SUB2_MAGO7
ID SUB2_MAGO7 Reviewed; 436 AA.
AC A4RBS3; G4NIX6; Q2KFX6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=ATP-dependent RNA helicase SUB2;
DE EC=3.6.4.13;
GN Name=SUB2; ORFNames=MGCH7_ch7g559, MGG_02806;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RA Thon M.R., Pan H., Diener A., Papalas J., Taro A., Mitchell T.K.,
RA Dean R.A.;
RT "The sequence of Magnaporthe grisea chromosome 7.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ71152.1; Type=Erroneous gene model prediction; Evidence={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; CM000230; EAQ71152.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM001237; EHA46192.1; -; Genomic_DNA.
DR RefSeq; XP_003720935.1; XM_003720887.1.
DR AlphaFoldDB; A4RBS3; -.
DR SMR; A4RBS3; -.
DR STRING; 318829.MGG_02806T0; -.
DR PRIDE; A4RBS3; -.
DR EnsemblFungi; MGG_02806T0; MGG_02806T0; MGG_02806.
DR GeneID; 2682359; -.
DR KEGG; mgr:MGG_02806; -.
DR VEuPathDB; FungiDB:MGG_02806; -.
DR eggNOG; KOG0329; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; A4RBS3; -.
DR OMA; IKPICRK; -.
DR OrthoDB; 779000at2759; -.
DR Proteomes; UP000009058; Chromosome 7.
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..436
FT /note="ATP-dependent RNA helicase SUB2"
FT /id="PRO_0000294646"
FT DOMAIN 83..258
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 270..431
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 52..80
FT /note="Q motif"
FT MOTIF 205..208
FT /note="DEAD box"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 436 AA; 49163 MW; CEFEE32F8409E539 CRC64;
MSAEEDLIDY SDEELNTNET AAPAADSNGK KGELAAGGNV DKKGSYVGIH STGFRDFLLK
PELLRAIGDC GFEHPSEVQQ TCIPQAMLGG DIICQAKSGL GKTAVFVLTT LQQVEPVAGE
CSVLVMCHTR ELAFQIRNEY NRFSKYMPDI KTGVFFGGTP IQKDAELLKN KETHPHIIVG
TPGRLNALVR DKFLRLSSVR IFVLDECDKM LDQIDMRRDV QEIFRATPQQ KQVMMFSATL
SDEIKPICKK FMQNPTEHYV DEDTKLTLHG LQQYFVALEE KEKNRKLNEL LDDLQFNQVI
IFVKSTLRAT ELDKLLRECN FPSIAVHSGV SQEERIRRYK EFKEFNKRIC VATDVFGRGI
DIERINLAIN YDMPADADSY LHRVGRAGRF GTKGLAVSFV TNDQDKEVLT AIEKRFEVPI
PEFPKDGIDA STYMAS
