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Database: UniProt
Entry: A0A093P4X2_PYGAD
LinkDB: A0A093P4X2_PYGAD
Original site: A0A093P4X2_PYGAD 
ID   A0A093P4X2_PYGAD        Unreviewed;       544 AA.
AC   A0A093P4X2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
DE   Flags: Fragment;
GN   ORFNames=AS28_05477 {ECO:0000313|EMBL:KFW69260.1};
OS   Pygoscelis adeliae (Adelie penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX   NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW69260.1, ECO:0000313|Proteomes:UP000054081};
RN   [1] {ECO:0000313|EMBL:KFW69260.1, ECO:0000313|Proteomes:UP000054081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW69260.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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|ARBA:ARBA00001556,
CC         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. DDX18/HAS1
CC       subfamily. {ECO:0000256|ARBA:ARBA00024357}.
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DR   EMBL; KL225231; KFW69260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093P4X2; -.
DR   STRING; 9238.A0A093P4X2; -.
DR   Proteomes; UP000054081; 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; cd17942; DEADc_DDX18; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR044773; DDX18/Has1_DEADc.
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   PANTHER; PTHR24031:SF301; ATP-DEPENDENT RNA HELICASE DDX18; 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.
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:UP000054081};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          84..259
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          273..443
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..37
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW69260.1"
FT   NON_TER         544
FT                   /evidence="ECO:0000313|EMBL:KFW69260.1"
SQ   SEQUENCE   544 AA;  61503 MW;  A001F90E10F2D308 CRC64;
     TKKAKTEEDE SVEVEDEDKQ DSGEKEVEEE EGEEDEVPSL PLGVTGAFED NSFTSLAGVV
     SENTLKGIND MGFTHMTEIQ HKSIKPLLEG RDILAAAKTG SGKTLAFLIP AVELIYKLKF
     MPRNGTGVII LSPTRELAMQ TYGVLKELMN HHVHTYGLIM GGSNRSAEAQ KLGNGINIIV
     ATPGRLLDHM QNTPGFMYKN LQCLVIDEAD RILEVGFEEE MKQIIKLLPK RRQTMLFSAT
     QTRKVDDLAK ISLKKAPLYV GVDDNKETAT VDGLEQGYVV CPSEKRFLLL FTFLKKNRKK
     KLMVFFSSCM SVKYHYELLN YIDLPVLAIH GKQKQTKRTT TFFQFCNAES GILLCTDVAA
     RGLDIPEVDW IVQYDPPDDP KEYIHRVGRT ARGINGRGHA LLILRPEELG FLRYLKQARV
     PLSEFEFSWS KISDIQSQLE KLIEKNYFLH KSAQEAYKAY IRAYDSHSLK QIYNVNNLDL
     PKVSLSFGFK VPPFVDLNVN SNHGRRLQKR GGGGGFGYQK SKNVHKAKIF KHISKKSDSR
     QFSR
//
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