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Database: UniProt
Entry: A0A2G5UMK3_9PELO
LinkDB: A0A2G5UMK3_9PELO
Original site: A0A2G5UMK3_9PELO 
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
//
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