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   03-AUG-2022, entry version 87.
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 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; 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-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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}.
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DR   EMBL; CP000498; ABN66290.1; -; Genomic_DNA.
DR   RefSeq; XP_001384319.1; XM_001384282.1.
DR   AlphaFoldDB; A3LST5; -.
DR   SMR; A3LST5; -.
DR   STRING; 4924.XP_001384319.1; -.
DR   EnsemblFungi; ABN66290; ABN66290; PICST_83587.
DR   GeneID; 4838602; -.
DR   KEGG; pic:PICST_83587; -.
DR   eggNOG; KOG0329; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; A3LST5; -.
DR   OMA; IKPICRK; -.
DR   OrthoDB; 779000at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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..433
FT                   /note="ATP-dependent RNA helicase SUB2"
FT                   /id="PRO_0000285148"
FT   DOMAIN          80..255
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          267..428
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           49..77
FT                   /note="Q motif"
FT   MOTIF           202..205
FT                   /note="DEAD box"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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