ID A0A3B4EZU8_9CICH Unreviewed; 975 AA.
AC A0A3B4EZU8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=ifih1 {ECO:0000313|RefSeq:XP_005723472.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000003882.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000003882.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005723472.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_005723472.1; XM_005723415.1.
DR AlphaFoldDB; A0A3B4EZU8; -.
DR Ensembl; ENSPNYT00000003981.1; ENSPNYP00000003882.1; ENSPNYG00000002971.1.
DR GeneID; 102194000; -.
DR CTD; 64135; -.
DR GeneTree; ENSGT00940000153173; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
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 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; 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 ECO:0000313|RefSeq:XP_005723472.1};
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000695023};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 283..476
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 641..809
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 833..961
FT /note="RLR CTR"
FT /evidence="ECO:0000259|PROSITE:PS51789"
FT REGION 194..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 111093 MW; 0A1D41FFD3F1CA22 CRC64;
MESETDEMRE CLIDCLRPRL KELIVVDRVL DLIGFIDNEQ KERIRQKARN DGDISAADYL
INTVVQKPHT PGWFTAFVDA LNNGGCKFAA DYMQLNLPTP EAEAENENCV RFIHLLIPSL
ADMVTEEVCG ECFSKRLLTE DERDRITAEI VNRGSRSGAR ELLRRIIKCP PGWYSTFLQV
LKDTEHHVLY NELTGNEGSD KKPSLKDKPI ATRESPTSAE SCDGTESMEI TVNEQPMDQS
TDLYAGNELP SNSEPSQPDG SALEVARSPE KEITLRDYQM EVAGPALEGK NIIVCLPTGS
GKTRVAVYIT KEHLDRRKAE GKPRKVIVLV NKVPLVEQHY SAEFLPFLKN KYKVERVSGD
SQLKISFTEI VKKNDIIICT AQILENYLER ANSGEDEGVN LSDLTLIIID ECHHTQKGGV
YNHIMMRYLK QKHKNKRLVK EQKEPVPLPQ ILGLTASPGV GGATKMEKAE EHILRICANL
DASRIMTRRQ EEFKKEQRKI VVSVEDRRED PFGDVIKKIM TAIHNHAELT PTCDLGSQNY
EQWVVQKERQ AAKDENQKVR VCAEHLRQYS ESLNLCNTIR MQDAFSFLNK YYEEEMKKKT
APEEEHKIQI TDTERFLFNL FKDNKKELES LAKNPEYEND SLSKLRTKIL HEFSSRDEAR
GIVFIKTRRS AIALNQWIQE NSKFADIGVK SAYVIGGGDQ SVVKPMTSAE QKDVLKKFGN
GQVNLLIATT VAEEGLDIPA CNFVIRYGLV TNEIAMIQAQ GRGRAEDSSY TLVEVKNSGV
AEKECVNEYR KNMMNKAIQK IKSLNQAAYE KRITEFQLQA IMEEKVRMTK KKQKDIKNES
PSNVKFSCRS CSEPICTGDD IQIIENMHRV NVTPQFRKLY IQRENTTLQE RLLDYETNGF
IACKNCGQRW GSMMMYKGIE CPCLDVKNFV VNLNGKKISK CTKWNEVPIK FSAFDYAEHA
INMTMSDNSD DDETM
//
