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Database: UniProt
Entry: A0A384BRN9_URSMA
LinkDB: A0A384BRN9_URSMA
Original site: A0A384BRN9_URSMA 
ID   A0A384BRN9_URSMA        Unreviewed;      1017 AA.
AC   A0A384BRN9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, 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|RefSeq:XP_008685253.1};
OS   Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008685253.1};
RN   [1] {ECO:0000313|RefSeq:XP_008685253.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008685253.1};
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_008685253.1; XM_008687031.2.
DR   AlphaFoldDB; A0A384BRN9; -.
DR   STRING; 29073.ENSUMAP00000016375; -.
DR   GeneID; 103659509; -.
DR   KEGG; umr:103659509; -.
DR   CTD; 64135; -.
DR   OrthoDB; 342391at2759; -.
DR   Proteomes; UP000261680; Unplaced.
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   ECO:0000313|RefSeq:XP_008685253.1};
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:UP000261680};
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          309..502
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          698..873
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          884..1012
FT                   /note="RLR CTR"
FT                   /evidence="ECO:0000259|PROSITE:PS51789"
FT   REGION          271..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..651
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         898
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT   BINDING         901
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT   BINDING         953
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT   BINDING         956
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
SQ   SEQUENCE   1017 AA;  115698 MW;  F5C53045B7D32553 CRC64;
     MSNGYSADQS FCHLISCFRA RVKTYIQVEP VLDYLNFLPD DVKEQIQRTA VNAGNMQAAD
     QLLSALEKGG WPPGWARQFL VALQRAGSDL AARYLNPELT DLPSPSSETT HDECLQLLTL
     LQPTLVDRLL VRDILDRCME KKLLTNEDRS RISAAESNGN ESGVRELLRR IVQKENWFSE
     FLTVLRQTEN HALVQELTGT TCFESNAEPE NLSQRDGPDV QEAVLSATGQ PSPEREGWDE
     DCDSLESSLV DSSVVSESDT SLAEGSVSCL DESLGHNSNM GSDSDEENVA ERASPEPELH
     LRPYQMEVAQ PALEGKNIII CLPTGSGKTR VAVYIAKDHL DKKKKASEPG KVIVLVNKVP
     LVEQLFRKEF EPFLKKWYHT IGLSGDTQLK ISFPEVVKTY DVIISTAQIL ENSLLNSEKG
     EDDGVQFSDF SLIVIDECHH TNKEAVYNNI MRRYLKQKLK NNKLKKECKP VIPLPQILGL
     TASPGVGGAK KQAEAKEHIL KICANLDACT IKTVKENIVQ LKDQIKEPCK KFAIADDTRE
     DPFKDKLLEI MNKIQSFCQM SPMSDFGTQP YEQWTTQMEK KAAREGNRKE RVCAEHLRKY
     NEALQINDTI RTIDAYNHLE AFYNDEKEKK FAVLEDDSDE SGEDGDGDED EDDVKKPLSL
     DRTDRFLMDL FFENRRMLKK LAENPKHENE KLIKLRNTIM EQYTRTEESA RGIIFTKTRQ
     SAYALSQWIT ENKKFAEVGV KAHHLIGAGH SSEFKPMTQN EQKEVISKFR TGKINLLIAT
     TVAEEGLDIK ECNIVIRYGL VTNEIAMVQA RGRARADEST YVLVAHSNSG VIEREIVNDF
     REKMMYKAID HVQNMNPEEY ARKILELQMQ SIMEKKMKIK RSIAKHYKEN PSLINFLCKN
     CSVLACSGED IHVIEKMHHV NMTPVFKELY IVRENKALRK KFADYQTNGE IICKKCGQAW
     GTMMVHKGLD LPCLKIKNFV VVFKNNTPKK QYKKWVELPI TFPDLDYSQY CLCSDED
//
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