ID A0A212EY30_DANPL Unreviewed; 779 AA.
AC A0A212EY30;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=KGM_205186 {ECO:0000313|EMBL:OWR46402.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR46402.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR46402.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR46402.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the helicase family.
CC {ECO:0000256|ARBA:ARBA00008708}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWR46402.1}.
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DR EMBL; AGBW02011630; OWR46402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212EY30; -.
DR STRING; 278856.A0A212EY30; -.
DR KEGG; dpl:KGM_205186; -.
DR eggNOG; KOG0953; Eukaryota.
DR InParanoid; A0A212EY30; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17913; DEXQc_Suv3; 1.
DR CDD; cd18805; SF2_C_suv3; 1.
DR Gene3D; 1.10.1740.140; -; 1.
DR Gene3D; 1.20.272.40; -; 1.
DR Gene3D; 1.20.58.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022192; SUV3_C.
DR InterPro; IPR041082; Suv3_C_1.
DR InterPro; IPR044774; Suv3_DEXQc.
DR InterPro; IPR041453; Suv3_N.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF1; ATP-DEPENDENT RNA HELICASE SUPV3L1, MITOCHONDRIAL; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12513; SUV3_C; 1.
DR Pfam; PF18147; Suv3_C_1; 1.
DR Pfam; PF18114; Suv3_N; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:OWR46402.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007151};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 357..535
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 747..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 88137 MW; 6FF205D590F44F3D CRC64;
MYKGFSRIWT VYSIERLQPF VSNLVFGVLN PQTERLSRIG YVFKRTKKHD KGPSSLFVPV
PVKPNPDDIN VGEEFTGRLK KQDLLKILNK FYQKPEVRVL ASENGLDDQI LHQAFLSFRR
HCLEHDLPPD LHITISDILV GAGNVNDLFP YFLRHARLAF PHLDCLDDLK KISDLRTPAN
WYPEARNINR KIIFHAGPTN SGKTYHAMEK FLAAKSGVYC GPLKLLATEI YHKSNSKGTP
CDLITGEERR HASQYKTLVD NVEDNKELDH EPFLLEEPVL TPSKHVACTV EMTSLNDTYD
VAIIDEIQML GDKGRGWAWT RAVLGLKADE IHLCGEAGAI SLVEEMCNTT GEELEVRTYK
RLTELKVENS ALGTLDNVKA GDCIVCFNKN DIYSVSRAIE QRGREVAVIY GSLPPGTKLA
QANKFNDPES SCKVMVATDA IGLGINLSIR RIIFYSLIKP VINVDGDKEM DVISISQALQ
IAGRAGRYGS AWETGYVTTF KSEDLATLKT LLSQPPDPVT QAGLHPTAEQ MELYAYHLPH
ASLSSLMDIF VHLCTVDATL YFMCNTEGFK FLAEMIQHVP LPLRARYVFC CAPINNKLPF
VCATFLKMVR QYSRNEPITR NWMSNVVDWP LPAPRTIMDL VHLEAVFDVL ELYLWLSYRF
PDMFPDVKLV REMEVELDAI IQQGIFQITR LLRNSEPVLE SETDMRDYGK GKKLHLHSRQ
DESKGKLSEM LVSKGLITPQ MLKKLQQELS TDKTEKRTKG RTAGRALPTA DLDQCVRNE
//
