ID   DHX16_CAEEL             Reviewed;        1008 AA.
AC   O45244; O45239;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Probable pre-mRNA-splicing factor ATP-dependent RNA helicase mog-4;
DE            EC=3.6.4.13;
DE   AltName: Full=Masculinization of germline protein 4;
DE   AltName: Full=Sex determination protein mog-4;
GN   Name=mog-4; ORFNames=C04H5.6;
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], PROBABLE FUNCTION, DEVELOPMENTAL STAGE, AND
RP   DISRUPTION PHENOTYPE.
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).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=8111975; DOI=10.1002/dvg.1020140608;
RA   Graham P.L., Schedl T., Kimble J.;
RT   "More mog genes that influence the switch from spermatogenesis to oogenesis
RT   in the hermaphrodite germ line of Caenorhabditis elegans.";
RL   Dev. Genet. 14:471-484(1993).
RN   [4]
RP   INTERACTION WITH MEP-1, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=12088146; DOI=10.1017/s1355838202028595;
RA   Belfiore M., Mathies L.D., Pugnale P., Moulder G., Barstead R., Kimble J.,
RA   Puoti A.;
RT   "The MEP-1 zinc-finger protein acts with MOG DEAH box proteins to control
RT   gene expression via the fem-3 3' untranslated region in Caenorhabditis
RT   elegans.";
RL   RNA 8:725-739(2002).
RN   [5]
RP   INTERACTION WITH SMN-1.
RX   PubMed=16964508; DOI=10.1007/s10158-006-0027-x;
RA   Burt E.C., Towers P.R., Sattelle D.B.;
RT   "Caenorhabditis elegans in the study of SMN-interacting proteins: a role
RT   for SMI-1, an orthologue of human Gemin2 and the identification of novel
RT   components of the SMN complex.";
RL   Invertebr. Neurosci. 6:145-159(2006).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18729217; DOI=10.1002/dvdy.21649;
RA   Konishi T., Uodome N., Sugimoto A.;
RT   "The Caenorhabditis elegans DDX-23, a homolog of yeast splicing factor
RT   PRP28, is required for the sperm-oocyte switch and differentiation of
RT   various cell types.";
RL   Dev. Dyn. 237:2367-2377(2008).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in pre-mRNA splicing
CC       (Probable). Operates during embryogenesis. {ECO:0000305}.
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   -!- SUBUNIT: Interacts with mep-1 and smn-1. {ECO:0000269|PubMed:12088146,
CC       ECO:0000269|PubMed:16964508}.
CC   -!- INTERACTION:
CC       O45244; Q21502: mep-1; NbExp=2; IntAct=EBI-326143, EBI-319858;
CC       O45244; P34498: mog-1; NbExp=2; IntAct=EBI-326143, EBI-3651301;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development but most strongly
CC       in embryos and the L4 larvae stage. {ECO:0000269|PubMed:10737793,
CC       ECO:0000269|PubMed:12088146}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal. Defects in oocytogenesis and
CC       spermatogenesis. Approximately 80% of mutants have an abnormal somatic
CC       gonad and no vulva. {ECO:0000269|PubMed:10737793,
CC       ECO:0000269|PubMed:12088146, ECO:0000269|PubMed:18729217,
CC       ECO:0000269|PubMed:8111975}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX16/PRP8 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF286900; AAG01333.1; -; mRNA.
DR   EMBL; Z81462; CAB03845.1; -; Genomic_DNA.
DR   EMBL; Z81457; CAB03845.1; JOINED; Genomic_DNA.
DR   PIR; T18832; T18832.
DR   RefSeq; NP_497027.1; NM_064626.4.
DR   AlphaFoldDB; O45244; -.
DR   SMR; O45244; -.
DR   BioGRID; 40398; 14.
DR   DIP; DIP-24771N; -.
DR   IntAct; O45244; 4.
DR   STRING; 6239.C04H5.6a; -.
DR   EPD; O45244; -.
DR   PaxDb; O45244; -.
DR   PeptideAtlas; O45244; -.
DR   PRIDE; O45244; -.
DR   EnsemblMetazoa; C04H5.6a.1; C04H5.6a.1; WBGene00003392.
DR   GeneID; 175117; -.
DR   KEGG; cel:CELE_C04H5.6; -.
DR   UCSC; C04H5.6; c. elegans.
DR   CTD; 175117; -.
DR   WormBase; C04H5.6a; CE15592; WBGene00003392; mog-4.
DR   eggNOG; KOG0923; Eukaryota.
DR   HOGENOM; CLU_001832_7_1_1; -.
DR   InParanoid; O45244; -.
DR   OMA; PHYHKKK; -.
DR   OrthoDB; 354219at2759; -.
DR   PhylomeDB; O45244; -.
DR   Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; O45244; -.
DR   PRO; PR:O45244; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00003392; Expressed in adult organism and 4 other tissues.
DR   ExpressionAtlas; O45244; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF04408; HA2; 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; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 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..1008
FT                   /note="Probable pre-mRNA-splicing factor ATP-dependent RNA
FT                   helicase mog-4"
FT                   /id="PRO_0000055153"
FT   DOMAIN          374..538
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          563..737
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          104..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1008
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           485..488
FT                   /note="DEAH box"
FT   COMPBIAS        106..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         387..394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1008 AA;  114290 MW;  F6EB913D919FFD5D CRC64;
     MSVEQFINDQ LHSIVGISDR SICQYVHALA KKAKSAPDLV EKLRDAGDFP ISPAIQSFAD
     QLMSRMPRQA TSARQRGPTT AELAEQELNR LNRAVGVLED YSASSTKTKN VRKRKESSSE
     DDEAPIKASK PGKSVKPSKS DDSESDIEAM EAKLDADIAE RDALAARINK KEKDKTRNVM
     EKKRDDNKDK EGSSMDKLRE ESRRQYLKKR KVDKLEELEA IVHDDQTLFA REKLTKREKA
     DMEYRKKVLE YTKAHGKAGD VMKMKRYHLP DASTKQIPSQ YVEDDEEDFR PGGDGAKWEE
     EQLMASMLHL GAKDAKRKEQ EFELLLDEKV DFIQALQMPG TNEEVVETEA EKKKMSIEET
     RKSLPVYAFR DAFIEAVKEH QVLIIEGETG SGKTTQLPQY LYEAGFCEGG KRIGCTQPRR
     VAAMSVAARV ADEVGCKLGT QVGYSIRFED CTSEKTVLKY MTDGMLLREF LNEPDLASYS
     VMMIDEAHER TLHTDILFGL VKDIARFRKD LKLLISSATL DAEKFSSFFD DAPIFRIPGR
     RFPVDIYYTQ APEADYVDAA IVTIMQIHLT QPLPGDILVF LTGQEEIETV QEALMERSKA
     LGSKIKELIP LPVYANLPSD LQAKIFEPTP KDARKVVLAT NIAETSVTID GINYVIDPGF
     SKQNSFDARS GVEHLHVVTI SKAAANQRAG RAGRTGPGKC FRLYTAWAYK HELEEQPIPE
     IQRTNLGNVV LMLKSLGIHD LVHFDFLDPP PQETLVIALE QLYALGALNH RGELTKLGRR
     MAEFPCDPCM SKMIIASEKY ECSEEIVTIA AMLSCNAAVF YRPKAQVIHA DSARKGFWSP
     AGDHITLMNV YNKWQESSFS QRWCVENYVQ HRTMKRARDV RDQLVGLLER VEIETKSSTD
     TIKIRKAITA GYFYNVSKLD NTGHYKTVKH KHTTHPHPNS CLFEETPRWV VYFELVFTSK
     EFMREMSEIE SGWLLEVAPH YYKGRELEDA TNKKMPKNKG KSGKDLER