DHX30_PONAB
ID DHX30_PONAB Reviewed; 1194 AA.
AC Q5R607; Q5RCD4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 (via N-
CC terminus) with ZC3HAV1 (via N-terminal domain) in an RNA-independent
CC manner. Found in a 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R607-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R607-2; Sequence=VSP_019748;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; CR858337; CAH90573.1; -; mRNA.
DR EMBL; CR860693; CAH92809.1; -; mRNA.
DR RefSeq; NP_001125306.1; NM_001131834.1.
DR AlphaFoldDB; Q5R607; -.
DR SMR; Q5R607; -.
DR STRING; 9601.ENSPPYP00000015564; -.
DR GeneID; 100172205; -.
DR KEGG; pon:100172205; -.
DR CTD; 22907; -.
DR eggNOG; KOG0920; Eukaryota.
DR InParanoid; Q5R607; -.
DR OrthoDB; 278674at2759; -.
DR Proteomes; UP000001595; 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; 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 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; 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 Alternative splicing; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..1194
FT /note="ATP-dependent RNA helicase DHX30"
FT /id="PRO_0000245540"
FT DOMAIN 53..121
FT /note="DRBM"
FT DOMAIN 444..612
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 654..827
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 559..562
FT /note="DEAH box"
FT BINDING 457..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L2E3"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PU8"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L2E3"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019748"
FT CONFLICT 170
FT /note="P -> L (in Ref. 1; CAH90573)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="A -> T (in Ref. 1; CAH90573)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="V -> A (in Ref. 1; CAH90573)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="L -> S (in Ref. 1; CAH90573)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="T -> I (in Ref. 1; CAH90573)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="E -> D (in Ref. 1; CAH90573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1194 AA; 133924 MW; 2DB50E848BAE48C1 CRC64;
MFSLDSFRKD RAQHRQRQCK LPPPRLPPMC VNPAPGGTIS RASRDLLKEF PQPKNLLNSV
IGRALGISHA KDKLVYVHTN GPKKKKVTLH IKWPKSVEVE GYGSKKIDAE RQAAAAACQL
FKGWGLLGPR NELFDAAKYR VLADRFGSPA DSWWRPEPTM PPTSWRQLNP ESIRPGGPGG
LSRSLGREEE EDEEEELEEG TIDVTDFLSM TQQDSHTPLR DSRGSSFEMT DDDSAIRALT
QFPLPKNLLA KVIQIATSSS TAKNLMQFHT VGTKTKLSTL TLLWPCPMTF VAKGRRKAEA
ENKAAALACK KLKSLGLVDR NNEPLTHAMY NLASLRELGE TQRRPCTIQV PEPILRKIET
FLNHYPVESS WIAPELRLQS DDILPLGKDS GPLSDPITGK PYVPLLEAEE VRLSQSLLEL
WRRRGPVWQE APQLPVDPHR DTILNAIEQH PVVVISGDTG CGKTTRIPQL LLERYVTEGR
GARCNVIITQ PRRISAVSVA QRVSHELGPS LRRNVGFQVR LESKPPARGG ALLFCTVGIL
LRKLQSNPSL EGVSHVIVDE VHERDVNTDF LLILLKGLQR LNPALRLVLM SATGDNERFS
RYFGGCPVIK VPGFMYPVKE HYLEDILAKL GKHQYLHRHR HHESEDECAL DLDLVTDLVL
HIDARGEPGG ILCFLPGWQE IKGVQQRLQE ALGMHESKYL ILPVHSNIPM MDQKAIFQQP
PVGVRKIVLA TNIAETSTTI NDIVHVVDSG LHKEERYDLK TKVSCLETVW VSRANVIQRR
GRAGRCQSGF AYHLFPRSRL EKMVPFQVPE ILRTPLENLV LQAKIHMPEK TAVEFLSKAV
DSPNIKAVDE AVILLQEIGV LDQREYLTTL GQRLAHISTE PRLAKAIVLA AIFRCLHPLL
VVVSCLTRDP FSSSLQNRAE VDKVKALLSH DSGSDHLAFV RAVAGWEEVL RWQDRSSREN
YLEENLLYAP SLRFIHGLIK QFSENIYEAF LVGKPSDCTL ASAQCNEYSE EEELVKGVLM
AGLYPNLIQV RQGKVTRQGK FKPNSVTYRT KSGNILLHKS TINREATRLR SRWLTYFMAV
KSNGSVFVRD SSQVHPLAVL LLTDGDVHIR DDGRRATISL SDSDLLRLEG DSRTVRLLKE
LRRALGRMVE RSLRSELAAL PPSVQEEHGQ LLALLAELLR GPCGSFDVRK TADD
