ID E3LS32_CAERE Unreviewed; 1134 AA.
AC E3LS32;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=Cre-mog-1 {ECO:0000313|EMBL:EFP09262.1};
GN ORFNames=CRE_25237 {ECO:0000313|EMBL:EFP09262.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS268414; EFP09262.1; -; Genomic_DNA.
DR RefSeq; XP_003113008.1; XM_003112960.1.
DR AlphaFoldDB; E3LS32; -.
DR STRING; 31234.E3LS32; -.
DR EnsemblMetazoa; CRE25237.1; CRE25237.1; WBGene00054980.
DR eggNOG; KOG0924; Eukaryota.
DR HOGENOM; CLU_001832_6_2_1; -.
DR InParanoid; E3LS32; -.
DR OMA; VDVMFHR; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0040022; P:feminization of hermaphroditic germ-line; IEA:EnsemblMetazoa.
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:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 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 3: Inferred from homology;
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:UP000008281}.
FT DOMAIN 454..617
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 632..815
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 130110 MW; B4D9331AA6A2D053 CRC64;
MSEKHADDRL EGSNDTFGGL VIKKKKVDGN DSKPSESSGK SLLGLDKLAS TKRENARKRL
DDDDDRGVTE SVRRGIEKVH EKHRDRDDRG MKYKTRDDDR RRDRHYDRSD RRDDSSRREW
RDRRGDETPR FKVPETPSRM SWEQDDREGS SRKKNSWDMP TPRGERDRKR DWDSERSVSS
AWRSERRRRD DDKRKRYNKP EDSVRSVKDE KAEPTFHDDE ERAQWEEEQK NLDREWYDNE
GAFDDEYNPF NKVSDEFVEK REKQWQEKTQ KPRLTVKQQA IKRENELWEN NRLHRSGVVA
MADELSSVFE DETDENRVTI LVQNIVPPFL DGRIVFTKQA QPIIPVVDTT CDMAVSAAKG
SVAVRRRREM EDRKRAQDKH WELAGSKLGN LMGVKEKADE TANPEDDDSG NYKESHQFAS
HMKDNEAVSD FAMEKTIKQQ REYLPVFACR QKMMNVIREN NVVIIVGETG SGKTTQLAQY
LLEDGFGESG LIGCTQPRRV AAMSVARRVA DEMGVDLGQD VGYAIRFEDC TSEKTIIKYM
TDGILLRECL GDGTLDQYSA IIMDEAHERS LNTDVLFGLL REVVAKRADL KLIVTSATMD
ADKFADFFGG NCPTFTIPGR TFPVELFHAR TPVEDYVDAA VKQAVTIHLG GMDGDILIFM
PGQEDIECTC EMIKEKLGEL DEAPPLAVLP IYSQLPSDLQ AKIFQRAPGG MRKAIVATNI
AETSLTVDGI LFVIDPGFCK MKVYNPRIGM DALSIFPVSQ ASANQRTGRA GRTGPGQCYR
LYTERQFKDE LLRSTVPEIQ RTNLANVVLL LKSLGVDDLL KFHFMDAPPQ DNMLNSMYQL
WTLGALDNTG QLTSMGRKMV EFPLDPTLSK MLIVSSEMGC SDEVLTIVSM LSVPAIFFRP
KGREEEADAK KEKFQVPESD HLTFLNVYLQ WREHKYSAKW CADNYLHVKA LKKVREVRAQ
LKEIMQDLKL PIISNGNEWD IVRKCICSAY FHNAARLKGI GEYVNVRTGI PCFLHPTSAL
FGMGFMPDYV VYHELIMTAK EYMQCVTAVD AIWLAELGPM FYSIKESKQS RREQKMESVR
TVETMEAEMR EAQKEMERRK EESDKAFKRP ESSRRVVEVG SKSVRSERRK LWGL
//