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Database: UniProt
Entry: A0A093ILY4_FULGA
LinkDB: A0A093ILY4_FULGA
Original site: A0A093ILY4_FULGA 
ID   A0A093ILY4_FULGA        Unreviewed;       544 AA.
AC   A0A093ILY4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=N327_07710 {ECO:0000313|EMBL:KFV99773.1};
OS   Fulmarus glacialis (Northern fulmar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC   Fulmarus.
OX   NCBI_TaxID=30455 {ECO:0000313|EMBL:KFV99773.1, ECO:0000313|Proteomes:UP000053806};
RN   [1] {ECO:0000313|EMBL:KFV99773.1, ECO:0000313|Proteomes:UP000053806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N327 {ECO:0000313|EMBL:KFV99773.1};
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; KK590497; KFV99773.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093ILY4; -.
DR   Proteomes; UP000053806; 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:UP000053806};
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..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV99773.1"
FT   NON_TER         544
FT                   /evidence="ECO:0000313|EMBL:KFV99773.1"
SQ   SEQUENCE   544 AA;  61546 MW;  2CBA05153135784E CRC64;
     TKKAKTEEDG SVEVEDEDKQ DSGEKEVEEE EGEEEEVPSL PRGVTGAFED NSFTSLAGVV
     SENTLKGIND MGFTHMTEIQ HKSIKPLLEG RDILAAAKTG SGKTLAFLIP AVELIYKLKF
     MPRNGTGVII LSPTRELAMQ TYGVLKELMN HHVHTYGLIM GGSNRSAEAQ KLGNGINVIV
     ATPGRLLDHM QNTPGFMYKN LQCLVIDEAD RILEVGFEEE MKQIIKLLPK RRQTMLFSAT
     QTRKVEDLAK ISLKKEPLYV 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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