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Database: UniProt
Entry: A0A182E1A2_ONCOC
LinkDB: A0A182E1A2_ONCOC
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ID   A0A182E1A2_ONCOC        Unreviewed;       811 AA.
AC   A0A182E1A2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=DNA helicase {ECO:0000313|WBParaSite:nOo.2.0.1.t01736-RA};
GN   ORFNames=NOO_LOCUS1736 {ECO:0000313|EMBL:VDK64796.1};
OS   Onchocerca ochengi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t01736-RA};
RN   [1] {ECO:0000313|Proteomes:UP000077448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22919073; DOI=10.1101/gr.138420.112;
RA   Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA   Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA   Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT   "Analysis of gene expression from the Wolbachia genome of a filarial
RT   nematode supports both metabolic and defensive roles within the
RT   symbiosis.";
RL   Genome Res. 22:2467-2477(2012).
RN   [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t01736-RA}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDK64796.1, ECO:0000313|Proteomes:UP000271087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UYRW01000235; VDK64796.1; -; Genomic_DNA.
DR   STRING; 42157.A0A182E1A2; -.
DR   WBParaSite; nOo.2.0.1.t01736-RA; nOo.2.0.1.t01736-RA; nOo.2.0.1.g01736.
DR   Proteomes; UP000077448; Unassembled WGS sequence.
DR   Proteomes; UP000271087; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR   CDD; cd17993; DEXHc_CHD1_2; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00598; CHROMO_1; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271087}.
FT   DOMAIN          280..365
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          399..464
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          507..694
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          1..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  93156 MW;  6F839DCA99349749 CRC64;
     MSSSSVTSDS EFTAESSGSE STSDHQRSES ISDHQETITV DLTARQESDT NADGITIVGE
     SFKEGNDGEI SSIGSSKSDS DTKDGESDTS DSKNSENGEF NVYERKSDSV FSAESGDGEV
     ATIKKKRGIK ITDETRKFLE DENILRRSSR QRKETTDSNA EKGTEKTVKK AGKRQLPQSG
     EDETSDDESP SEITLARKTY QKFKKSQAKK RSRKHNISSD DDSGGIRPTR QSKIDGEKNR
     INYRDISSDE EINSDDVLEW DEGDKVGGDG SADHNTSGNE TIEKILRHRA GYPGATGAST
     TCYNVEDKGD PNVKLAENGN EMELERQYLI KWLGWSHLHN TWESENSLKL CNAKGLKKID
     NYMKRLRDIE EWKITADKEY IEFFDCEQQM NDELNEQYKI IERVIAHQIS RNQGETEGTE
     YFVKWCGLPY SECTWEEEHL IARQFKDKID AYYDRRDNGK VPNKHCPVLR KRPRFEKLND
     IPEFLQRKDD PEHELRDYQL EGVNWMLHAW TKENSCILAD EMGLGKTIQS ISFLSVLYHK
     YQLYGPFLVV VPLSTMASWQ HEFETWAPDL NVVTYVGDVT SRDLIRQFEI YVQSAKRLKV
     NVVLTTYEIL LKDKASFPLL LRVGINFVYL QSFLGSFEWA VLAVDEAHRL KNDESLLYRS
     LFEFTTNHRL LITGTPLQNS LKELWALLHF IMPDKFDSWT EFEAEHHDSD HKTIASLHRK
     LQPFLLRRVK KDVEKSLPAK VEQILRVDMT AQQKQYYKWI LTKNYKELSK GVKGSINGFV
     NLVMELKKCC NHASLVRSYD QSEESADARL Q
//
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