SUB2_ASPOR
ID SUB2_ASPOR Reviewed; 441 AA.
AC Q2U6P7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=ATP-dependent RNA helicase sub2;
DE EC=3.6.4.13;
GN Name=sub2; ORFNames=AO090120000149;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
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DR EMBL; AP007166; BAE62768.1; -; Genomic_DNA.
DR RefSeq; XP_001823901.1; XM_001823849.2.
DR AlphaFoldDB; Q2U6P7; -.
DR SMR; Q2U6P7; -.
DR STRING; 510516.Q2U6P7; -.
DR EnsemblFungi; BAE62768; BAE62768; AO090120000149.
DR GeneID; 5996160; -.
DR KEGG; aor:AO090120000149; -.
DR VEuPathDB; FungiDB:AO090120000149; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR OMA; IKPICRK; -.
DR Proteomes; UP000006564; Chromosome 5.
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..441
FT /note="ATP-dependent RNA helicase sub2"
FT /id="PRO_0000232261"
FT DOMAIN 89..264
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 292..437
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..86
FT /note="Q motif"
FT MOTIF 211..214
FT /note="DECD box"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 441 AA; 49499 MW; 875AEF81CE994178 CRC64;
MSHEEDLIDY SDEELQTTDA AATTAAPAAN GDAAKKGDLT VSGGRPDKKG SYVGIHSTGF
RDFLLKGELL RAITDCGFEH PSEVQQVCIP TAILNVDVLC QAKSGLGKTA VFVLTTLHQL
EPVPGECSVL VMCHTRELAY QIKNEYARFS KYLPDVKTAV FYGGTPIQKD VEVLSNKESY
PNIVVGTPGR LNALVRDKKL SLRNVKAFVL DECDKMLDQI DMRRDVQEIF RATPADKQVM
MFSATLSQEI RPVCKKFMRN PLEVYVDDDT KLTLHGLQQY YIKLSEAEKN RKLNELLDSL
EFNQVIIFVK STLRANELDK LLRECNFPSI AVHSGVSQEE RIKRYKEFKE FNKRICVATD
VFGRGIDIER INLAINYDLP ADADSYLHRV GRAGRFGTKG LSISFVSNEE DEKVLKDIEK
RFEVALPEYP EGGVDSSTYM A
