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Database: UniProt
Entry: K7G5C6_PELSI
LinkDB: K7G5C6_PELSI
Original site: K7G5C6_PELSI 
ID   K7G5C6_PELSI            Unreviewed;       928 AA.
AC   K7G5C6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=RIGI {ECO:0000313|Ensembl:ENSPSIP00000015487.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000015487.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000015487.1}
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; AGCU01087092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01087093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01087094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006123152.1; XM_006123090.2.
DR   AlphaFoldDB; K7G5C6; -.
DR   STRING; 13735.ENSPSIP00000015487; -.
DR   Ensembl; ENSPSIT00000015560.1; ENSPSIP00000015487.1; ENSPSIG00000013490.1.
DR   GeneID; 102452744; -.
DR   KEGG; pss:102452744; -.
DR   CTD; 23586; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   GeneTree; ENSGT00940000153173; -.
DR   OMA; FFANHVP; -.
DR   OrthoDB; 342391at2759; -.
DR   TreeFam; TF330258; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0038187; F:pattern recognition receptor activity; IEA:Ensembl.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR   GO; GO:0071360; P:cellular response to exogenous dsRNA; IEA:Ensembl.
DR   GO; GO:0009597; P:detection of virus; IEA:Ensembl.
DR   GO; GO:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
DR   GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IEA:Ensembl.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR   GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0039529; P:RIG-I signaling pathway; IEA:Ensembl.
DR   CDD; cd08816; CARD_RIG-I_r1; 1.
DR   CDD; cd08817; CARD_RIG-I_r2; 1.
DR   CDD; cd15805; RIG-I_C; 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; IPR042145; CARD_RIG-I_r2.
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:SF16; ANTIVIRAL INNATE IMMUNE RESPONSE RECEPTOR RIG-I; 1.
DR   PANTHER; PTHR14074; HELICASE WITH DEATH DOMAIN-RELATED; 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:UP000007267};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          250..429
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          608..774
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          795..925
FT                   /note="RLR CTR"
FT                   /evidence="ECO:0000259|PROSITE:PS51789"
SQ   SEQUENCE   928 AA;  106593 MW;  C9AA2CFEF4851509 CRC64;
     MTAEQKANLQ CYRQYIEKTL NPAYVVGNMK EWLPDDVSER IQIEQKGLTA AAQFFVDSLL
     QLESEGWFRG FLDALHEAGY TGLREAIENW DFQKLENLEI HRQLLKRIEA TLRKIDTDQI
     IPLVYTCLID RECQEIKQVK EHKGPMAGAV KLIECLCRSD KENWPKTFHL ALDRAGYDEA
     SKLWNMKEGN DTDMDVEMMD EQNRTLDINV QYSEEAEVHN FSERPCSPSE VSEQPTYEPK
     KARSYQIELA QPAISGKNTI ICAPTGSGKT FVSLLICDNH LRNLSQDQKG KIVFLATKVP
     VYEQQKKVFT QHFERTRYKV AGISGETAGD VSSARVIEGN DIIVLTPQIL VNSLKDGTIP
     SLAIFTLIIF DECHNTTGNH PYNVLMTSYL NLKYDSAAKQ LPQIVGLTAS VGVGSAKTTE
     ETIEYICTLC ACLDIQVIST VRENTDELEK IVYKPKKSIR HVGNRPKNRF MDIISVLMSE
     TEALARKVYP IDALSHIKTK SFGTQCYEQW IVDTQKKCRM LQLPDKEEES RICRALFIYT
     EHLRKYNDTL IINEDARTCD ALVYLTEFFN DIRSGGFDET DQQLTANFEA KQQELKAASE
     DELSENPKLE ELTFILDEEY RLNPETRTIL FVKTRALVAA LKKWIDENPA LSYLKPDTLM
     GRSKRNEQTG MTLSNQKGVL DSFRSNGDSK ILIATAVADE GIDIAQCNLV LLYEYSGNVT
     KMIQVRGRGR AKDSKCILVT SKSEVVENER NNIYREEMMN QAIEQLQEWD EDRFARKISN
     LQNKEKAMRD CRKREKKQKP LGGNRELLCG KCKTYVCNTE DIRVIAESHH TVVDAQFKER
     FITKPHKRPK RYGQFEKKCK MHCQDAKCQH DWGITVKYME FDDCPVIKIE SFVVRDITTG
     KLSNFRRWKD VDFAMKEFDT NEMLVILC
//
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