ID A0A109FH69_9BASI Unreviewed; 838 AA.
AC A0A109FH69;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=p-loop containing nucleoside triphosphate hydrolase protein {ECO:0000313|EMBL:KWU44397.1};
DE Flags: Fragment;
GN ORFNames=RHOSPDRAFT_11946 {ECO:0000313|EMBL:KWU44397.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44397.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44397.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44397.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000256|ARBA:ARBA00003706}.
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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DR EMBL; KQ954479; KWU44397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FH69; -.
DR STRING; 1305733.A0A109FH69; -.
DR OrthoDB; 5475716at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
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:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 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 {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KWU44397.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 48..76
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 94..271
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 336..478
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 473..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..76
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 474..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KWU44397.1"
FT NON_TER 838
FT /evidence="ECO:0000313|EMBL:KWU44397.1"
SQ SEQUENCE 838 AA; 91529 MW; 07AE7E005BBB9BA8 CRC64;
SDDDEDEEED ALFASLASLQ HSRNLAEGAA LVRKGKDNKQ SKQLTGGGSF QSLGLPPLLL
KALLQRGFTT PTPIQRLALP SILASTESVV SDKGQKITVA RDHLCMARTG SGKTLCYLLP
LLSQLWTHSD KFGARGLILV PTRELALQVL KVGKDLARGI KGEGESLRWA MIVGGEAMEA
QFELMAGNPD VIIATPGRFL HLLVEMNYSL STISSLIIDE ADRLFELGFA EQLTEILHRV
PATRQTLLFS ATLPSSLVGF AKAGLQNPKL IRLDVDQKIS KDLRMAYLNV KSTEKEAVLL
GLLREVIRVP VMSEEQRSAE HARVARENEA ELDLNSVNGA NIAPHQTVVF VSTKHHVEYI
TGLLTAANYS VSPIYGSMDQ TARKISLSRF RSGQTSILVV TDLAARGIDV PGVENVINYD
FPNGTRAFVH RVGRTARAGR TGWAYTFVTA NDLPYLFDLE LFLSRPLKLC PLSSSAADPS
SSSSGDDTAV TGEPDYAHTL ILGAPPRLLT DTDIETHRSL VEHHPHLEQL QQVSQRGQRM
YERGLGKASP ESYRRAKEMA REKVERAAKT GGVITEAGEE HPIYDEYLAS ALGRAVERSR
AELLAKIGGF RPNETVLEVN AKGKNGASEG SVASLMKERR KALLRSERAR QLTKKVDEEE
LPEVPEGAAA RDDSANGQMD AVFGKKPAKR AKPAGDKPSW RDERFFMGYE QEGAATEAGY
ALTNGESFVA QAKHSTYDMG GRGDTEGTPA EALAQRASTL KWDRKSKKFV RADQVGQDNK
KLIRSESGQR LPATFKSGVY DEWRKNARIN VPRVGDQEIS GRTTATGGGG GGGKRFRH
//
