ID   DBP2_PICST              Reviewed;         530 AA.
AC   A3LQW7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP-dependent RNA helicase DBP2;
DE            EC=3.6.4.13;
GN   Name=DBP2; ORFNames=PICST_82821;
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-dependent RNA helicase involved nonsense-mediated mRNA
CC       decay and ribosome biogenesis through rRNA processing. {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 polysomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000497; ABN65631.1; -; Genomic_DNA.
DR   RefSeq; XP_001383660.1; XM_001383623.1.
DR   AlphaFoldDB; A3LQW7; -.
DR   SMR; A3LQW7; -.
DR   STRING; 4924.XP_001383660.1; -.
DR   EnsemblFungi; ABN65631; ABN65631; PICST_82821.
DR   GeneID; 4838019; -.
DR   KEGG; pic:PICST_82821; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   HOGENOM; CLU_003041_16_9_1; -.
DR   InParanoid; A3LQW7; -.
DR   OMA; STMPKFE; -.
DR   OrthoDB; 638613at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; 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; Cytoplasm; Helicase; Hydrolase; Nonsense-mediated mRNA decay;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN           1..530
FT                   /note="ATP-dependent RNA helicase DBP2"
FT                   /id="PRO_0000285138"
FT   DOMAIN          128..303
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          318..478
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           97..125
FT                   /note="Q motif"
FT   MOTIF           251..254
FT                   /note="DEAD box"
FT   COMPBIAS        513..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         141..148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   530 AA;  58594 MW;  B9520538171558D8 CRC64;
     MNNYNNGDYK GGREQHFGGN NNYNRGYGGN GGFGGNRYNE RVELTTPDWD LESLPKFEKN
     FYTEHPDVAA RSDKDIAAFR NEHQMSCLGS DIPHPITTFD EAGFPEYVLN EVKAQGFPSP
     TAIQCQGWPM ALSGRDMVGI AATGSGKTLS YCLPAIVHIN AQPLLSPGDG PVVLVLAPTR
     ELAVQIQQEC SKFGSSSRIR NTCVYGGAPK GQQIRDLARG VEIVIATPGR LIDMLEMGKT
     NLKRVTYLVL DEADRMLDMG FEPQIRKIVD QIRPDRQTLM WSATWPKEVQ NLARDYLQDP
     IQVRIGSLEL AASHTITQVV EVISEYEKRD RLVKHLETAT TEKESKVLIF ASTKKTCDEV
     TSYLRADGWP ALAIHGDKQQ SERDWVLREF KTGKSPIMVA TDVAARGIDV KGINFVINFD
     MPGNIEDYVH RIGRTGRGGA TGTAVSFFTD GNNKLGGDLC KIMREAKQTI PPELQRFDRK
     SFGAHIRYGG GRGGRGGYGR GRGGYGGRGG YGQRNYQTGS NQAPLSNRRF