ID A0A179G747_METCM Unreviewed; 627 AA.
AC A0A179G747;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=VFPPC_01001 {ECO:0000313|EMBL:OAQ73233.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ73233.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ73233.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ73233.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates
CC from pre-60S ribosomal particles after processing of 27SB pre-rRNA.
CC Required for the normal formation of 18S rRNA through the processing of
CC pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and
CC 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
CC {ECO:0000256|ARBA:ARBA00037566}.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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:0000256|RuleBase:RU365068};
CC -!- SUBUNIT: Component of pre-60S ribosomal complexes.
CC {ECO:0000256|ARBA:ARBA00038757}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC subfamily. {ECO:0000256|ARBA:ARBA00038002}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAQ73233.1}.
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DR EMBL; LSBJ02000001; OAQ73233.1; -; Genomic_DNA.
DR RefSeq; XP_018149316.1; XM_018280910.1.
DR AlphaFoldDB; A0A179G747; -.
DR STRING; 1380566.A0A179G747; -.
DR GeneID; 28844904; -.
DR KEGG; pchm:VFPPC_01001; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000078397; Chromosome 1.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd17960; DEADc_DDX55; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF2; ATP-DEPENDENT RNA HELICASE DDX55; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT DOMAIN 15..43
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 46..247
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 283..438
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 532..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..43
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 532..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 70285 MW; D67BCE4E38E07DAF CRC64;
MAPGKVAPRR DPRAWDALTP PLAEWILDAV STMGFSRMTP VQAATMPHFM GNKDVVVEAV
TGSGKTLSFL IPIVQKILRL QEPTKKHHVA AIIVSPTREL AAQIHSVLVS LLEFHAPSAE
ILPHLKDDEK RPATTVPVVV PQLLVGGTTT TAQDLSYFLR HSPNVLISSP GRLVELLSSP
HVHCPQSSFE VLVLDEADRL LDLGFKQDLQ GIISHLPKQR RTGLFSASVS EAVSEIIRVG
LRNPVKIEVR VKMKDGGVLE DRKTPASLQM TYLVKPATQK LPALGQLLER LPITPQRTIV
FLSTCAAVDY FQHVLPGILP AGFSLIPLHG KHPAKVREKN FNRFLSAVSP TVLLTTDLAA
RGLDIPQVDL VVQIDAPSDP KVFIHRSGRA GRAGRKGLAV VMLHPGREED YVRFLDIRKT
PITPLEKPGI SISEDAATRA TNHIRKLAKT DRAIYDKAQK AFVSWVRSYG AHQATSIFRV
TDLDWVDLAK AWGLLRMPRM PELKTWKGDK KLGIEMDWDT FAYKEKARET ARKEAMEAAK
NGDVPEKKDD KKRKRKNEAW SAKHEKEEQR VERREKRHKK KEAERNANLT DDQRLEKMKL
DDLIEQVREQ NRTKAASKDD EFEGFDD
//
