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Database: UniProt
Entry: A0A091N0M8_APAVI
LinkDB: A0A091N0M8_APAVI
Original site: A0A091N0M8_APAVI 
ID   A0A091N0M8_APAVI        Unreviewed;       455 AA.
AC   A0A091N0M8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   Flags: Fragment;
GN   ORFNames=N311_06795 {ECO:0000313|EMBL:KFP83026.1};
OS   Apaloderma vittatum (Bar-tailed trogon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX   NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP83026.1, ECO:0000313|Proteomes:UP000054244};
RN   [1] {ECO:0000313|EMBL:KFP83026.1, ECO:0000313|Proteomes:UP000054244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP83026.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:ARBA00001556};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX41 subfamily.
CC       {ECO:0000256|ARBA:ARBA00023594}.
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DR   EMBL; KL374780; KFP83026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091N0M8; -.
DR   Proteomes; UP000054244; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   CDD; cd17951; DEADc_DDX41; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR044113; DEADc_DDX41.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF103; ATP-DEPENDENT RNA HELICASE DDX41-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 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; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KFP83026.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        196..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          118..146
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          149..335
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          346..455
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           118..146
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        27..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP83026.1"
FT   NON_TER         455
FT                   /evidence="ECO:0000313|EMBL:KFP83026.1"
SQ   SEQUENCE   455 AA;  50744 MW;  E41249DE0AD2FBAF CRC64;
     RDSGSEQRGD EDDIPLGPQS NISLLDQHQH LKEKAEARKE SAKEKQLKEE EKILESVAEG
     RALMSVKEMA KGITYDDPIK TSWRAPRYIL GMSEARHDRV RKKYHILVEG EGIPPPIKSF
     KEMKFPAAIL RGLKKKGIQQ PTPIQIQGIP TILSGRDMIG IAFTGSGKTL VFTLPVIMFC
     LEQEKRLPFS KREGPYGLII CPSVTSFVSA AGAGSFFFYC RLLQEDGLPP LRCALCIGGM
     SVKEQMETIK HGVHMMVATP GRLMDLLQKK MVSLDICRYL ALDEADRMID MGFEGDIRTI
     FSYFKGQRQT LLFSATMPKK IQNFAKSALV KPITINVGRA GAASLDVVQE VEYVKEEAKM
     VYLLECLQKT PPPVLIFAEK KADVDAIHEY LLLKGVEAVA IHGGKDQEER TKAIEAFRDG
     KKDVLVATDV ASKGLDFPAI QHVINYDMPG EIENY
//
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