GenomeNet

Database: UniProt
Entry: A7EIX7
LinkDB: A7EIX7
Original site: A7EIX7 
ID   SUB2_SCLS1              Reviewed;         444 AA.
AC   A7EIX7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   16-OCT-2019, entry version 69.
DE   RecName: Full=ATP-dependent RNA helicase sub2;
DE            EC=3.6.4.13;
GN   Name=sub2; ORFNames=SS1G_05270;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White
OS   mold) (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in transcription
CC       elongation and required for the export of mRNA out of the nucleus.
CC       SUB2 plays also a role in pre-mRNA splicing and spliceosome
CC       assembly. May be involved in rDNA and telomeric silencing, and
CC       maintenance of genome integrity (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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH476626; EDO02793.1; -; Genomic_DNA.
DR   RefSeq; XP_001593842.1; XM_001593792.1.
DR   SMR; A7EIX7; -.
DR   STRING; 5180.EDO02793; -.
DR   PRIDE; A7EIX7; -.
DR   EnsemblFungi; EDO02793; EDO02793; SS1G_05270.
DR   GeneID; 5490006; -.
DR   KEGG; ssl:SS1G_05270; -.
DR   EuPathDB; FungiDB:SS1G_05270; -.
DR   InParanoid; A7EIX7; -.
DR   KO; K12812; -.
DR   OMA; VCADEAP; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000346; C:transcription export complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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; Complete proteome; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; mRNA transport; Nucleotide-binding; Nucleus;
KW   Reference proteome; RNA-binding; Spliceosome; Transport.
FT   CHAIN         1    444       ATP-dependent RNA helicase sub2.
FT                                /FTId=PRO_0000310222.
FT   DOMAIN       90    265       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      277    438       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     103    110       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        59     87       Q motif.
FT   MOTIF       212    215       DECD box.
SQ   SEQUENCE   444 AA;  49655 MW;  D673C788EFD7DABB CRC64;
     MSAAEEDLID YSDEELATTE APAPAAGANG GVKGDSGNLT VSGNAAAAKK GSYVGIHSTG
     FREFLLKPEL LRAISWCGFE HPSEVQQVCI PQAILGTDVL CQAKSGLGKT AVFVLTTLQQ
     VEVVAGETSV LVMCHTRELA YQIRNEYQRF CHFMPDVKIG VFYGGVPISK DVEVLKNPET
     HPHIIVGTPG RLNALVRDKY LRLNSVKVFV LDECDKMLDQ IDMRRDVQEI FRATPPQKQV
     MMFSATLSQE VRPICKKFMQ NPLEIYIDNE TKLTLYGLQQ YYIKLEEREK NRRLNELLDE
     LSFNQVIIFV KSTVRATELD KLLRECNFPS VAIHSGVSQE ERIKRFNDFK DFNKRICVAT
     DVFGRGIDVN KINLAINYDL PPDADSYLHR VGRAGRFGTK GLAISFVSNE ADQEVLKAVE
     KRFEVALPEY PEGGVDSAAY TKTD
//
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