ID   A7LCX1_PIG              Unreviewed;      1023 AA.
AC   A7LCX1;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=MDA5 {ECO:0000313|EMBL:ABS29718.1};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:ABS29718.1};
RN   [1] {ECO:0000313|EMBL:ABS29718.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang D., Xiao S.;
RT   "Identification and characterization of swine MDA-5.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:4I1S}
RP   X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 666-808.
RX   PubMed=23328395; DOI=10.1126/science.1230949;
RA   Motz C., Schuhmann K.M., Kirchhofer A., Moldt M., Witte G.,
RA   Conzelmann K.K., Hopfner K.P.;
RT   "Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to
RT   inhibit antiviral signaling.";
RL   Science 339:690-693(2013).
RN   [3] {ECO:0000313|EMBL:HDA80240.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
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   -!- INTERACTION:
CC       A7LCX1; P11207: P/V; Xeno; NbExp=2; IntAct=EBI-16032125, EBI-6148694;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
CC       {ECO:0000256|ARBA:ARBA00006866}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU006039; ABS29718.1; -; mRNA.
DR   EMBL; DQIR01124764; HDA80240.1; -; Transcribed_RNA.
DR   RefSeq; NP_001093664.1; NM_001100194.1.
DR   PDB; 4I1S; X-ray; 2.29 A; A=546-640, A=666-808.
DR   PDBsum; 4I1S; -.
DR   SMR; A7LCX1; -.
DR   DIP; DIP-61736N; -.
DR   IntAct; A7LCX1; 1.
DR   GeneID; 100101927; -.
DR   KEGG; ssc:100101927; -.
DR   CTD; 64135; -.
DR   OrthoDB; 342391at2759; -.
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; 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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4I1S};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:HDA80240.1};
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   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          315..508
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          704..874
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          890..1018
FT                   /note="RLR CTR"
FT                   /evidence="ECO:0000259|PROSITE:PS51789"
FT   REGION          270..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..657
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   BINDING         959
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
FT   BINDING         962
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01125"
SQ   SEQUENCE   1023 AA;  115917 MW;  C92B17D46B267222 CRC64;
     MSSDGYSADQ NFCYLISCFR ARVKRYIQVE PVLDYLTFLP AEVKEQIQRA VATTGNINAA
     ELLLNTLEKG VWPPGWTRMF VQALRETGNS LAARYVNPDL TDLPSPSFES SHDECLQLLN
     LLQPTVVDKL LVTDVLDKCV EEQLLTGEDR NRVSAAENDG NESGVRELLK RIVQKENWFS
     TFLTVLRQTG NDALARELTG TDCCESNAES DDLLGENGPE VQEPLLLATD QPSLDVSDIE
     KSSLESSFAD SSVVSESDTS LAEGSVSCLD ESLGHNSNMG SDSGTMGSDS DEETVAQRAS
     PEPELHLRPY QLEVAQPALE GKNIIICLPT GSGKTRVAVY IAKDHLDKKK EASEPGKVIV
     LVNKVPLVEQ LFRKEFEPFL KKWYRVTRLS GDTQLKITFP EVVKSCDVII STAQILENSL
     LNSEEGEDPG VQLSDFSLII IDECHHTNKE AVYNNIMRRY LKQKLKNNKL KKEEKPVIPL
     PQILGLTASP GVGGAKKQAK AEEHILKICA NLDAFTIKTV KKNINQLKDQ IKEPCKKFVI
     ADDTREDLFK DRLLEIMTNI QTFCQISPMS DFGTQPYEQW LIQMEKKAAR DGNRKDRVCA
     EHLKKYNEAL QINDTIRRID AYNHLKTFYN DEKEKKFEVL EDDSDDNGDD SDNDEDENDE
     KKPSKLDESD IFLMTLFLRN KKILKKLAEN PEYENEKLTK LRNTIMEHFT RTEESARGII
     FTKTRQSAYA LSQWITDNKK FAEVGVKAHH LIGAGHSSEF KPMTQNEQRE VISKFRTGKI
     NLLIATTVAE EGLDIKECNI VIRYGLVTNE IAMVQARGRA RADESTYVLV AQSGSGVIER
     ETVNDFREKM MYKAIDRVQN MKPEEYAHKI LELQMQSIME KKMKIKRSIA KQCKDNPSLI
     SFLCKNCSVL ACSGEDIHII EKMHHVNMTP EFKNLYIVRG NKALQTKFAD YQTNGEIICK
     KCGQAWGTMM VHKGLDLPCL KIKNYVVAFK NNLFKKQYKK WVELPITFPD LNYSEYCLSS
     DED
//