ID W7I8M9_9PEZI Unreviewed; 795 AA.
AC W7I8M9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=DRE_00789 {ECO:0000313|EMBL:EWC45390.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC45390.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC45390.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC45390.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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|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; KI966427; EWC45390.1; -; Genomic_DNA.
DR AlphaFoldDB; W7I8M9; -.
DR HOGENOM; CLU_003041_26_1_1; -.
DR Proteomes; UP000024837; 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:UniProtKB-EC.
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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837};
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 80..254
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 280..439
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 89938 MW; EF97B0E90150D2D3 CRC64;
MAKGTRPASS LPQLKPRRKE SRSLKRKREE EELQTLEKTA QEFDASNISQ FSELPISRAT
TTGLDKSHFK ILTDIQRKAI PLALKGRDIL GAAKTGSGKT LAFLVPVLEI LYRRKWTQED
GLGALIISPT RELAIQIFEV LRKVGQRHSF SAGLVIGGKN LQDERERLGR MNILVCTPGR
MKQHLEQNPD LDTYSLQVLV LDEADRILDM GFKDAIDAIV QGIPKNRQTL LFSATQTKNV
NDLARLSLKD PEYVSVHESA SSATPGKLQQ HYIITPLPEK LDILWSFIRA NVKSKILVFL
SSTKQVRFVY ETFRQMQPGI PLLHLHGKQK QTARLDITAN FSGSKNSCLF ATDVVARGLD
FPAVDWVIQV DCPEDVDTYI HRVGRTARYE RDGRAVLFLC PTEEKGMLEK LKVKKVPIEK
INVRQNKKQS IQKQLQGICF KEPEIKYLGQ KAFTSYARSV YIQKDKDIFD LEKLPLQDFA
TSLGLPGAPR VKFMKGEDAK QRKNAPRALL KDDDSSDGRG SDGEEEDQAT KKEEKKKKEV
RTKYDRMFER QNQNIFTPHF TEMVRHGDGS GDEGKDEDFL AVKGHGYGSD AEDVDGEKTS
ARYIQVHGKE PLLVDSKRRE KLATTKKAML KYKGKGTKLI FDDEGEAHAI YELEDEEAFV
KAGDAEAQRG KFLAEETKRV SAADEEDKTV AKEKRRAKKE RQKARALEDI EDDGSDFDGG
VPLVPYQDYG EDSAPELVEE GRPAKKQKKW FEDDSEEERK KEKESKRKRK TKVVQMDEAP
ETLEDLEALA AGLLA
//
