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Database: UniProt
Entry: A0A1V4JS84_PATFA
LinkDB: A0A1V4JS84_PATFA
Original site: A0A1V4JS84_PATFA 
ID   A0A1V4JS84_PATFA        Unreviewed;       597 AA.
AC   A0A1V4JS84;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   Name=DDX55 {ECO:0000313|EMBL:OPJ75086.1};
GN   ORFNames=AV530_018541 {ECO:0000313|EMBL:OPJ75086.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ75086.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ75086.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ75086.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ75086.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000256|ARBA:ARBA00038002}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ75086.1}.
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DR   EMBL; LSYS01006629; OPJ75086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4JS84; -.
DR   STRING; 372326.A0A1V4JS84; -.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17960; DEADc_DDX55; 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; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR24031:SF2; ATP-DEPENDENT RNA HELICASE DDX55; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
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, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          9..37
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          40..223
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          254..411
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          485..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           9..37
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        485..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..535
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  67742 MW;  674395B8311798A7 CRC64;
     MEAVTEGSWE SLPVALSPGV LRALRELGFA RMTPVQSATI PLFMNNKDVA AEAVTGSGKT
     LAFVIPILEI LLRREEKLKK MQVGAIIITP TRELAIQIDE VLSHFTKHFP RFSQILLIGG
     RNPMEDVEKF KEHGGNIIVA TPGRLEDLFR RKADGLDLAS CVKSLDVLVL DEADRLLDMG
     FEASLNTILD FLPKQRRTGL FSATQTQEVE NLVRAGLRNP VRISVKEKGV AASNAQKTPT
     RLENYYMICK ADEKFNQLVH FLRQHKQEKH LVFFSTCACV EYYGKALESL IKQVKIMSIH
     GKMKHKRNKI FTEFRKLPGG ILVCTDVMAR GIDIPEVHWV LQYDPPSSAS AFVHRCGRTA
     RIGNVGSALV FLLPMEESYV NFLSINQKCP MQEMKPQTNV SDLLPKLKAM ALADRAVFEK
     GMKAFVSYVQ AYAKHECNLI FRIKDLDFAS LAKGFALLKM PKMPELRGKC FPDFTPVTVN
     TDSISFKDKN REKQRQKQLE QQRKEREENG GKKKFVKNKA WSKQKAKREK KKKITAKRKR
     EEGSDIDDED MEELLNDTRL LKRLKKGKIS EEEFEKRLTG NPSRLKAETV ADLESEG
//
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