ID Q20644_CAEEL Unreviewed; 1425 AA.
AC Q20644;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 183.
DE SubName: Full=RNA helicase {ECO:0000313|EMBL:CAA99855.1};
GN ORFNames=CELE_F52B5.3 {ECO:0000313|EMBL:CAA99855.1}, F52B5.3
GN {ECO:0000313|EMBL:CAA99855.1, ECO:0000313|WormBase:F52B5.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA99855.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA99855.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA99855.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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DR EMBL; BX284601; CAA99855.1; -; Genomic_DNA.
DR PIR; T22493; T22493.
DR RefSeq; NP_492260.1; NM_059859.4.
DR AlphaFoldDB; Q20644; -.
DR SMR; Q20644; -.
DR STRING; 6239.F52B5.3.1; -.
DR EPD; Q20644; -.
DR PaxDb; 6239-F52B5-3; -.
DR PeptideAtlas; Q20644; -.
DR EnsemblMetazoa; F52B5.3.1; F52B5.3.1; WBGene00009922.
DR GeneID; 172615; -.
DR KEGG; cel:CELE_F52B5.3; -.
DR UCSC; F52B5.3; c. elegans.
DR AGR; WB:WBGene00009922; -.
DR WormBase; F52B5.3; CE05718; WBGene00009922; -.
DR eggNOG; KOG0920; Eukaryota.
DR HOGENOM; CLU_001832_1_4_1; -.
DR InParanoid; Q20644; -.
DR OMA; FGICLKC; -.
DR OrthoDB; 1095660at2759; -.
DR PhylomeDB; Q20644; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009922; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd02325; R3H; 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 Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF01424; R3H; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51061; R3H; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:CAA99855.1};
KW Hydrolase {ECO:0000313|EMBL:CAA99855.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|EPD:Q20644,
KW ECO:0007829|PeptideAtlas:Q20644};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 35..101
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 191..356
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 630..805
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 433..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..416
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1247..1275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1425 AA; 162468 MW; 2A04352CC193199E CRC64;
MSDEPPGFFR GGVDSKRCSR NGFDASRVLP RGTDNDTRKE YRRVANEIIR SFLKSGQKNT
TLEPMGRDQR KVMHEVALLN EMTTKSHGRE PDRYMILSKR VNRLSKSTLV ATEPITPSFE
CLQKLSKFVE KHPITREEMD EFLTETQTKQ MHTTKGHISD RMVIPPKSKC SKELQKVRNS
LPASKYCDQV LKSISSCNVV IISGGTGCGK TTQVPQFILD EAHENNKHVR VMVTQPRRIA
AISIAERVAR ERGEPIGRTV GYQVRLDSRR SDDTVLTYCT TGVLLRMLTS DPVASGITHI
VMDEIHEREI NTDYLLIALR ECLKMRPDLK VILMSATIEG NMQLFSNYFE NHSMDVIRIE
SRAFDVKVFY LDQILAMTGY QPPESKAFFS TAEYEEEDWK DEIEAVEREE KDKAKQRAAD
SSLSTLSKPV TKMAANTKRN SPIEEREWTS GPCSTPDGDI IDERAMRQYM NIIGNPDIRP
VITVEFRPTT PNSVFINDVK YTTNPNQSAQ ALLQQKRERC LMPRGPLTFT CENPASTTKS
PPSPTPTLGI SSGLAKFTPF GGFGEKQRIS TLLEKKFKEE LKTALPDRTV YYHPQMNDVV
DKTDFSKLRF GEKYNLFYGS SSNNSVDYVL LDQVIQYLAD SPVFGTILVF LPGYEDIQQM
LKAIDCWKNS LKNMKNVIVL PLHSQMTSIN HGDIFKSVPK DTRKIILATN IAEASITIED
VIFVVDTGKV KEKSFDHEAK LSTLTVKPIA RSNADQRSGR AGRVANGYCI RLYTEQEYNS
MPETQIAEMK RAAIYDVTLH AKLFAPKTLK ISEFLSLAPE PPEKESILQA ITFLEQIGAF
YTPIKIYDNS GNEEGLKNDE EAENSENPED PELTDLGRLM ARLPLDPQLS RMLLFGLALK
CLTPIVNLVA LLASREPYVL ALSEDRDLQS KMKFEMAQQD LSDHLLYIRL CNEFCSKNNS
QQNQFCRDHF LNFSTMRMVQ GTRRQLLREL VRAKLINISP NRDVLTVLTD HHFNQFSQCW
PMIQAVIAAG CYPFIGVSAS ESNLKKVQTF NDKPAFLHPS SMVKKQIVKM GKSEKSPRVE
YVAFQEMCQM PSDRSLSMKT VTVIPSMTAL LFTGPIRLDE RTIEDNNIIF EEGEDISVED
KPLPWGASLS LLKLDEWYNV RSVKKNLCHF LRLRHKFMHF FVKGISDPDT FGKQTSLADL
EMLELIRYVL ESENKRYNFA PVVMPHLNLK FYSNSENPYA SIVRNDNNRR NHSDPNQKST
ERESRKPKEA VSHGNSRKQS KPPKNHQTKT TSNFPSHNFP PPDLMRNSHY NQNMSTSHQS
SSSNNHHYSH NYSYPHYNIQ LPQNQYQSWT PQFDFHSMNT SYGEHGHNGN HQYMESSGIH
GHIPYQGGNF NTRGVSRGGF SYTSGNQFRG RGLSRKLYEH NPRNE
//
