ID U6CWH4_NEOVI Unreviewed; 1023 AA.
AC U6CWH4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=IFIH1 {ECO:0000313|EMBL:CCP73918.1};
OS Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Neogale.
OX NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP73918.1};
RN [1] {ECO:0000313|EMBL:CCP73918.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pool of brain {ECO:0000313|EMBL:CCP73918.1};
RA Anistoroaei R., Christensen K.;
RT "An American mink transcriptome.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNVIP00000008306.1}
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; HAAF01002092; CCP73918.1; -; mRNA.
DR Ensembl; ENSNVIT00000009725.1; ENSNVIP00000008306.1; ENSNVIG00000006456.1.
DR GeneTree; ENSGT00940000153173; -.
DR Proteomes; UP000694425; 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:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IEA:Ensembl.
DR CDD; cd08819; CARD_MDA5_r2; 1.
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; IPR001315; CARD.
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; PS50209; CARD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51789; RLR_CTR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CCP73918.1};
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:UP000694425};
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 110..176
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT DOMAIN 316..509
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 697..879
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 890..1018
FT /note="RLR CTR"
FT /evidence="ECO:0000259|PROSITE:PS51789"
FT REGION 225..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..291
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 962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
SQ SEQUENCE 1023 AA; 115974 MW; 9AA8F56236FB9DB3 CRC64;
MSNGYSADKS FCYLISCFRA RVKTYIQVEP VLDYLDFLPN DVKEQIQRTA VNAGNMQAAD
ELLNALEKGG WPPGWPRQFL VALQRAGSVL AARYLNPELT DLPSPSSENA HDECLQLLNL
LQPTLVDRLL VRDVLDKCVE KKLLTNEDRN RISAAENNGN ESGVRELLKR IVQKENWFSS
FLAALSETEN HALVQELTGT PHFESNAETE NLSQESGPDI QEAVLLATGP PSPEGAGWDE
DSDSPDSSLV DSSVVSESDT SLAEGSVSCL DESLGHNSNM GSDSGTMGSD SDEENVAERA
SPEPELNLRP YQMEVAQPAL EGKNIIICLP TGSGKTRVAV YIAKEHLDKK KKASEPGKVI
VLVNKVPLVE QLFRKEFEPF LKKWYHTIGL SGDTQLKISF PEVVKTYDVI ISTAQILENS
LSNSEKGEDD GVQFSDFSLI VIDECHHTNK EAVYNNIMRR YLKQKLKNNK LKKECKPVIP
LPQILGLTAS PGVGGAKRQA EAKDHILKIC ANLDACTIKT VKENIHQLKD QIKEPCKKFA
IADDTREDPF KDKLLEIMNK IQSFCQMSPM PDFGTQPYEQ WTTQMEKKAA REGNRKERVC
AEHLRKYNEA LQINDTIRTI DAYNHLETFY NDEKEKKYAV QEDESDEDGD GGGDEDEDDE
KKPLSLDKTD RFLMDLFFEN RRMLKKLAEN PKHENEKLTK LRNTIMEQYT RTEESARGII
FTKTRQSAYA LSQWITENKK FAEVGVKAHH LIGAGHSSEF KPMTQNEQKE VISKFRTGKI
NLLIATTVAE EGLDIKECNI VIRYGLVTNE IAMVQARGRA RADESTYVLV AHSNSGVIER
EIVNDFREKM MYKAIDHVQN MNPEEYARKI LELQMQSIME KKMKIKRSIA KCYKENPSLI
NFLCKNCGEL ACSGEDIHVI EKMHHVNMTP VFKELYTVRE NKALQKKFVD YQTNGEIICK
TCGQAWGTMM VHKGLDLPCL KIKNFVVFFK NNMLKKQYKK WVELPITFPD LDYTQYCLFS
DED
//
