ID DHX30_RAT Reviewed; 1194 AA.
AC Q5BJS0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-APR-2013, entry version 63.
DE RecName: Full=Putative ATP-dependent RNA helicase DHX30;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 30;
GN Name=Dhx30;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP ZC3HAV1.
RX PubMed=21204022; DOI=10.1007/s13238-010-0117-8;
RA Ye P., Liu S., Zhu Y., Chen G., Gao G.;
RT "DEXH-Box protein DHX30 is required for optimal function of the zinc-
RT finger antiviral protein.";
RL Protein Cell 1:956-964(2010).
CC -!- FUNCTION: Associates with mitochondrial DNA (By similarity).
CC Required for optimal function of the zinc-finger antiviral protein
CC ZC3HAV1.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Identified in a complex with TFAM and SSBP1 (By
CC similarity). Interacts (via N-terminus) with ZC3HAV1 (via N-
CC terminal domain) in an RNA-independent manner.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC (By similarity). Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC subfamily.
CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR EMBL; BC091359; AAH91359.1; -; mRNA.
DR IPI; IPI00949701; -.
DR RefSeq; NP_001013267.1; NM_001013249.1.
DR UniGene; Rn.163034; -.
DR ProteinModelPortal; Q5BJS0; -.
DR SMR; Q5BJS0; 44-152.
DR STRING; 10116.ENSRNOP00000040917; -.
DR PhosphoSite; Q5BJS0; -.
DR PaxDb; Q5BJS0; -.
DR PRIDE; Q5BJS0; -.
DR Ensembl; ENSRNOT00000048764; ENSRNOP00000043896; ENSRNOG00000029194.
DR GeneID; 367172; -.
DR KEGG; rno:367172; -.
DR UCSC; RGD:1308888; rat.
DR CTD; 22907; -.
DR RGD; 1308888; Dhx30.
DR eggNOG; COG1643; -.
DR GeneTree; ENSGT00700000104393; -.
DR HOGENOM; HOG000112212; -.
DR HOVERGEN; HBG081437; -.
DR KO; K13185; -.
DR OrthoDB; EOG4VHK5M; -.
DR NextBio; 690809; -.
DR ArrayExpress; Q5BJS0; -.
DR Genevestigator; Q5BJS0; -.
DR GermOnline; ENSRNOG00000029194; Rattus norvegicus.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR011709; DUF1605.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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 PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS50137; DS_RBD; FALSE_NEG.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1 1194 Putative ATP-dependent RNA helicase
FT DHX30.
FT /FTId=PRO_0000245541.
FT DOMAIN 53 121 DRBM.
FT DOMAIN 444 612 Helicase ATP-binding.
FT DOMAIN 654 827 Helicase C-terminal.
FT NP_BIND 457 464 ATP (By similarity).
FT MOTIF 559 562 DEAH box.
FT COMPBIAS 188 199 Poly-Glu.
FT COMPBIAS 1010 1013 Poly-Glu.
SQ SEQUENCE 1194 AA; 133997 MW; A453E243EB1A5929 CRC64;
MFTLDSFRKD RTQHRQRQCK LPPPRLPPMC VNPAPGGTIS RASRDLLKEF PQPKNLLNSV
IGRALGISHA KDKLVYVHTN GPKKKKVTLH IKWPKSVEVE GYGSKKIDAE RQAAAAACQL
FKGWGLLGPR NELFDAAKYR VLADRFGSPA DSWWRPEPTM PPTSWRQLNP ENIRPAGTGG
LSRSLGREEE EDEEEELEEG TIDVTEFLSM TQQDSHNPLR DSRGGSFEMT DDDSAIRALT
QFPLPKNLLA KVIQIATSSS TAKNLMQFHT VGTKTKLATL TLLWPCPMTF VAKGRRKAEA
ENKAAALACK KLKSLGLVDR NNEPLTHAMY NLASLRELGE TQRRPCTIQV PEPILRKIEA
FLSHYPVDSS WISPELRLQS DDILPLGKDS GPLSDPITGK PYMPLSEAEE VRLSQSLLEL
WRRRGPIWQE APQLPVDPHR DTILSAIEQH PVVVISGDTG CGKTTRIPQL LLERYVTEGR
GARCNVIITQ PRRISAVSVA QRVSHELGPS LRRNVGFQVR LESKPPARGG ALLFCTVGIL
LRKLQSNPSL EGVSHVIVDE VHERDVNTDF LLILLKGLQR LNPALRLVLM SATGDNERFS
RYFGGCPVIK VPGFMYPVKE HYLEDILAKL GKHQYPHRHR HHESEDECAL DLDLVTDLVL
HIDARGEPGG ILCFLPGWQE IKGVQQRLQE ALGMHESKYL ILPVHSNIPM MDQKAIFQQP
PLGVRKIVLA TNIAETSITV NDIVHVVDSG LHKEERYDLK TKVSCLETVW VSRANVIQRR
GRAGRCQSGF AYHLFPRSRL EKMVPFQVPE ILRTPLENLV LQAKIHMPEK TAVEFLSKAV
DSPNIKAVDE AVILLQEIGV LDQREYLTTL GQRLAHISTD PRLAKAIVLA AIFRCLHPLL
VVVSCLTRDP FSSSLQNRAE VDKVKALLSH DSGSDHLAFV RAVAGWEEVL RWQDRTSREN
YLEENLLYAP SLRFIHGLIK QFSENIYEAF LVGKPSDCTL PSAQCNEYSE EEELVKGVLM
AGLYPNLIQV RQGKVTRQGK FKPNSVTYRT KSGNILLHKS TINREATRLR SRWLTYFMAV
KSNGSVFVRD SSQVHPLAVL LLTDGDVHIR DDGRRATISL SDSDLLRLEG DSRTVRLLRE
LRRALGRMVE RSLRSELAAL PLSVQQEHGQ LLALLAELLR GPCGSFDVRK TADD
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