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Database: UniProt
Entry: A3LST5
LinkDB: A3LST5
Original site: A3LST5 
ID   SUB2_PICST              Reviewed;         433 AA.
AC   A3LST5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   16-OCT-2019, entry version 78.
DE   RecName: Full=ATP-dependent RNA helicase SUB2;
DE            EC=3.6.4.13;
GN   Name=SUB2; ORFNames=PICST_83587;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 /
OS   NRRL Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-
RT   fermenting yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000498; ABN66290.1; -; Genomic_DNA.
DR   RefSeq; XP_001384319.1; XM_001384282.1.
DR   SMR; A3LST5; -.
DR   STRING; 4924.XP_001384319.1; -.
DR   PRIDE; A3LST5; -.
DR   EnsemblFungi; ABN66290; ABN66290; PICST_83587.
DR   GeneID; 4838602; -.
DR   KEGG; pic:PICST_83587; -.
DR   eggNOG; KOG0329; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; A3LST5; -.
DR   KO; K12812; -.
DR   OMA; VCADEAP; -.
DR   OrthoDB; 779000at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:EnsemblFungi.
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:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
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    433       ATP-dependent RNA helicase SUB2.
FT                                /FTId=PRO_0000285148.
FT   DOMAIN       80    255       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      267    428       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      93    100       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        49     77       Q motif.
FT   MOTIF       202    205       DEAD box.
SQ   SEQUENCE   433 AA;  48980 MW;  7B08307FD5A6416A CRC64;
     MSHEGQEELL DYSDSEEIAV PTTTEVAGAD SATDKEADKK GSYVGIHATG FRDFLLKPEL
     LRAIGDCGFE HPSEVQQVCI PQSILGTDVL CQAKSGLGKT AVFVLSTLQQ LDPVPGEIST
     LVICHTRELA YQIRNEYARF SKYMPDVKTE VFYGGTPIKR DIEKLKSKDT CPHIVVATPG
     RLHALVNEKA IRLSNVKSFV IDECDKVLES IDMRRDVQDI FRATPHQKQV MMFSATLSQE
     IRPVCKKFMQ NPLEIYVDDE AKLTLHGLQQ YYIKLEEKEK NRKLSDLLDS LEFNQVIIFV
     KSTQRANELN KLLCSCNFPS IAVHSGLPQE ERIERYRSFK EFNKRICVST DVFGRGIDIE
     RINLAINYDL PNEADQYLHR VGRAGRFGTK GLAISLVGSK EDEEVLEKIQ SRFDVKITEF
     PEEGVDPSTY MNT
//
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