DRS1_PICST
ID DRS1_PICST Reviewed; 741 AA.
AC A3LSN3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
GN Name=DRS1; ORFNames=PICST_1703;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN65601.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CP000497; ABN65601.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001383630.2; XM_001383593.1.
DR AlphaFoldDB; A3LSN3; -.
DR SMR; A3LSN3; -.
DR STRING; 4924.XP_001383630.2; -.
DR EnsemblFungi; ABN65601; ABN65601; PICST_1703.
DR GeneID; 4838308; -.
DR KEGG; pic:PICST_1703; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_2_1; -.
DR InParanoid; A3LSN3; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000002258; Chromosome 3.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
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; 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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..741
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000285146"
FT DOMAIN 253..429
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 458..603
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 35..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 610..657
FT /evidence="ECO:0000255"
FT MOTIF 222..250
FT /note="Q motif"
FT MOTIF 376..379
FT /note="DEAD box"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 741 AA; 83217 MW; 348AAAF28656F162 CRC64;
MAAKDDLILT IDSDGDEIVY SEESEAEVEI SVKKVKNKKN KKSKAQPQQK EEDEEKNEDI
NPNFIFSLDG IETTSKFDGW DFSVDRNANE VANKEVDLDG ILRRKGGLVS LAGSDAQKEE
EVEDEEEEEN DEDIQNEDED EGEEELALDG FGMGAEEKVI DEEDEEDEED ENDKSDGEDD
KDTEVEVSEE GEEENDEDTA EAMAEFYADE KETKSAKSQV HTTFQTLQLS RPVLKGLSQL
GYTKPSPIQS ASIPIALLGR DIVAGAVTGS GKTAAYMIPI IERLLYKPSK VASTRVIVLT
PTRELAIQVG DVGKKIGQFV NNLNFGLAVG GLNLRQQEQQ LKSRPDVVIA TPGRLIDHIR
NSPSFSIDSL EVLVIDEADR MLDEGFQVEL TEILSLIPKN KRQTLLFSAT MNTKIQDLIQ
LSLQRPVRIM IDPPKTAATK LTQEFVRIRK RDHLKPALLF QLLKKLDPAQ QSRIVVFVSR
KESAHKLRIV LGLLGMKVSE LHGSLTQEQR LNNVNDFKKL IVPVLICTDL AARGLDIPKI
EIVINYDMPK SHEVYLHRVG RTARAGRDGT SISFVGESTS DRNIVKDAIK SLEGGEVKGK
AVSRNIDWVD VEQLNKIVES KQEIIEEVLD EEKQAKEILQ AEMQLAKASN MMKHEKEIQS
RPKRTWFESE KDKKKHQTEV MQQLTKHGKK VNSKKRKAIE VKKDDGGRSY KKTKVDRITD
QKRNPKAKIG NGSSKGGKRR K
