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Database: UniProt
Entry: A0A452RP09_URSAM
LinkDB: A0A452RP09_URSAM
Original site: A0A452RP09_URSAM 
ID   A0A452RP09_URSAM        Unreviewed;       968 AA.
AC   A0A452RP09;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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:ENSUAMP00000020973.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000020973.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000020973.1}
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   AlphaFoldDB; A0A452RP09; -.
DR   Ensembl; ENSUAMT00000023430.1; ENSUAMP00000020973.1; ENSUAMG00000015811.1.
DR   GeneTree; ENSGT00940000153173; -.
DR   OMA; TFCQMNP; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   CDD; cd08818; CARD_MDA5_r1; 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   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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022};
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          260..453
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          649..824
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          835..963
FT                   /note="RLR CTR"
FT                   /evidence="ECO:0000259|PROSITE:PS51789"
FT   REGION          224..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..605
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         849
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT   BINDING         852
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
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"
SQ   SEQUENCE   968 AA;  110498 MW;  413246C78FFFFEF8 CRC64;
     MSNGYSADQS FCHLISCFRA RVKTYIQVEP VLDYLNFLPD DVKEQIQRTA VNAGNMQAAD
     QLLSALEKGG WPPGWARQFL VALQRAGSDL AARYLNPELT DLPSPSSETT HDECLQLLTL
     LQPTLVDRLL VRDILDRCME KKLLTNEDRS RISAAESNGN ESGVRELLRR IVQKENWFSE
     FLTVLRQTEN HALVQELTGT TCFESNAESD TSLAEGSVSC LDESLGHNSN MGSDSDEENV
     AERASPEPEL HLRPYQMEVA QPALEGKNII ICLPTGSGKT RVAVYIAKDH LDKKKKASEP
     GKVIVLVNKV PLVEQLFRKE FEPFLKKWYH TIGLSGDTQL KISFPEVVKT YDVIISTAQI
     LENSLLNSEK GEDDGVQFSD FSLIVIDECH HTNKEAVYNN IMRRYLKQKL KNNKLKKECK
     PVIPLPQILG LTASPGVGGA KKQAEAKEHI LKICANLDAC TIKTVKENIV QLKDQIKEPC
     KKFAIADDTR EDPFKDKLLE IMNKIQSFCQ MSPMSDFGTQ PYEQWTTQME KKAAREGNRK
     ERVCAEHLRK YNEALQINDT IRTIDAYNHL EAFYNDEKEK KFAVLEDDSD ESGEDGDGDE
     DEDDEKKPLS LDRTDRFLMD LFFENRRMLK KLAENPKHEN EKLIKLRNTI MEQYTRTEES
     ARGIIFTKTR QSAYALSQWI TENKKFAEVG VKAHHLIGAG HSSEFKPMTQ NEQKEVISKF
     RTGKINLLIA TTVAEEGLDI KECNIVIRYG LVTNEIAMVQ ARGRARADES TYVLVAHSNS
     GVIEREIVND FREKMMYKAI DHVQNMNPEE YARKILELQM QSIMEKKMKI KRSIAKHYKE
     NPSLINFLCK NCSVLACSGE DIHVIEKMHH VNMTPVFKEL YIVRENKALR KKFADYQTNG
     EIICKKCGQA WGTMMVHKGL DLPCLKIKNF VVVFKNNTPK KQYKKWVELP ITFPDLDYSQ
     YCLCSDED
//
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