SUB2_ASHGO
ID SUB2_ASHGO Reviewed; 438 AA.
AC Q759L6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=ATP-dependent RNA helicase SUB2;
DE EC=3.6.4.13;
GN Name=SUB2; OrderedLocusNames=ADR260C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52180.1; -; Genomic_DNA.
DR RefSeq; NP_984356.1; NM_209709.1.
DR AlphaFoldDB; Q759L6; -.
DR SMR; Q759L6; -.
DR STRING; 33169.AAS52180; -.
DR PRIDE; Q759L6; -.
DR EnsemblFungi; AAS52180; AAS52180; AGOS_ADR260C.
DR GeneID; 4620518; -.
DR KEGG; ago:AGOS_ADR260C; -.
DR eggNOG; KOG0329; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q759L6; -.
DR OMA; IKPICRK; -.
DR Proteomes; UP000000591; Chromosome IV.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; 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 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..438
FT /note="ATP-dependent RNA helicase SUB2"
FT /id="PRO_0000227961"
FT DOMAIN 85..260
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 272..433
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 54..82
FT /note="Q motif"
FT MOTIF 207..210
FT /note="DECD box"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 438 AA; 49743 MW; 87C1D8B58EEFEFE3 CRC64;
MSHEGEEDLL EYSDNEQEIQ VDNTKATEVA GNGEEAADGK DGDKKGSYVG IHSTGFKDFL
LKPELSRAII DCGFEHPSEV QQHTIPQSIH GTDVLCQAKS GLGKTAVFVL STLQQLDPVP
GEVSVVVLCN ARELAYQIRN EYLRFSKYMP DVKTAVFYGG TDTRKDIELL KNKDTAPHIV
VATPGRLKAL VRDNNIDLSH VKNFVIDECD KVLEELDMRR DVQDIFRATP RDKQVMMFSA
TLSQEIRPIC RRFLQNPLEI FVDDEAKLTL HGLQQYYIRL EEREKNRKLA QLLDDLEFNQ
VIIFVKSTLR ANELTKLLNA SNFPAITVHG HMRQEERIAR YKAFKEFEKR ICVSTDVFGR
GIDIERINLA INYDMPSEAD QYLHRVGRAG RFGTKGLAIS LVSSKDDEEV LAKIQERFDV
KITEFPEEGV DPSTYLNT
