DDX28_MACFA
ID DDX28_MACFA Reviewed; 546 AA.
AC Q4R4T6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX28;
DE EC=3.6.4.13;
DE AltName: Full=Mitochondrial DEAD box protein 28;
GN Name=DDX28; ORFNames=QccE-21131;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an essential role in facilitating the proper assembly
CC of the mitochondrial large ribosomal subunit and its helicase activity
CC is essential for this function. May be involved in RNA processing or
CC transport. Has RNA and Mg(2+)-dependent ATPase activity (By
CC similarity). {ECO:0000250|UniProtKB:Q9NUL7}.
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 -!- SUBUNIT: Monomer. Found in a complex with GRSF1, DHX30, FASTKD2 and
CC FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA) and
CC with the mitochondrial ribosome large subunit (39S).
CC {ECO:0000250|UniProtKB:Q9NUL7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NUL7}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion matrix,
CC mitochondrion nucleoid {ECO:0000250|UniProtKB:Q9NUL7}. Mitosome matrix
CC {ECO:0000250|UniProtKB:Q9NUL7}. Note=Transported between these two
CC compartments. Nuclear localization depends on active RNA polymerase II
CC transcription. Localizes to mitochondrial RNA granules found in close
CC proximity to the mitochondrial nucleoids (By similarity).
CC {ECO:0000250|UniProtKB:Q9NUL7}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; AB169808; BAE01889.1; -; mRNA.
DR RefSeq; NP_001271761.1; NM_001284832.1.
DR AlphaFoldDB; Q4R4T6; -.
DR SMR; Q4R4T6; -.
DR STRING; 9541.XP_005592383.1; -.
DR GeneID; 101867446; -.
DR CTD; 55794; -.
DR eggNOG; KOG0330; Eukaryota.
DR OrthoDB; 1223767at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0032047; C:mitosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 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.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Mitochondrion nucleoid;
KW Mitosome; Nucleotide-binding; Nucleus; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA-binding.
FT CHAIN 1..546
FT /note="Probable ATP-dependent RNA helicase DDX28"
FT /id="PRO_0000055034"
FT DOMAIN 159..351
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 377..536
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 3..18
FT /note="Mitochondrial targeting signal"
FT /evidence="ECO:0000255"
FT MOTIF 126..156
FT /note="Q motif"
FT MOTIF 180..191
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT MOTIF 286..289
FT /note="DEAD"
FT /evidence="ECO:0000250"
FT MOTIF 520..523
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 546 AA; 60402 MW; 871C28A9DA5EED9E CRC64;
MALSRPVRLF SLVARLILAP RRGLTVRSPD EPLPVVRIPV ALQRQLEQRQ SRQRNLPRPV
LARPGRLLVS ARRPEFNQPA RLTLGRWESA PLASQGWKSR RARRDHFSIE RAQQEAPAVQ
KLSSEGNFAD LGLEPRVLHA LQEVAPEVVQ PTTVQSNTIP QLLRGRHVLC AAETGSGKTL
SYLLPLFQRL MVQPSLDSLR IPAPRGLVLV PSRELAQQVQ AVAQPLGRSL GLLVRDLEGG
HGMCRIRMQL ARQPSADVLV ATPGALWKAL KSRLISLEQL SFLVLDEADT LLDESFLELV
DCILEKSHIA DGPADLEDRF NPKAQLVLVG ATFPEGVGQL LDKVASPDAV TTITSSNLHC
IMPHVKQTFL RLKGADKVAE LVHILKHHNR AERTGPSGTV LVFCNSSSTV NWLGYILDDH
KIQHLRLQGQ MPALMRAGIF QSFQKSSRDI LLCTDIASRG LDSTGVELVV NYDFPPTLQD
YIHRAGRVGR VGSEVPGTVI SFVTHPWDVS LVQKIELAAR RRRSLPGLVS SVKEPLPQQP
DFDKSD
