ID A0A091UWG3_PHALP Unreviewed; 1177 AA.
AC A0A091UWG3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE Flags: Fragment;
GN ORFNames=N335_10388 {ECO:0000313|EMBL:KFQ81978.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ81978.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ81978.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ81978.1};
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. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK466251; KFQ81978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UWG3; -.
DR PhylomeDB; A0A091UWG3; -.
DR Proteomes; UP000053638; 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; IPR048333; HA2_WH.
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; PF04408; HA2_N; 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:KFQ81978.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053638}.
FT DOMAIN 483..646
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 668..843
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ81978.1"
FT NON_TER 1177
FT /evidence="ECO:0000313|EMBL:KFQ81978.1"
SQ SEQUENCE 1177 AA; 135314 MW; 35A4DD0EBC9EDD41 CRC64;
GGKRSRVSSY KDWEEGRDEA GSPEEDEEEE EETDRSSRTR KDRHYRSVHV ETPSYTGGVS
EEFWERSRQR ERERREHGVF ASSKEEKERK KERSRDRDHD RKRDREERDR GRHSSRSERD
GSSERSSRKS EPESPRHRPK DAATPSRSSW EEDDSGYSSA RRSQWESPSP MPSCRDSERS
HRASSLRDTD RRDRDRSVRS RYSDKTPLPT PSYKYNEWAD DRRHLGATPR LSRGRGRRAD
GEEGIAFETE EERQQWEDDQ RQADRDWYMM DEGYDEFHNP LAYSSEEYVK KREQHLHKQR
QKRISAQRRQ INEDNERWET NRMLTSGVVH RIEVDEDFEE DNSAKVHLLV HNLVPPFLDG
RIVFTKQPEP VIPVKDATSD LAIIARKGSQ LVRKHREQKE RKRAQHKHWE LAGTKLGDIM
GIKKEEEKDE MVTEDGKVDY RTEQKFAEHM KEKSEASSEF AKKKSILEQR QYLPIFAVQQ
ELLSILRDNS IVIVVGETGS GKTTQLTQYL HEDGYTDYGM IGCTQPRRVA AMSVAKRVSE
EMGVRLGEEV GYAIRFEDCT SENTVIKYMT DGILLRESLR EADLDNYSAI IMDEAHERSL
NTDVLFGLLR EVVARRSDLK LVVTSATMDA DKFASFFGNV PIFHIPGRTF PVDILFSKTP
QEDYVEAAVK QALQVHLSGA PGDILIFMPG QEDIEVTSEQ IVEHLEELEK APALAVLPIY
SQLPSDLQAK IFQKAPDGVR KCIVATNIAE TSLTVDGIMF VIDSGYCKLK VFNPRIGMDA
LQIYPISQAN ANQRAGRAGR TGPGHCFRLY TQSAYKNELL TTTVPEIQRT NLANVVLLLK
SLGVQDLLQF HFMDPPPEDN MLNSMYQLWI LGALDNTGGL TSTGRLMVEF PLDPALSKML
IVSCDMGCSS EILLIVSMLS VPAIFYRPKG REEESDQVRE KFAVPESDHL TYLNVYLQWK
NNSYSTLWCN QHFIHAKAMR KVREVRAQLK DIMVQQRMSL ASCGTDWDVV RKCICAAYFH
QAAKLKGIGE YVNIRTGMPC HLHPTSSLFG MGYTPDYIVY HELVMTTKEY MQCVTAVDGE
WLAELGPMFY SIKHAGKSRQ ENRRRAKEEV SAMEEEMALA EEQLRARREE QERRNPLGSA
RQVLALPGHR STKIYTPGRK EQGEPLTPRR TPARFGL
//
