ID A0A3Q7UBB9_VULVU Unreviewed; 925 AA.
AC A0A3Q7UBB9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=DDX58 {ECO:0000313|RefSeq:XP_025864780.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025864780.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025864780.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025864780.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025864780.1};
RG RefSeq;
RL Submitted (NOV-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_025864780.1; XM_026008995.1.
DR AlphaFoldDB; A0A3Q7UBB9; -.
DR STRING; 9627.ENSVVUP00000028923; -.
DR KEGG; vvp:112927563; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd08817; CARD_RIG-I_r2; 1.
DR CDD; cd18073; DEXHc_RIG-I_DDX58; 1.
DR CDD; cd12090; MDA5_ID; 1.
DR CDD; cd15805; RIG-I_C; 1.
DR Gene3D; 1.20.1320.30; -; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 2.
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; IPR031964; CARD_dom.
DR InterPro; IPR042145; CARD_RIG-I_r2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR011029; DEATH-like_dom_sf.
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:SF16; ANTIVIRAL INNATE IMMUNE RESPONSE RECEPTOR RIG-I; 1.
DR PANTHER; PTHR14074; HELICASE WITH DEATH DOMAIN-RELATED; 1.
DR Pfam; PF16739; CARD_2; 2.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 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; 2.
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 ECO:0000313|RefSeq:XP_025864780.1};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01125}.
FT DOMAIN 246..425
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 610..776
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 794..925
FT /note="RLR CTR"
FT /evidence="ECO:0000259|PROSITE:PS51789"
FT BINDING 810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 813
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 864
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
SQ SEQUENCE 925 AA; 105883 MW; 79584C3BAB40717D CRC64;
MTAEERRNLH AFRDYVIKTL DPAYILSYMA PWFKDDEVQY IQAEKNNKGT MEAASLFLKY
LLELQEEGWF RGFLDALGHA GYSGLYEAIE SWNFQKIESL EEYRLLLKRL QPEFKTTVNP
NDILPKISEC LISQECEEII QICSNKGLMA GAEKMVECLL RSDKENWPKT LKLALETEES
KFSQLWIVDK DAEPKVLEDD EIETSEVQIF YKEEPECQNL SQDPCPPSAA STCTPLKPRN
YQLELALPAK EGKNTIICAP TGCGKTFVAL LICEHHLKKF PQGQKGKIVF FAIQIPVYEQ
QNSVFSKYFE RLGYKVAGIS GATSENISVE QIVENNDIIV LTPQILVNCL RNGTIPSLSV
FTLMIFDECH NTSKHHPYNM IMFNYLDQKL GGSSDPLPQV VGLTASVGIG DAKNTMEAME
YICKLCASLD TSVIATVKDN LEELEEIIYK PQKFFRKVES RTTDRFKCII SQLMRETESL
AKNVFDELGT ITLENVSQIQ NRNFGTQKYE QWIVSVQKAC MVFQLPNKDE ESRICKALFL
YTSHLRKYND ALIINEHARM KDALDYLKDF FTDVRAAGFD EIEQHLTCRF EEKLQELESI
SMDLSNENPK LKDLSFILQE EYHLNPESRT ILFVKTRALV DALKKWIEEN SELSFLKPGI
LTGRGKTNHS TGMTLPAQKC ALDAFRTDGD KKILIATSVA DEGIDIAQCN LVILYEYVGN
VIRMIQTRGR GRARGSKCFL LTSNADVIKK EKLNIYKEKI MNDSILSLQM WNEAVFKEKV
LQIQIQEKNI RDSQEKVELV PDKENKKLLC RKCKAFACYT ADIRVVEECH YTVVGDAFTK
CFVSKLHPKP KSFGHFEKRA KIFCARRNCG HDWGIHVKYK TFEIPVIKIE SFVVEDIATG
AQKLYAKWKG FPFEKIPFGS PEIPK
//
