MOG5_CAEEL
ID MOG5_CAEEL Reviewed; 1200 AA.
AC Q09530;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-5;
DE EC=3.6.4.13;
DE AltName: Full=Masculinization of germline protein 5;
DE AltName: Full=Sex determination protein mog-5;
GN Name=mog-5; ORFNames=EEED8.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10737793; DOI=10.1073/pnas.97.7.3276;
RA Puoti A., Kimble J.;
RT "The hermaphrodite sperm/oocyte switch requires the Caenorhabditis elegans
RT homologs of PRP2 and PRP22.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3276-3281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Could act late in the splicing of pre-mRNA and mediate the
CC release of the spliced mRNA from spliceosomes. {ECO:0000250}.
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 -!- INTERACTION:
CC Q09530; Q21502: mep-1; NbExp=3; IntAct=EBI-329912, EBI-319858;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX8/PRP22 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF286899; AAG01332.1; -; mRNA.
DR EMBL; FO081042; CCD68732.1; -; Genomic_DNA.
DR PIR; T15921; T15921.
DR RefSeq; NP_495019.1; NM_062618.6.
DR AlphaFoldDB; Q09530; -.
DR SMR; Q09530; -.
DR BioGRID; 39264; 22.
DR DIP; DIP-25759N; -.
DR IntAct; Q09530; 2.
DR STRING; 6239.EEED8.5; -.
DR iPTMnet; Q09530; -.
DR EPD; Q09530; -.
DR PaxDb; Q09530; -.
DR PeptideAtlas; Q09530; -.
DR PRIDE; Q09530; -.
DR EnsemblMetazoa; EEED8.5.1; EEED8.5.1; WBGene00003393.
DR GeneID; 173920; -.
DR KEGG; cel:CELE_EEED8.5; -.
DR UCSC; EEED8.5; c. elegans.
DR CTD; 173920; -.
DR WormBase; EEED8.5; CE01889; WBGene00003393; mog-5.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000155510; -.
DR HOGENOM; CLU_001832_2_4_1; -.
DR InParanoid; Q09530; -.
DR OMA; DPMVAPE; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; Q09530; -.
DR PRO; PR:Q09530; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003393; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0048589; P:developmental growth; IMP:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0040022; P:feminization of hermaphroditic germ-line; IMP:WormBase.
DR GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1200
FT /note="Probable pre-mRNA-splicing factor ATP-dependent RNA
FT helicase mog-5"
FT /id="PRO_0000055133"
FT DOMAIN 234..304
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 550..713
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 738..911
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 138..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 660..663
FT /note="DEAH box"
FT COMPBIAS 138..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..178
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 563..570
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1200 AA; 135759 MW; 023C46E494D7F44F CRC64;
MDQLEHLSLV SKVLSEVENH FGVVEKDVAE FVIHLAQENP TFDKLKKALD SQGLGDQFDD
SLTATILRIV QSMTAVKKKN KKGGDSKEDI KDSHKITLIS DAKEEIKARL PALAMANTAK
EKEDNEDDLM AQLEKMEGRY ESEKRLQKES DSKRNRSRSR SRSRDRKRRR SRSGDRDRRR
RSRSREDRRD RDRRDRDRDR DRGRGDRRGD DRQRDRRDRR DDGGARKSEV AEIGKIYDGR
VNSIQSFGAF ITLEGFRQKQ EGLVHISQIR NERVQTVADV LKRGENVKVK VNKIENGKIS
LSMKEVDQNS GEDLNPRETD LNPDAIGVRP RTPPASTSSW MNPEASGVGQ GPSTSIGGGK
ARVRISTPER WELRQMQGAG VLTATDMPDF DEEMGVLRNY DDESDGEDIE IELVEDEPDF
LRGYGKGGAE IEPVKVVKNP DGSLAQAALM QGALSKERKE TKIQAQRERD MDTQKGFSSN
ARILDPMSGN QSTAWSADES KDRNNKMKEM PEWLKHVTAG GKATYGRRTN LSMVEQRESL
PIFALKKNLM EAMIDNQILV VVGETGSGKT TQMTQYAIEA GLGRRGKIGC TQPRRVAAMS
VAKRVAEEYG CKLGTDVGYT IRFEDCTSQD TIIKYMTDGM LLRECLIDPD LSGYSLIMLD
EAHERTIHTD VLFGLLKAAA RKRPELKLII TSATLDSVKF SEYFLEAPIF TIPGRTFPVE
ILYTREPESD YLEAAHITVM QIHLTEPPGD VLVFLTGQEE IDTSCEVLYE RMKSMGPDVP
ELIILPVYGA LPSEMQTRIF DPAPAGKRKV VIATNIAETS LTIDGIFYVV DPGFVKQKIY
NPKSGMDSLV VTPISQAAAK QRSGRAGRTG PGKCYRLYTE RAFRDEMLPT PVPEIQRTNL
ASTLLQLKAM GINNLIDFDF MDAPPLDSMI TALNTLHTLS ALDGDGLLTK LGRRMAEFPL
EPSLSKLLIM SVDLGCSEEV LTIVAMLNVQ NIFYRPKEKQ DHADQKKAKF HQPEGDHLTL
LAVYNSWKNH HFSQPWCFEN FIQVRSMKRA QDIRKQLLGI MDRHKLLMVS CGRDVSRVQK
AICSGFFRNA AKRDPQEGYR TLTDGQNVYI HPSSACFQQQ PEWVVYHELV MTTKEYMREV
TAIDPKWLVE FAPSFFKIGD STKLSTFKRN QKIDPLFDKY ADANAWRITR VKKRIYNPNK
