ID   SUB21_VANPO             Reviewed;         441 AA.
AC   A7TLA0;
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 SUB2-1;
DE            EC=3.6.4.13;
GN   Name=SUB2-1; ORFNames=Kpol_1041p33;
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; DS480413; EDO16975.1; -; Genomic_DNA.
DR   RefSeq; XP_001644833.1; XM_001644783.1.
DR   AlphaFoldDB; A7TLA0; -.
DR   SMR; A7TLA0; -.
DR   STRING; 436907.A7TLA0; -.
DR   EnsemblFungi; EDO16975; EDO16975; Kpol_1041p33.
DR   GeneID; 5545160; -.
DR   KEGG; vpo:Kpol_1041p33; -.
DR   eggNOG; KOG0329; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; A7TLA0; -.
DR   OMA; IKPICRK; -.
DR   OrthoDB; 779000at2759; -.
DR   PhylomeDB; A7TLA0; -.
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..441
FT                   /note="ATP-dependent RNA helicase SUB2-1"
FT                   /id="PRO_0000310223"
FT   DOMAIN          88..263
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          291..436
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           57..85
FT                   /note="Q motif"
FT   MOTIF           210..213
FT                   /note="DECD box"
FT   BINDING         101..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   441 AA;  49857 MW;  FAC3D02A46D8CAEC CRC64;
     MSHEGEEDLL EYSDNEQDIQ VDASKAAEPS ELDATTAEDA SNGDAEKKGS YVGIHSTGFK
     DFLLKPELAR AIIDCGFEHP SEVQQHTIPQ SIHGTDVLCQ AKSGLGKTAV FVLSTLQQLD
     PVPGEVSVVV ICNARELAYQ IRNEYLRFSK YMPDVKTAVF YGGTPINKDA ELLKNKETAP
     HIVVATPGRL KALVRDKLID LSHVKNFVID ECDKVLEELD MRRDVQDIFR ATPRDKQVMM
     FSATLSEEIR PICRRFLQNP LEIFVDDEAK LTLHGLQQYY TKLQENEKNR KLAQLLDDLE
     FNQVIIFVKS TKRANELTKL LNESNFPAIT VHGHMKQAER IARYKAFKEF EKRICVSTDV
     FGRGIDIERI NLAINYDLTT EADQYLHRVG RAGRFGTKGL AISFVSSPED EEVLGKIQER
     FDVKIAEFPE EGIDPSTYLN N