SUB2_KLULA
ID SUB2_KLULA Reviewed; 437 AA.
AC Q6CM95;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=ATP-dependent RNA helicase SUB2;
DE EC=3.6.4.13;
GN Name=SUB2; OrderedLocusNames=KLLA0E22033g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382125; CAH00031.1; -; Genomic_DNA.
DR RefSeq; XP_454944.1; XM_454944.1.
DR AlphaFoldDB; Q6CM95; -.
DR SMR; Q6CM95; -.
DR STRING; 28985.XP_454944.1; -.
DR EnsemblFungi; CAH00031; CAH00031; KLLA0_E21935g.
DR GeneID; 2894435; -.
DR KEGG; kla:KLLA0_E21935g; -.
DR eggNOG; KOG0329; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q6CM95; -.
DR OMA; IKPICRK; -.
DR Proteomes; UP000000598; Chromosome E.
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; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:EnsemblFungi.
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..437
FT /note="ATP-dependent RNA helicase SUB2"
FT /id="PRO_0000232266"
FT DOMAIN 84..259
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 287..432
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 53..81
FT /note="Q motif"
FT MOTIF 206..209
FT /note="DECD box"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 437 AA; 49822 MW; F58D08652F80F469 CRC64;
MSHEAEEDLL EYSDNEQEVQ VDNKATEVNA EGNGESQAKD SDKKGSYVGI HSTGFKDFLL
KPELSRAIID CGFEHPSEVQ QHTIPQSIHG TDVLCQAKSG LGKTAVFVLS TLQQLDPVQG
EVSVVVLCNA RELAYQIRNE YLRFSKYMPD VKTAVFYGGT EYKNDIDLLS KKETVPHIIV
ATPGRLKALV RDKHIDLSHV KNFVIDECDK VLEELDMRRD VQDIFRATPR DKQVMMFSAT
LSQEIRPICR RFLQNPLEIF VDDEAKLTLH GLQQYYIKLN EKEKNRKLAQ LLDDLEFNQV
IIFVKSTVRA NELTKLLNAS NFPAITVHGH MKQEERIARY KAFKEFEKRI CVSTDVFGRG
IDIERINLAI NYDMPNEADQ YLHRVGRAGR FGTKGLAISM ISSEDDEQVL AKIQERFDVK
ITEFPEEGVD PSTYLNT
