DRS1_ASPCL
ID DRS1_ASPCL Reviewed; 826 AA.
AC A1CNV8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ATP-dependent RNA helicase drs1;
DE EC=3.6.4.13;
GN Name=drs1; ORFNames=ACLA_020360;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW07329.1; -; Genomic_DNA.
DR RefSeq; XP_001268755.1; XM_001268754.1.
DR AlphaFoldDB; A1CNV8; -.
DR SMR; A1CNV8; -.
DR STRING; 5057.CADACLAP00002940; -.
DR EnsemblFungi; EAW07329; EAW07329; ACLA_020360.
DR GeneID; 4701381; -.
DR KEGG; act:ACLA_020360; -.
DR VEuPathDB; FungiDB:ACLA_020360; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_1_1; -.
DR OMA; AAHTDIR; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000006701; 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..826
FT /note="ATP-dependent RNA helicase drs1"
FT /id="PRO_0000282489"
FT DOMAIN 337..511
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 538..690
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 306..334
FT /note="Q motif"
FT MOTIF 459..462
FT /note="DEAD box"
FT COMPBIAS 16..39
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..199
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..253
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 826 AA; 90985 MW; 4485FED045CBFC7E CRC64;
MAPSKKRTSV PDDDFVFTLS DDENDVLENG ADEGDEQADE ETASGSKKRK RETAEAPKGK
NKKQKQLKQS KKGKGAAVAG SDGEEEEEGD EEEAADAGED DGALDSEFEF DVGGHATAGV
IEGFDGWETQ NGDASANKNG DKKAVDIDDI ISRRKEQKDA ELKRKLKKEE KRKRMEESED
EAEAEDVESD GDMSVDFQDD ELLAADGFGM GADGEDESGE SDAGDGAGSD EENDSDDNGD
DEGDADDDDA ASDNDSVATP VGHPDDEVAS DDESGAESEV DAEEAEKRKA FFAPEEKTTE
EPTSKRSFQD FNLSRPILRG LASVNFTTPT PIQQKTIPVA LLGKDIVGSA VTGSGKTAAF
VVPILERLLF RPRKVPTSRV AILMPTRELA VQCYNVATKL ATHTDVTFCQ LVGGFSLREQ
ENILKKRPDV IIATPGRFID HMRNSPSFTV DTLEILVLDE ADRMLEDGFA DELNEILTTI
PKSRQTMLFS ATMTDSVDKL IRVGLNRPVR LMVDSKKNTS MNLTQEFVRL RPGREGKRLG
YLLYLCSEIF TGRVIVFFRQ KKEAHRVRIV FGLLGLKAAE LHGSMSQEQR IKSVESFREG
KVAFLLATDL ASRGLDIKGV ETVINYEAPQ SHEIYLHRVG RTARAGRSGR ACTIAADPDR
KVVKAAVRAG KAQGAKIASR VVEPAVADQW AAKVEALEEE IEEVLKEEKL EKHMAQAEMQ
VTKGENLMKH GAEIMSRPKR TWFETERDKR ASRKLGATEL NGPSKKDKVK LSNKDKKRLD
DSRQRHEGNQ GWKKGKTERE APKQAKTKGG KNQSDKKNKN KMKGKK
