SUB2_YEAS7
ID SUB2_YEAS7 Reviewed; 446 AA.
AC A6ZXP4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=ATP-dependent RNA helicase SUB2;
DE EC=3.6.4.13;
DE AltName: Full=Suppressor of BRR1 protein 2;
GN Name=SUB2; ORFNames=SCY_0832;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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 -!- SUBUNIT: Component of the TREX complex composed of at least SUB2, TEX1,
CC YRA1 and the four THO complex components: HPR1, MFT1, THO2 and THP1.
CC Interacts with HPR1, YRA1, and YRA2. SUB2 may mediate the interaction
CC between the THO complex and YRA1. Associates with growing mRNP
CC complexes during transcription. This association requires the presence
CC of HPR1. Interacts also with SAC3 (By similarity). {ECO:0000250}.
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; AAFW02000145; EDN60274.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZXP4; -.
DR SMR; A6ZXP4; -.
DR IntAct; A6ZXP4; 1.
DR MINT; A6ZXP4; -.
DR PRIDE; A6ZXP4; -.
DR EnsemblFungi; EDN60274; EDN60274; SCY_0832.
DR HOGENOM; CLU_003041_1_0_1; -.
DR Proteomes; UP000007060; 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 Acetylation; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleotide-binding; Nucleus; Phosphoprotein;
KW RNA-binding; Spliceosome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q07478"
FT CHAIN 2..446
FT /note="ATP-dependent RNA helicase SUB2"
FT /id="PRO_0000310225"
FT DOMAIN 93..268
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 280..441
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 23..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 62..90
FT /note="Q motif"
FT MOTIF 215..218
FT /note="DECD box"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q07478"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07478"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07478"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07478"
SQ SEQUENCE 446 AA; 50279 MW; 6C17345B74E8C190 CRC64;
MSHEGEEDLL EYSDNEQEIQ IDASKAAEAG ETGAATSATE GDNNNNAAAG DKKGSYVGIH
STGFKDFLLK PELSRAIIDC GFEHPSEVQQ HTIPQSIHGT DVLCQAKSGL GKTAVFVLST
LQQLDPVPGE VAVVVICNAR ELAYQIRNEY LRFSKYMPDV KTAVFYGGTP ISKDAELLKN
KDTAPHIVVA TPGRLKALVR EKYIDLSHVK NFVIDECDKV LEELDMRRDV QEIFRATPRD
KQVMMFSATL SQEIRPICRR FLQNPLEIFV DDEAKLTLHG LQQYYIKLEE REKNRKLAQL
LDDLEFNQVI IFVKSTTRAN ELTKLLNASN FPAITVHGHM KQEERIARYK AFKDFEKRIC
VSTDVFGRGI DIERINLAIN YDLTNEADQY LHRVGRAGRF GTKGLAISFV SSKEDEEVLA
KIQERFDVKI AEFPEEGIDP STYLNN
