ID W5MPL9_LEPOC Unreviewed; 851 AA.
AC W5MPL9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010328.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000010328.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. DDX54/DBP10
CC subfamily. {ECO:0000256|ARBA:ARBA00010379}.
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DR EMBL; AHAT01005287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01005288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015221580.1; XM_015366094.1.
DR AlphaFoldDB; W5MPL9; -.
DR STRING; 7918.ENSLOCP00000010328; -.
DR Ensembl; ENSLOCT00000010341.1; ENSLOCP00000010328.1; ENSLOCG00000008485.1.
DR GeneID; 102686496; -.
DR KEGG; loc:102686496; -.
DR CTD; 79039; -.
DR eggNOG; KOG0337; Eukaryota.
DR GeneTree; ENSGT00550000075100; -.
DR HOGENOM; CLU_003041_5_2_1; -.
DR InParanoid; W5MPL9; -.
DR OMA; EDQFGMM; -.
DR OrthoDB; 5475716at2759; -.
DR Proteomes; UP000018468; Linkage group LG20.
DR Bgee; ENSLOCG00000008485; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd17959; DEADc_DDX54; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10_DEAD-box_helicase.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF8; RNA HELICASE; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 81..109
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 112..284
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 311..461
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..109
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 707..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 94874 MW; 2FF880880DA48D65 CRC64;
MAQRKKRFTR KKRHAAHREP DADSDGGDFE LAAEASCDDT ATKKVGKKLP RFPAPSDCLS
DVEPDTRELV RAQNKKKKKS GGFQSMGLSY PVFKGVMKKG YKVPTPIQRK TIPLILEGRD
VVAMARTGSG KTAAFLIPLF ERLKAPQAQT GARALILSPT RELALQTLKF TKELGKFTGL
KTALILGGDR MDDQFAALHE NPDIIIGTPG RLMHVAVEMN LKLRGVEYVV FDEADRLFEM
GFAEQLQEII RRLPEARQTL LFSATLPKLL VEFARAGLTE PVLIRLDVDT KLSDQLKLAF
FQLRQDDKPA LLLHLLRSVV KPQEQTVVFA ATKHHVEYLK EVLSSEGVDC SYIYSALDQT
ARKINIGRFV HRKCMVMLVT DVAARGIDIP LLDNVINYNF PSKAKLFLHR VGRVARAGRT
GTAYSLVCPD EVPFMFDLHL FLGRPLQFAT AGLPQDVDGV FGRVPQSVLD DEEALLIAAH
QNSQDLQNLR RVAENAYKQY LRSRPSPSAE SIKRAKGVDL SSLAVHPLLG SALGGEELDR
LKMVDGVKNY KSKATIFEIN SSSRTAASEV MRAKRRRDAG QVGSFLRARE DKAAEGPASQ
PAAGAALQAE SDEEHIQGVF SAVLGGKRKM TQGEAEAPKK KKKRETFCDQ EFYIPYRPKD
FDSERGLSLV GEGSTFEQQA SGAVLDLMGD EGDKMSQHKN MLKWDRKKKR FVRETGKEDQ
KKKVRTESGQ LISSSYKKNL YEQWKKKYKM EDGASDSEGE GGGSGARRAS TGRKGGRGPQ
PQKHSPGPRP RSELKSRDQI LKQRKKREKQ QFLQSGGLKK LRRKNRQHVG EVARSGFGRG
TSRKGKLRKR L
//
