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Database: UniProt
Entry: J8Q2Q3_SACAR
LinkDB: J8Q2Q3_SACAR
Original site: J8Q2Q3_SACAR 
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}.
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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
//
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