ID A0A3L8S4B9_CHLGU Unreviewed; 1002 AA.
AC A0A3L8S4B9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=DV515_00012234 {ECO:0000313|EMBL:RLV96980.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV96980.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV96980.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV96980.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV96980.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005601}.
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:RLV96980.1}.
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DR EMBL; QUSF01000065; RLV96980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8S4B9; -.
DR STRING; 44316.ENSEGOP00005020833; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR CDD; cd18038; DEXXQc_Helz-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR049080; MOV-10-like_beta-barrel.
DR InterPro; IPR026122; MOV-10/SDE3_DEXXQ/H-box.
DR InterPro; IPR049079; Mov-10_helical.
DR InterPro; IPR049077; MOV-10_Ig-like.
DR InterPro; IPR049075; MOV-10_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF537; HELICASE MOV-10; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF21634; MOV-10_beta-barrel; 1.
DR Pfam; PF21635; Mov-10_helical; 1.
DR Pfam; PF21633; MOV-10_Ig-like; 1.
DR Pfam; PF21632; MOV-10_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT DOMAIN 12..75
FT /note="Helicase MOV-10 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21632"
FT DOMAIN 121..242
FT /note="Helicase MOV-10 Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21633"
FT DOMAIN 294..355
FT /note="Helicase MOV-10 helical"
FT /evidence="ECO:0000259|Pfam:PF21635"
FT DOMAIN 356..440
FT /note="Helicase MOV-10-like beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF21634"
FT DOMAIN 492..568
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 604..686
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 695..954
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 92..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 112540 MW; 3BFAF9139344C3E9 CRC64;
MPRFSVAETS LWGHQFVQFL QDTGRQQTSL RETLRTIYNQ EFRGRTDAKT PNFSCILYAL
KIAQQVQVRG EVVKFKVERH VVVADQYRRT RRNAQTSVST SASGQQLSST PQMPQSHGKQ
WAKRIRGKHG VEIISDCDQG NGNIRFPVVP GEPRTVTVLV QNCGTEVVTL QRFQLHQQSR
ELSFTDEQGA VQGQSLLLHP GGMYPIQVRC LTACNGHFSA LVVFEFTKEP GERFSISRYV
AAIAESQLAK DLGPSAPFQP YEASLQHHVT VITEDGIPPD SSLRNQLERE IPVGTYQYPK
SLKDAILLGP NSSASSSWAA MRSLLEAPLQ AENYQQKFQL LLHLEEIQME VDIRRYDMQD
VTMVQERALL VLHVPGVAEN RPSLLRGDHL FAHLSSERDH SPLVQYKGYV HSVELEKVRL
GFSSKLQKKF VKNLKFDVTF TFNRLPLQVQ HRAAVLAVHR GLFSLLFPSA SCHKSLFPGP
FQPRWFNRKL ETNEEQCRAV THIVTGVSRP APYLIFGPPG TGKTVTMVEA IKQVWTCFKD
ARILACAPSN SAADLLCQCL IKDIAPRNVY RLIASSRSYR EVPADIMPCC NWDDEQSSYV
YPSKESLRHY RIIITTLVTA GRLVSANFPP GFFSHVFIDE CGHAVEPESV VAIAGLLAPM
DEETNPNGGQ LVLAGDPKQL GPVLTSPLAL QYGLGTSLLE RLMLHNPLYK KSGGGYDPQF
ITKLLWNYRS HEAILRIPNE LFYDNELKVC KSDGLDIRNV YCTWEELPKK GFPIIFHGVC
GEDQREAKSP SFFNTAEIEV LVDYLKKLLQ RQGKGGCPTV SPKEIGIISP YRKQVEKIRK
AITSLDPDLQ KLPDISQLKV RPEHGGERSK GGRSPDSPSP GVLLAPDLLS LPQVGSVEEF
QGQERLVILI STVRSCSTYL QFDQTFRLGF LKNPKRLNVA ITRAKALLIV VGNPTVLSKD
DHWCRFLRYC KEQGGYTGYP YEDEGVVENR LANELQMLQF SV
//
