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Database: UniProt
Entry: A3LSN3
LinkDB: A3LSN3
Original site: A3LSN3 
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   31-JUL-2019, entry version 63.
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 /
OS   NRRL Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   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-
RT   fermenting 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
CC       box family of RNA helicases and controls ATP binding and
CC       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};
DR   EMBL; CP000497; ABN65601.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001383630.2; XM_001383593.1.
DR   SMR; A3LSN3; -.
DR   STRING; 4924.XP_001383630.2; -.
DR   PRIDE; A3LSN3; -.
DR   EnsemblFungi; ABN65601; ABN65601; PICST_1703.
DR   GeneID; 4838308; -.
DR   KEGG; pic:PICST_1703; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000265456; -.
DR   InParanoid; A3LSN3; -.
DR   KO; K13181; -.
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: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   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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding.
FT   CHAIN         1    741       ATP-dependent RNA helicase DRS1.
FT                                /FTId=PRO_0000285146.
FT   DOMAIN      253    429       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      458    603       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     266    273       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED      610    657       {ECO:0000255}.
FT   MOTIF       222    250       Q motif.
FT   MOTIF       376    379       DEAD box.
FT   COMPBIAS    119    212       Glu-rich.
FT   COMPBIAS    671    741       Lys-rich.
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
//
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