ID A0A091CWA4_FUKDA Unreviewed; 1026 AA.
AC A0A091CWA4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=H920_16139 {ECO:0000313|EMBL:KFO22443.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO22443.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO22443.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO22443.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KN124048; KFO22443.1; -; Genomic_DNA.
DR RefSeq; XP_010605150.1; XM_010606848.1.
DR AlphaFoldDB; A0A091CWA4; -.
DR STRING; 885580.ENSFDAP00000003758; -.
DR Ensembl; ENSFDAT00000017387; ENSFDAP00000003758; ENSFDAG00000013122.
DR GeneID; 104850088; -.
DR CTD; 64135; -.
DR eggNOG; KOG0354; Eukaryota.
DR OMA; TFCQMNP; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000028990; 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 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:KFO22443.1};
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:UP000028990};
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 317..510
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 708..883
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 894..1021
FT /note="RLR CTR"
FT /evidence="ECO:0000259|PROSITE:PS51789"
FT REGION 198..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 963
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT BINDING 965
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
SQ SEQUENCE 1026 AA; 116651 MW; 9251BA481C69DAC9 CRC64;
MSNGYSADKC FCHLLSCFRT RLKMYIQVEP VLDYLTFLPI DLKEQIVKTA DTSGNMKAVE
LLLSTLEQER DWGPGWTREF VDALERAGSP LAARYVNPNL TDLPSPSFEA AQDECVQLLT
LLQPTLVDRL LVRDVLDKCM EKELLTIEDR NRISAAENNG NESGVRELLK RIIQKENWFS
TFLHILHQTG NSALAQELTG SDHSKSNAGV ENLSHEDGPE VNESLLSATD QSDLDKEDWN
IKNNLSETSY ADSSVVSESD TSLAEGSVSC LDESLGHNSN MGSDSGTMGS DSDEPTVAKR
ASPEPELKLR SYQMEVAQPA LEGKNVIICL PTGSGKTRVA VYITKDHLFK KRQASEPGKV
IVLVNKVMLV GQIFHKEFKP FLKKWYHITG LSGDTQLKIS FPEVVRSHDV IISTAQILEN
SLLNSKSGED SGVQLSDFSL VIIDECHHTN KEAVYNNIMR RYVKQKLKNK RLQKENKPVI
PLPQILGLTA SPGVGGATTQ AKAEEHILKI CANLDACTIK TVKEYYDQLK DQIKEPCRKF
VIADDTREDL FKDKLLEIMS SIQTYCQVSS MSDFGTQNYE QWAIQMEKKA AREGNRKARV
CAEHLRKYNE ALQINDTIRV IDAYNHLETF YHDENVKKFA VLEDDSDVNS SDDDCDGDGD
RTALKRLEKQ DETDRFLVTL FSENKKMLKN LADNPEYENE KLTKLRNTIL EHYTRTEKPA
HGIIFTKTRQ SAHALSQWIT ENGKFAEVGV KAHHLIGAGH SSEFKAMTQN EQKEVISKFR
TGKINLLIAT TVAEEGLDIK ECNIIIRYGL VTNEIAMVQA RGRARAEEST YILVAPSDSG
VVEREIVNDF REKMMYKAIH HVQNMNPEDY TQKILELQMQ SIMEQQMKIR RNIAKHFKDN
PSSITFLCKN CHVLACSGED IHVIERMHHV NMTKEFQQLY IVRENKALKN KFSDYQTNRE
IICKCGQAWG TMMVHKGLDF PCLKIRNFVV VFKDNLPKKQ YKKWVELPIT FPELDYSEYY
NFSDED
//
