ID W5MPI9_LEPOC Unreviewed; 1015 AA.
AC W5MPI9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010298.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000010298.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AHAT01020068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006636679.1; XM_006636616.2.
DR AlphaFoldDB; W5MPI9; -.
DR STRING; 7918.ENSLOCP00000010298; -.
DR Ensembl; ENSLOCT00000010311.1; ENSLOCP00000010298.1; ENSLOCG00000008460.1.
DR GeneID; 102693765; -.
DR KEGG; loc:102693765; -.
DR CTD; 64135; -.
DR eggNOG; KOG0354; Eukaryota.
DR GeneTree; ENSGT00940000153173; -.
DR InParanoid; W5MPI9; -.
DR OMA; TFCQMNP; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000018468; Linkage group LG12.
DR Bgee; ENSLOCG00000008460; Expressed in mesonephros and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0140374; P:antiviral innate immune response; IBA:GO_Central.
DR GO; GO:0039530; P:MDA-5 signaling pathway; IBA:GO_Central.
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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR011029; DEATH-like_dom_sf.
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; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 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};
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 321..514
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 687..863
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 879..1006
FT /note="RLR CTR"
FT /evidence="ECO:0000259|PROSITE:PS51789"
FT REGION 205..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 115644 MW; EB60CFC4745D8F04 CRC64;
MTSSMPDETW FWLIDDCFRN RIRRLIQVEP VLDHISFIER EQKEMIIEKA KNAGNIRAAD
LLLDTIINRK PRPVGWYREF VNALRLGGCK HAAVYVDPDE LPAPSLEAEN DHCIHLIELL
VPNLVDKMKT TDVSLCCYTL DILTTEDKEN ILTECANNGN RSGARLLLRR IIQKPPGWFS
NFLKALEKTG HKDLAQELTG VPLEEPSQED ITDEGNESGV LRDHLSENKD GEENSSISHE
NEETLNSSVD SVDRCLDESI DDASIHSVSD LYSDGPEGEK QEELTVNGNS LQSNDFSESD
SSAGGFQEAE IVLRDYQMEV AKPALEGKNI IICLPTGSGK TRVAVYITKQ HLDKRRIQKH
PGKAIVLVNK VPLVEQHYRT EFGKHLKSQY KVERVSGDSQ LKISFSDIVK NNDIIICTAQ
ILENSFSQAK NEEDEGVRMS DISLIVIDEC HHTQKGGVYN NIMTRYLKQK MKNEELRKEN
KEPVPIPQIL GLTASPGVGG AKNSQKAEEH ILKICANLDA YKIMTVQINA GELGEKVKEP
YKKIAIAEER KEDPFGDLIK RIMQDIHEHS NLKPSSDPGT QNYEQWVVQK EQKAAKEENQ
KVRVCAEHLR KYNEALNQNN TIRMSDAFNF LKKFYDEEIR NKIRPDEENS TMFAETSETD
KYLFKLFQDN QQTLQDLAKN PAYENKNLAQ LKTTILEEFT KPEEARGIIF TKTRLSAIAL
NQWIQENKKF EEAGVKSSHL IGAGHQSIIK PMTAAEQREV LDKFRHGEIN LLVATTVAEE
GLDIKECNIV IRYGLVTNEI AMVQARGRAR ADDSTYALVA SEGSGVVERE GVNVFREKMM
KKAIEKVQRL IRKDYEKKIK GFQIQAIMEK RVRTKKKKQR VLQEDPSKVK FSCRNCSQLI
CSGENIEVIE NSHHVNVTKE FKELFLVREN KALQERFLDY EVNGEIACRK CAQAWGTMMV
HRGIECPCLG IKNFVVSFED KQKKTFSKWS ELAIKFPSFD YTDHVFLDVD DSDDD
//
