ID A0A3P9AEK1_ESOLU Unreviewed; 937 AA.
AC A0A3P9AEK1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
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};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000039488.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000039488.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000039488.2}
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; A0A3P9AEK1; -.
DR Ensembl; ENSELUT00000030842.2; ENSELUP00000039488.2; ENSELUG00000019690.2.
DR GeneTree; ENSGT00940000153173; -.
DR Proteomes; UP000265140; LG16.
DR Bgee; ENSELUG00000019690; Expressed in spleen and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd08819; CARD_MDA5_r2; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 248..441
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 613..782
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 798..925
FT /note="RLR CTR"
FT /evidence="ECO:0000259|PROSITE:PS51789"
SQ SEQUENCE 937 AA; 107054 MW; D81E3FC4D539014C CRC64;
LNLGFSFINL IKDFTPRLRK LIEVELVLDH LDFIGKEQKD LIRTKAKTQS NLKAVDLLIE
TIIYRQHPDG WFREFVDALS AGGCKHAAIY VDCPPSPSVE AENDYCVRLI ELLSPSLLRM
KTTEVCHACF AEEILSREDL EIVLAECQNK GNISGARELL KRIVRFPPGW FSTFLNVLKK
TEHLDLFKEL TGDTPDDFLI ELQQSVADVD NSSGVIFSPL QYFTDCTTVA EGPEKDDIVL
RDYQMAVAKP ALEGKNIIIC LPTGSGKTRV AVYITKEHLD NRRREGRQGK VVILVNKVPL
VEQHYSTEFW KFLKHKYKVE RVSGDSQLKI SFTEIVQKND IIICTAQILE NYLERAHSGD
DDGIKLSDLS LIVIDECHHT QKGGVYNNIM IRYLKQKHKN VKLKKDQKET VAIPQILGLT
ASPGVGGAKK MEKAEEHILR ICANLDAYKI MTGDLGENKK EPHKNIATAE ARKEDPFGDV
IKGIMNAIHT HAELNPTCDV GTQNYEQWVV QKEQNAAKEE NQKVRVCAEH LRQYNEALYQ
NNTIRMCDAF SFLEKYFDEE LKKKVAPEGE ETIIKTDTEK FLFTLFKDNK VKLQELAKNP
QYENNSLFKL RTKILQEFTS REKARGIIFT KTRRSAIALA QWVQENPKFQ EVGVKACHVI
GGGDQSVVKP MTAAEQRDVL NKFRIAEVNL LIATTVAEEG LDIAECNFVI RYCLVTNEIA
MIQARGRGRA EDSSYTLVAG EGSGVAERES VNEYREKMMS KAIEKVKKLN QEEYENRIKE
YQIQAIMEER VRTTKKKQKG LKKESPSKVK FSCRGCNKPV CSGEDIEIIE NMHRVNVKPQ
FREIFIQREN TTLAERLLDY DTNGFIACKD CGQRWGSLML YRSIECPCLD VKNLLVTYDE
KKKNIKKWNE LTIQFPAFDY AEYARNMAES SEDEESM
//
