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Database: UniProt
Entry: A0A2K6AAE6_MANLE
LinkDB: A0A2K6AAE6_MANLE
Original site: A0A2K6AAE6_MANLE 
ID   A0A2K6AAE6_MANLE        Unreviewed;       678 AA.
AC   A0A2K6AAE6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=DHX58 {ECO:0000313|Ensembl:ENSMLEP00000037005.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000037005.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000037005.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:ARBA00029316};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00029316};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
CC       {ECO:0000256|ARBA:ARBA00006866}.
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DR   RefSeq; XP_011854213.1; XM_011998823.1.
DR   RefSeq; XP_011854214.1; XM_011998824.1.
DR   AlphaFoldDB; A0A2K6AAE6; -.
DR   STRING; 9568.ENSMLEP00000037005; -.
DR   Ensembl; ENSMLET00000060611.1; ENSMLEP00000037005.1; ENSMLEG00000042616.1.
DR   GeneID; 105552964; -.
DR   KEGG; mleu:105552964; -.
DR   CTD; 79132; -.
DR   GeneTree; ENSGT00940000153173; -.
DR   OMA; HRAVGNY; -.
DR   OrthoDB; 342391at2759; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045824; P:negative regulation of innate immune response; IEA:Ensembl.
DR   GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IEA:Ensembl.
DR   GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IEA:Ensembl.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; IEA:Ensembl.
DR   GO; GO:1900245; P:positive regulation of MDA-5 signaling pathway; IEA:Ensembl.
DR   GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IEA:Ensembl.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR   CDD; cd18075; DEXHc_RLR-3; 1.
DR   CDD; cd15806; LGP2_C; 1.
DR   CDD; cd12090; MDA5_ID; 1.
DR   CDD; cd18802; SF2_C_dicer; 1.
DR   Gene3D; 1.20.1320.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.170.150.30; RIG-I-like receptor, C-terminal regulatory domain; 1.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041204; RIG-I-like_C.
DR   InterPro; IPR038557; RLR_C_sf.
DR   InterPro; IPR021673; RLR_CTR.
DR   PANTHER; PTHR14074:SF7; ATP-DEPENDENT RNA HELICASE DHX58; 1.
DR   PANTHER; PTHR14074; HELICASE WITH DEATH DOMAIN-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF18119; RIG-I_C; 1.
DR   Pfam; PF11648; RIG-I_C-RD; 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.
DR   PROSITE; PS51789; RLR_CTR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01125}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01125}.
FT   DOMAIN          11..188
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          350..514
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          539..669
FT                   /note="RLR CTR"
FT                   /evidence="ECO:0000259|PROSITE:PS51789"
FT   BINDING         556
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT   BINDING         559
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT   BINDING         612
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT   BINDING         615
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
SQ   SEQUENCE   678 AA;  76745 MW;  E31A89C208F57575 CRC64;
     MELRPYQWEV IMPALEGKNI IIWLPTGAGK TRAAAYVAKR HLETVDGAKV VVLVNRVHLV
     TQHGEEFRRM LDGRWTVTTL SGDMGPRAGF GHLARCHDLL ICTAELLQMA LTSPEEEEHV
     ELTAFSLIVV DECHHTHKDT VYNVIMSRYL ELKLQRARPL PQVLGLTASP GTGGASKLDG
     AIDHVLQLCA NLDTWCIMSP QNYRPRLQEH SQQPCKQYNL CHRRSQDPFG DLLKKLMDQV
     HDHLEMPELS RNFGTQMYEQ QVVKLSEAAA LAGLQEQRVY ALHLRRYNDA LLIHDTVRAV
     DALAALQDFY HREHVTKTQI LCAERRLLAL FDGHKNVLAH LATHGPENPK LEMLEKILQR
     QFRSSDSPRG IIFTRTRQSA HSLLLWLQQQ PGLQTVDIRA QLLIGAGNSS QSTHMTQRDQ
     QEVIRKFRDG TLNLLVATSV AEEGLDIPQC NVVVRYGLLT NEISMVQARG RARADQSVYS
     FVATEGSREL KRELINEALE TLMEQAVAAV QKMDQAEYQA KIRDLQQAAL TKRAAQAAQR
     ESQRRQFPVE HVQLLCINCM VAVGHGSDLR KVEGTHHVNV NPNFSIYYNV SRDPVVINKV
     FKDWKPGGVI SCRNCGEIWG LQMIYKSVKL PALKVRSMLL ETPQGRIQAK KWSRVPFSVP
     DFDFLQHCAQ NLSDLSLD
//
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