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Database: UniProt
Entry: A0A1E3NNN7_9ASCO
LinkDB: A0A1E3NNN7_9ASCO
Original site: A0A1E3NNN7_9ASCO 
ID   A0A1E3NNN7_9ASCO        Unreviewed;       793 AA.
AC   A0A1E3NNN7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=PICMEDRAFT_71749 {ECO:0000313|EMBL:ODQ47710.1};
OS   Pichia membranifaciens NRRL Y-2026.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ47710.1, ECO:0000313|Proteomes:UP000094455};
RN   [1] {ECO:0000313|EMBL:ODQ47710.1, ECO:0000313|Proteomes:UP000094455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ47710.1,
RC   ECO:0000313|Proteomes:UP000094455};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- FUNCTION: ATP-dependent RNA helicase required for ribosome biogenesis.
CC       Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC       Required for pre-rRNA cleavage at site A2.
CC       {ECO:0000256|ARBA:ARBA00037374}.
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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         Evidence={ECO:0000256|ARBA:ARBA00001556,
CC         ECO:0000256|RuleBase:RU365068};
CC   -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC       ribosomal complexes. {ECO:0000256|ARBA:ARBA00038587}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
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       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC       subfamily. {ECO:0000256|ARBA:ARBA00038084}.
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DR   EMBL; KV454002; ODQ47710.1; -; Genomic_DNA.
DR   RefSeq; XP_019018823.1; XM_019163997.1.
DR   AlphaFoldDB; A0A1E3NNN7; -.
DR   STRING; 763406.A0A1E3NNN7; -.
DR   GeneID; 30180684; -.
DR   OrthoDB; 149428at2759; -.
DR   Proteomes; UP000094455; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd17941; DEADc_DDX10; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
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   PANTHER; PTHR24031:SF54; ATP-DEPENDENT RNA HELICASE DDX10-RELATED; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094455};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          43..71
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          74..248
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          267..439
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          500..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          10..37
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           43..71
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        645..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..743
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   793 AA;  89540 MW;  85D5A97FA63C6B06 CRC64;
     MVKKSKTISR DDKKVKREQA EKQLKEIKQR VQDLTSEEYK TFERFKELPL TADILRGLDR
     SGFHSLTEIQ KLAIPECLKG NDVLAAAKTG SGKTLAFLVP VVQKLVFENW SDMDGLGALI
     ITPTRELAVQ IYEVLLKIGK YTQLSAGLVI GGKDYSFEKE RVGRVNILIG TPGRLLQHMD
     ESATLQTDNV QMLVLDEADR ILDMGFKKTL DAILGQLPAG RQTLLFSATQ TKSVGDLARL
     SMVNPKYVNG NLANGGIGGE ELSLPESLEQ SYVVVPLNEK LSLLWSFLKS HLQAKILVFV
     SSSKQVHFIY ETFRKLQPGI PLMKLHGRQK QKARLETSMK FTQSKNCCLI ATDVVARGLD
     FPAIDWVIQL DCPEDVSTYV HRVGRCARFG RQGKSMLVLL PNEEEGFISQ MSAKKIEIKK
     LNIKGSKKKN IQSQIQSLCF NSAELKYLAQ KAFISYCKSV IIQKNKSVFK IDELPLDLFA
     SSYGLPGMPK LRLPKKVDDE SRMKLKEKKN ENRKLKSLSN ANDEGEIEDQ TKKVRTKYDK
     MFERKNQDVL SEHYMQLNPG LGGKMSNTSD DDDDDEEFMK VKRHDDEVKT ADLPELELNS
     SKRAMKKALS RKLTAMKGDK GAKLVFDEDG KAHPVYELDD EETFLKEGPS KVHSEFLSTE
     REKMTKADEI DKGVVRDKRA EKKRRRKELE KQLEGDSDDS EGPYVATLGA LASGDENADN
     YESDEYGEGV PDLENDLEDS EGEDDVQPEK KKQKKWFDSD KYKDRDSKDA GVFEIEQPET
     TEDLEALAAK LMN
//
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