SUB2_ASPNC
ID SUB2_ASPNC Reviewed; 440 AA.
AC A2R0B5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ATP-dependent RNA helicase sub2;
DE EC=3.6.4.13;
GN Name=sub2; ORFNames=An12g08030;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: ATP-binding RNA helicase involved in transcription elongation
CC and required for the export of mRNA out of the nucleus. SUB2 also plays
CC a role in pre-mRNA splicing and spliceosome assembly. May be involved
CC in rDNA and telomeric silencing, and maintenance of genome integrity
CC (By similarity). {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 -!- SUBCELLULAR LOCATION: 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. DECD subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270283; CAK41253.1; -; Genomic_DNA.
DR RefSeq; XP_001395854.1; XM_001395817.2.
DR AlphaFoldDB; A2R0B5; -.
DR SMR; A2R0B5; -.
DR PaxDb; A2R0B5; -.
DR PRIDE; A2R0B5; -.
DR EnsemblFungi; CAK41253; CAK41253; An12g08030.
DR GeneID; 4986154; -.
DR KEGG; ang:ANI_1_978104; -.
DR VEuPathDB; FungiDB:An12g08030; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0000346; C:transcription export complex; IEA:EnsemblFungi.
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:0031124; P:mRNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
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; 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; 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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW mRNA transport; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding; Spliceosome; Transport.
FT CHAIN 1..440
FT /note="ATP-dependent RNA helicase sub2"
FT /id="PRO_0000282687"
FT DOMAIN 88..263
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 291..436
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..85
FT /note="Q motif"
FT MOTIF 210..213
FT /note="DEAD box"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 440 AA; 49532 MW; 95218DCE98D59CEC CRC64;
MSHEEDLIDY SDEELQTTDA AATTAAPASN GEAKKGDLTV SGGRPDKKGS YVGIHSTGFR
DFLLKEELLR AITDCGFEHP SEVQQVCIPT AILNVDVLCQ AKSGLGKTAV FVLTTLHQLE
PVPGECSILV MCHTRELAYQ IKNEYARFSK YLPDVKTAVF YGGTPIQKDV ELLSNKESYP
NIVVGTPGRL NALVRDKKLS LRNVKAFVLD ECDKMLDQID MRRDVQEIFR ATPADKQVMM
FSATLSQEIR PVCKKFMRNP LEVYVDDDTK LTLHGLQQYY IKLSEAEKNR KLNELLDSLE
FNQVIIFVKS TLRANELDKL LRECNFPSIA VHSGVSQEER IKRYKEFKEF NKRICVATDV
FGRGIDIERI NLAINYDLPA DADSYLHRVG RAGRFGTKGL SISFVSTEDD EKVLKDIEKR
FEVALPEYPE GGVDSSTYMA
