESR
     PRIADDMMNL SKESGAISDA ITGKTYIPML EAEEVRLSQN LLALWKRRGS SWQESHPLPV
     DPHKDTILSA IEQNPVVVIA GDTGCGKTTR IPQLLLEHYI LEGRGARCNV VITQPRRISA
     ISVAQRVAQE LGPNMRKNVG YQVRLESKPP ARGGALLFCT VGILLRKLQG NPSLEGVSHV
     VVDEVHERDV NTDFLLILLK GIQKLNPDLR LVLMSATGDN QRFSHYFGGC PVVKVPGFMY
     PVKEYYLEEI LAKLGRHRHR HYEIKQSDDE CVLDLDLITD LVLQIDAHGE PGGILCFLPG
     WQEIKGVQQR LLEMLGSQNS RYLVLPVHSN IPMMDQQNIF QRPPPGVRKI VLATNIAETS
     ITINDIVHVV DSGTHKEERY DLKTKVSCLE TVWVSKSNVV QRRGRAGRCQ SGFAYHLFPR
     SRLDKMPTYQ VPEILRTPLE NLVVQAKIHM PEKTAVEFLS KALDSPDIKA VDEAVILLQE
     IGVLDQREAL TTLGKRLAQI STDPRLAKAI VLASIYRCLH PLLVIVSCLT RDPFSSSLQN
     RAEVDKAKAV LSRESGSDHL AFVRAVAGWE EVLRRRDSRA RDNYLQDYYL YGPSLRFING
     LVKQFSENLY EAFLVSSPSD CTMPSSVCNQ YSEEEELVKG VLMAGLYPNL IQVRQGKVTR
     QGKFKPNSYA YRTKAGTVLL HKSTINREAS KLYSRWLTYF MAVKSNGGVF VRDSSQVHPL
     AVLLMTDTDI HVRDDGWRAT VSLTDSDLLV LEGDSYTIRL LRDFRVSLSK MVETCLCYEM
     AAIPGDLHHQ HSQLLDILVD LLKGPPGSFG A