ID G3HZV6_CRIGR Unreviewed; 1022 AA.
AC G3HZV6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=Ifih1 {ECO:0000313|Ensembl:ENSCGRP00001027862.1};
GN ORFNames=I79_016620 {ECO:0000313|EMBL:EGW01901.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW01901.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2] {ECO:0000313|EMBL:EGW01901.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCGRP00001027862.1}
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 EMBL; JH000988; EGW01901.1; -; Genomic_DNA.
DR RefSeq; XP_003508679.1; XM_003508631.3.
DR STRING; 10029.G3HZV6; -.
DR PaxDb; 10029-XP_007608367-1; -.
DR Ensembl; ENSCGRT00001032110.1; ENSCGRP00001027862.1; ENSCGRG00001024740.1.
DR GeneID; 100767593; -.
DR CTD; 64135; -.
DR eggNOG; KOG0354; Eukaryota.
DR GeneTree; ENSGT00940000153173; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR Proteomes; UP000694386; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0038187; F:pattern recognition receptor activity; IEA:Ensembl.
DR GO; GO:0043021; F:ribonucleoprotein complex 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:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0039530; P:MDA-5 signaling pathway; IEA:Ensembl.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; IEA:Ensembl.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IEA:Ensembl.
DR CDD; cd15807; MDA5_C; 1.
DR CDD; cd12090; MDA5_ID; 1.
DR CDD; cd18802; SF2_C_dicer; 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; IPR011029; DEATH-like_dom_sf.
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; HELICASE WITH DEATH DOMAIN-RELATED; 1.
DR PANTHER; PTHR14074:SF14; INTERFERON-INDUCED HELICASE C DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF16739; CARD_2; 2.
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; SSF47986; DEATH domain; 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, ECO:0000313|EMBL:EGW01901.1};
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:UP000001075};
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 314..507
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 704..869
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 890..1017
FT /note="RLR CTR"
FT /evidence="ECO:0000259|PROSITE:PS51789"
FT REGION 231..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 959
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 961
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
SQ SEQUENCE 1022 AA; 115469 MW; A7D38BA414DFFC1C CRC64;
MSNVCSTEDS FCYLISIFRS RLKKCFEVEP VLDYLTFLPT ETKEQILKKA ATCGNTSAAE
LLLSTLEKRE WQPGWTQIFV EALEHSGSHL AARYVRLTDL PSPSIETAHD ECLHLLNLLQ
PTLVDKLLIN DVLDTCMEKG LLTPEDRNRI SAAGNAGNES GVRELLRRIV HKENWFSTFL
DVLRQTGNDA LCQELTGAGC PEDIAELENL YQEDGPEAHE PVLCALDESS LETEAGDTEN
SSPETSFADC SVTSESDTSL AAGSVSCLDE SLGHNSNMGS DSGIMGSDSD ESTGTQRASP
DPELQLRPYQ MEVAQPALEG KNIIICLPTG SGKTRVAVYI TKDHLDKKKQ ASEPGKVMVL
VNKVMLAEQL FRKEFNPFLK KWYRIIGLSG DTQLKISFPE VVKSYDVIIS TAQILENSLL
NLESGEDDGV QLSDFSLIII DECHHTNKEA VYNNIMRRYL KQKLKNNKLK KQNKPVVHLP
QILGLTASPG VGGAKKQAEA EKHILNICAN LDAFTIKTVK ENLGQLKHQI KEPCKKFVIA
DDTRENPFKE KLLEIMTSIQ TYCQMSPMSD FGTQPYEQWA ILMEKKAAKS GNRKNRVCAE
HLRKYNEALQ INDTIRMIDA YSHLETFYSD EKEKKLAVLE DSDESEDDAS GHAEELKDNV
KESLKLDETD EFLMNLFFDN KKMLKKLAEN PKYENEKLIK LRKTILEQFT KTEESSRGII
FTKTRQSTYA LSQWITENEK FAEVGVKAHH LIGAGHSSEV KPMTQNEQKE VISKFRTGKI
NLLIATTVAE EGLDIKECNI VIRYGLVTNE IAMVQARGRA RADESTYVLV TSSGSGVTER
EIVNDFREKM MYKAINRVQN MKPEEYAREI LALQVQSILE KKMKVKRSIA KHYINNPSLI
TLLCKNCSML VCSGENIHVI EKMHHVNMTQ EFKRLYIVRE NKALQKKFAD YQANGEIICK
CGQAWGTMMV HKGLDLPCLK IRNFVVEFKN NSSKKQYKKW VELPVRFPDL DCSEYCLCSD
ED
//
