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Database: UniProt
Entry: E3LS32_CAERE
LinkDB: E3LS32_CAERE
Original site: E3LS32_CAERE 
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}.
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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
//
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