ID A0A0A0A2I7_CHAVO Unreviewed; 1224 AA.
AC A0A0A0A2I7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, 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=N301_08669 {ECO:0000313|EMBL:KGL87235.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL87235.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL87235.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL87235.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR EMBL; KL870252; KGL87235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0A2I7; -.
DR STRING; 50402.A0A0A0A2I7; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
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 CDD; cd17983; DEXHc_DHX38; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KGL87235.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858}.
FT DOMAIN 540..703
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 725..900
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 49..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL87235.1"
FT NON_TER 1224
FT /evidence="ECO:0000313|EMBL:KGL87235.1"
SQ SEQUENCE 1224 AA; 140471 MW; 2D4C8481C632E36E CRC64;
LHRLAGTSPD AEAGGLVLRK RSAAAEQHVF KAPAPRASLL GLDLLAAQKR REREEEASGG
KRSRVSSYKD WEEGHDEAGS PEEEDEEEID RSSRSTRKDR HYRSVHVETP SYTGGVSEEF
WERSRQRERE RREHGVFASS KEEKERKKER SRDRDHDRKR DREERDRSRH SSRSERDGSS
ERSSRRSEPE SPRHRPKDAA TPSRSSWEED DSGYSSARRS QWESPSPTPS YRDSERSHRS
SSLRDTDRRD RDRSVRSRYS DKTPLPTPSY KYNEWADDRR HLGATPRLSR GRGRHADGEE
GIAFETEEER QQWEDDQRQA DRDWYMMDEG YDEFHNPLAY SSEEYVKKRE QHLHKQRQKR
ISAQRRQINE DNERWETNRM LTSGVVHRIE VDEDFEEDNS AKVHLLVHNL VPPFLDGRIV
FTKQPEPVIP VKDATSDLAI IARKGSQLVR KHREQKERKR AQHKHWELAG TKLGDIMGIK
KEEEKDEMVT EDGKVDYKTE QKFAEHMKEK SEASSEFAKK KSILEQRQYL PIFAVQQELL
SILRDNSIVI VVGETGSGKT TQLTQYLHED GYTDYGMIGC TQPRRVAAMS VAKRVSEEMG
VRLGEEVGYA IRFEDCTSEK TVIKYMTDGI LLRESLREAD LDNYSAIIMD EAHERSLNTD
VLFGLLREVV ARRSDLKLVV TSATMDADKF ASFFGNVPIF HIPGRTFPVD ILFSKTPQED
YVEAAVKQAL QVHLSGAPGD ILVFMPGQED IEVTSEQIVE HLEELEKAPA LAVLPIYSQL
PSDLQAKIFQ KAPDGVRKCI VATNIAETSL TVDGIMFVID SGYCKLKVFN PRIGMDALQI
YPISQANANQ RAGRAGRTGP GHCFRLYTQS AYKNELLTTT VPEIQRTNLA NVVLLLKSLG
VQDLLQFHFM DPPPEDNMLN SMYQLWILGA LDNTGIGRRG RLMVEFPLDP ALSKMLIVSC
DMGCSSEILL IVSMLSVPAI FYRPKGREEE SDQVREKFAV PESDHLTYLN VYLQWKNNSY
STLWCNQHFI HAKAMRKVRE VRAQLKDIMV QQRMSLASCG TDWDVVRKCI CAAYFHQAAK
LKGIGEYVNI RTGMPCHLHP TSSLFGMGYT PDYIVYHELV MTTKEYMQCV TAVDGEWLAE
LGPMFYSIKH AGRSRQENRR RAKEEVSAME EEMALAEEQL RARREEQERR NPLGSARSTK
IYTPGRKEQG EPLTPRRTPA RFGL
//
