ID A0A2G5UMK3_9PELO Unreviewed; 722 AA.
AC A0A2G5UMK3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=RNA helicase {ECO:0008006|Google:ProtNLM};
GN Name=Cni-ddx-35 {ECO:0000313|EMBL:PIC40764.1};
GN Synonyms=Cnig_chr_III.g8398 {ECO:0000313|EMBL:PIC40764.1};
GN ORFNames=B9Z55_008398 {ECO:0000313|EMBL:PIC40764.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC40764.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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 -!- 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:PIC40764.1}.
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DR EMBL; PDUG01000003; PIC40764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UMK3; -.
DR STRING; 1611254.A0A2G5UMK3; -.
DR Proteomes; UP000230233; Chromosome iii.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17980; DEXHc_DHX35; 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:SF136; ATP-DEPENDENT RNA HELICASE DHX35-RELATED; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT DOMAIN 87..251
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 283..457
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 81759 MW; 32D51C50C0AC9126 CRC64;
MSRYHPGHGQ REHRGSAPTR RGFARPSDAA DEPRTGPLIL EEKTTETTSS AGPEDQQLKV
FNNPYASLNI QQQRIRLPIF KNRGHILYMC ERYRTLIIVG ETGCGKSTQV PQFLLEFGWA
DDGRQIAITQ PRRVAVVTLA TRVAEETDTL LGHNIGYTVR FDDVSDEATK VKFMTDGLLL
REILQDPMLS KYSIIMIDEA HERSCNTDIL LGLLRKIMQV RNDLRIIVSS ATLDAELFRD
FFEMNETGNP EKDTAAILSV EGRTHPVAVH HTKTPVPNYC QAAVDTVINI HKHEMPGDIL
VFLTGQDEVE DVCEKLREEA RKLRNCDKLW VVPCYGALPA SEQMKAFDST PHGTRKVVVA
TNIAEASITI PGICYVIDTG YVKLRAVNAN NGVESLMRVT VSQASAEQRA GRAGRIRPGK
CYRLYPESEF QKFSEGTIPE IQRCHLAATI LQLKALGVQN VHKFHYLSPP PSWSMIQGLE
LLYALGAIDE SSQLTDPLGL QMAEFPLAPM HSKCLLKSAE FGCSDEIVTI VAMMQIQDVF
LTPFRARHQA DIIRKKFSVE EGDHMTMLNV FTKFVENGRS KKWCSDHFVN YRGLMRADNV
RSQLVRLLKR FEIPKVSCRG LINASENIRQ CLVTGFFSQA AQYHYTGKYM TVKENFPFNV
YKGSSIMFKK DYPKWVIFTE VMQDSIRDVT VIEPEWLYEL APHYYEFGTE GELAEKRMRG
GQ
//