ID   SUB22_VANPO             Reviewed;         442 AA.
AC   A7TJT7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP-dependent RNA helicase SUB2-2;
DE            EC=3.6.4.13;
GN   Name=SUB2-2; ORFNames=Kpol_1058p53;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480403; EDO17516.1; -; Genomic_DNA.
DR   RefSeq; XP_001645374.1; XM_001645324.1.
DR   AlphaFoldDB; A7TJT7; -.
DR   SMR; A7TJT7; -.
DR   STRING; 436907.A7TJT7; -.
DR   EnsemblFungi; EDO17516; EDO17516; Kpol_1058p53.
DR   GeneID; 5545734; -.
DR   KEGG; vpo:Kpol_1058p53; -.
DR   eggNOG; KOG0329; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; A7TJT7; -.
DR   OMA; INFELPM; -.
DR   OrthoDB; 779000at2759; -.
DR   PhylomeDB; A7TJT7; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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..442
FT                   /note="ATP-dependent RNA helicase SUB2-2"
FT                   /id="PRO_0000310224"
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   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   442 AA;  49980 MW;  F19EDFB438592F65 CRC64;
     MSHEGEEDLL EYSDNEQEIQ VDATNINESA VDATVSETAE GATTDSEKKG SYVGIHSTGF
     KDFLLKPELA RAIIDCGFEH PSEVQQHTIP QSIHGTDVLC QAKSGLGKTA VFVLSTLQQL
     DPVPGEVSVV VICNARELAY QIRNEYLRFS KYMPDVKTAV FYGGTPITKD AELLKNKETA
     PHIVVATPGR LKALVRDKLI DLSHVKNFVI DECDKVLEEL DMRRDVQDIF RATPRDKQVM
     MFSATLSEEI RPICRRFLQN PLEIFVDDEA KLTLHGLQQY YIKLQENEKN RKLAQLLDDL
     EFNQVIIFVK STKRANELTK LLNESNFPAI TVHGNMKQAE RIARYKAFKE FEKRICVSTD
     VFGRGIDIER INLAINYDLT TEADQYLHRV GRAGRFGTKG LAISFVSSPE DEEVLGKIQE
     RFDVKIAEFP EEGIDPSTYL NN