ID J8Q2Q3_SACAR Unreviewed; 887 AA.
AC J8Q2Q3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=SU7_3040 {ECO:0000313|EMBL:EJS41894.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS41894.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS41894.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJS41894.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ALIE01000173; EJS41894.1; -; Genomic_DNA.
DR AlphaFoldDB; J8Q2Q3; -.
DR HOGENOM; CLU_001832_7_2_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000006968; Chromosome XIV.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:UniProt.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR GO; GO:0006396; P:RNA processing; IEA:UniProt.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006968}.
FT DOMAIN 244..410
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 435..609
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 100838 MW; D6CCBD8028C04E4A CRC64;
MSNSISKTGK RRVKRTHEFT RRDENIKSTG PSSPLSREDE DKEAKGKSCT PSEPKRSRYD
PNKIFSSTTQ RLEDSAAFCE GINGSEREGF KYHKQTSSNN GVSSERDLLY VTQDQAKDAP
PVDLDERSNS NRKEKPVQKR TNAKKSDKIN RQQMWEEQQL RNAMANKTDH PDDITVEGSD
KYDYVFDTDA MIDYTNDNDD LLPEEKLQYE TRLAEALETE EARILTIQET RELLPVYQHK
DDLLKEIKKN QVLIIMGETG SGKTTQLPQY LVDDGYTKNG EFQIAITQPR RVAATSVAAR
VADEMNVVLG KEVGYQIRFE DKTTPNETVL KYMTDGMLLR EFLADSKLSR YSCIMIDEAH
ERTLATDILI GLLKGILPQR PTLKLLISSA TMNAKKFSEF FDDCPIFNVP GRRYPVDIHY
TLQPEANYIH AAITTIFQIH TTQALPGDIL VFLTGQEEIE RTKIKLEEIM CKLGSRTRQM
LITPIYANLP QEQQSKIFQP TPEDCRKVVL ATNIAETSLT IDGIKYVIDP GFVKENSYVP
STGMTQLLTV PCSRASVDQR AGRAGRVGPG KCFRIFTKWS YLHELELMPK PEITRTNLSN
TVLLLLSLGV TDLIKFPLMD KPNIPTLRKS LENLYILGAL NSKGAITHMG KMMCEFPCEP
EFAKVLYTAA THEQCQGVLE ECLTIVSMLH ETSSLFIGQK GEAAASITGE VESDHILYLE
IFNQWRNSKF SRSWCQDHKI QFKTMSRVRN IRNQLFKCSE KVGLVKKNDE ARRKMSNLVA
YINGRITRCF ISGFPMNVVQ LGPTGYHTIG KSSGGLNVNV HPSSILFANY KKKSQRPSKY
VLYQQLMLTS KEFIRDCLVI SKEEWLVEMV PQVFKGLIGD KTTRRRE
//