ID R9APL1_WALI9 Unreviewed; 801 AA.
AC R9APL1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=J056_002201 {ECO:0000313|EMBL:EOR04123.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR04123.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
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 {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
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DR EMBL; KE007225; EOR04123.1; -; Genomic_DNA.
DR RefSeq; XP_009266340.1; XM_009268065.1.
DR AlphaFoldDB; R9APL1; -.
DR STRING; 1299270.R9APL1; -.
DR GeneID; 20375153; -.
DR KEGG; wic:J056_002201; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_6_1; -.
DR OMA; REAMTAC; -.
DR OrthoDB; 276261at2759; -.
DR Proteomes; UP000014064; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR24031:SF384; DEAD-BOX ATP-DEPENDENT RNA HELICASE 31; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|RuleBase:RU365068, ECO:0000313|EMBL:EOR04123.1};
KW Hydrolase {ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 116..316
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 344..522
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 26..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..538
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 61..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 89325 MW; 064212B1625255E9 CRC64;
MLLRPVRRFT SPLRLLSVVR STATVSASSQ SQQPPSRHHP QPEFPQLIPS SVQTGSYHPI
APDDSHKRKE DDESFDSVAT KLSPETMKAI TVSPHKHTKM SAVQSAIFNL LPGLSDAQSN
DRKDLFVKSK TGTGKTMAFL VPAIEARLMA IQNAFDSASG SDKEKFKAGK QYANSTVGAV
IISPTRELAT QIANEAIKLC THHKGFQVRL FVGGANKGKQ LSEFKNGRGD IIVTTPGRMN
DVLQTSPMVK SALNTSPTLI LDEADTLLEM GFKDELNAII EHLPGHPTRQ SVLLSATLSE
GIRKVAKSIL KPNHLYIDTV PEGESNSHAK IPQFYSALSS PGHQLPHLLR LISHDQLTNP
KSKIMIFCPT TKMTMLYSTI FRALSKSLPK KANIFEIHSK RTMEQRSRAS EHFRRDKSDS
SVLVTSDVSA RGVDYPNVTR VIQIGVPPSA DQYVHRIGRT GRGGSSGRAD FVMDYYELPF
LTWQLNQHNI ADNPAKEFAK QVAQLAESTG NQDVVDKVNN IENELKDLIS QVDELAVRET
FASLLGYYLP KAPVMRTTKG VVVEGLKSWT TEAMGLPRPP YISDTFLLKM GLTDNRSKRF
GQKDRYSGDA AKEYFSVADK RSGKDQGLRY NLDGRQTYRG SDKGKLRSEW DKRGLYGYRG
QGAPPPSERN KPEMDADEYR SAPYGREHLS PEYIGASNRP RVRSRTDFDY GGKGRSGGIK
KPTDRRSYMT SAHPTRAVYA HDEERQAEAE VQARKQRAQK IAESPRTASH YELSNKLARR
RRTANKEFHA RKVLIQDAMH Q
//
