DRS1_NEOFI
ID DRS1_NEOFI Reviewed; 819 AA.
AC A1D1R8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP-dependent RNA helicase drs1;
DE EC=3.6.4.13;
GN Name=drs1; ORFNames=NFIA_010420;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: ATP-binding RNA helicase involved in ribosome assembly.
CC {ECO:0000250}.
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: Associates with pre-ribosomal particles. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC subfamily. {ECO:0000305}.
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DR EMBL; DS027688; EAW22361.1; -; Genomic_DNA.
DR RefSeq; XP_001264258.1; XM_001264257.1.
DR AlphaFoldDB; A1D1R8; -.
DR SMR; A1D1R8; -.
DR STRING; 36630.CADNFIAP00001694; -.
DR EnsemblFungi; EAW22361; EAW22361; NFIA_010420.
DR GeneID; 4591505; -.
DR KEGG; nfi:NFIA_010420; -.
DR VEuPathDB; FungiDB:NFIA_010420; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_1_1; -.
DR OMA; AAHTDIR; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..819
FT /note="ATP-dependent RNA helicase drs1"
FT /id="PRO_0000282493"
FT DOMAIN 330..504
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 531..678
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 299..327
FT /note="Q motif"
FT MOTIF 452..455
FT /note="DEAD box"
FT COMPBIAS 37..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 343..350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 819 AA; 90304 MW; A538734C9BA16513 CRC64;
MAPNATTKKR AAAKDDDFVL TLSDDENDVL ENGVEEDTLS SSKKRKRDAA EAPKGKNKKQ
KQLKKSKKGE SAAGAVSDDQ SGEEDEAEAM DAGEDDGALD SEFEFDVGGN ANTGVIEGFD
GWEARNGAGP ADAPKNGDKK AVDIDDIISR RKAKKEAELK KKQQKEKKRR EEEGEEESED
EDADSDGGMS VDFQDDELLA ADGFGMGADG ADESGDDVEN DSNDSDDADE KGSEDEESDD
DAAASDNDSV ATPVHHPDDE AASDEESEAE SEVDAEEAEK RKAFFAPEEK STAASTSNRS
FQDFNLSRPI LRGLASVNFT TPTPIQQKTI PVALLGKDIV GSAVTGSGKT AAFVVPILER
LLFRPRKVPT SRVAILMPTR ELAVQCYNVA TKLATHTDIT FCQLVGGFSL REQENILKKR
PDVIIATPGR FIDHMRNSPS FTVDTLEILV LDEADRMLED GFADELNEIL TTIPQSRQTM
LFSATMTDSV DKLIRVGLNR PVRLMVDSKK NTSMNLTQEF VRLRPGREDK RLGYLLYLCN
EIYTGRVIVF FRQKREAHRV RIVFGLLGLK AAELHGSMSQ EQRIKSVENF REGKVAFLLA
TDLASRGLDI KGVETVINYE APQSHEIYLH RVGRTARAGR SGRACTIAAE PDRKIVKSAV
KAGKAQGAKI VSRVVDPAVA DEWAAKAKGL EDEIEEVLQE EKLEKQMAQA EMQVTKGENM
IKHEAEIMSR PKRTWFETER DKRAARKLGA TELNGPSKKD KVKLSNKDKK RLDDARQRHE
GNIGWKKGKA DREAPKQGKN KGSKNKSDKK NNIKMKGKK
