GLH3_CAEEL
ID GLH3_CAEEL Reviewed; 720 AA.
AC O01836;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=ATP-dependent RNA helicase glh-3;
DE EC=3.6.4.13;
DE AltName: Full=Germline helicase 3;
GN Name=glh-3 {ECO:0000312|WormBase:B0414.6};
GN ORFNames=B0414.6 {ECO:0000312|WormBase:B0414.6};
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].
RC STRAIN=Bristol N2;
RX PubMed=10851135; DOI=10.1242/dev.127.13.2907;
RA Kuznicki K.A., Smith P.A., Leung-Chiu W.M., Estevez A.O., Scott H.C.,
RA Bennett K.L.;
RT "Combinatorial RNA interference indicates GLH-4 can compensate for GLH-1;
RT these two P granule components are critical for fertility in C. elegans.";
RL Development 127:2907-2916(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 INTERACTION WITH CSN-5; KGB-1 AND ZYX-1.
RX PubMed=12435362; DOI=10.1006/dbio.2002.0832;
RA Smith P., Leung-Chiu W.-M., Montgomery R., Orsborn A., Kuznicki K.,
RA Gressman-Coberly E., Mutapcic L., Bennett K.;
RT "The GLH proteins, Caenorhabditis elegans P granule components, associate
RT with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a
RT predicted cytoskeletal protein.";
RL Dev. Biol. 251:333-347(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=21402787; DOI=10.1083/jcb.201010106;
RA Hanazawa M., Yonetani M., Sugimoto A.;
RT "PGL proteins self associate and bind RNPs to mediate germ granule assembly
RT in C. elegans.";
RL J. Cell Biol. 192:929-937(2011).
CC -!- FUNCTION: Probable ATP-binding RNA helicase.
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 csn-5. Interacts (via C-terminus) with kgb-1.
CC Interacts with zyx-1. {ECO:0000269|PubMed:12435362}.
CC -!- INTERACTION:
CC O01836; P91001: csn-5; NbExp=2; IntAct=EBI-1571750, EBI-313007;
CC O01836; P34689: glh-1; NbExp=2; IntAct=EBI-1571750, EBI-1571791;
CC O01836; O44408: kgb-1; NbExp=2; IntAct=EBI-1571750, EBI-319489;
CC O01836; Q9U3F4: zyx-1; NbExp=2; IntAct=EBI-1571750, EBI-322208;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21402787}.
CC -!- DEVELOPMENTAL STAGE: During germline proliferation.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000305}.
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DR EMBL; AF079509; AAC28388.1; -; mRNA.
DR EMBL; FO080197; CCD61900.1; -; Genomic_DNA.
DR PIR; T15231; T15231.
DR RefSeq; NP_491681.1; NM_059280.4.
DR AlphaFoldDB; O01836; -.
DR SMR; O01836; -.
DR BioGRID; 37700; 5.
DR IntAct; O01836; 4.
DR STRING; 6239.B0414.6; -.
DR iPTMnet; O01836; -.
DR EPD; O01836; -.
DR PaxDb; O01836; -.
DR PeptideAtlas; O01836; -.
DR PRIDE; O01836; -.
DR EnsemblMetazoa; B0414.6.1; B0414.6.1; WBGene00001600.
DR GeneID; 172245; -.
DR KEGG; cel:CELE_B0414.6; -.
DR UCSC; B0414.6; c. elegans.
DR CTD; 172245; -.
DR WormBase; B0414.6; CE07736; WBGene00001600; glh-3.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000157507; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; O01836; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; O01836; -.
DR SignaLink; O01836; -.
DR PRO; PR:O01836; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001600; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
DR GO; GO:0008432; F:JUN kinase binding; IPI:WormBase.
DR GO; GO:0043621; F:protein self-association; IPI:WormBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..720
FT /note="ATP-dependent RNA helicase glh-3"
FT /id="PRO_0000055091"
FT DOMAIN 329..513
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 549..698
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 202..219
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 222..239
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 298..326
FT /note="Q motif"
FT MOTIF 456..459
FT /note="DEAD box"
FT COMPBIAS 11..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 342..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 720 AA; 79728 MW; A91F49FE2B79DEAA CRC64;
MDKSPTKTSI RTKFARHQPI SDVDTTEQSS SCIKKDDRGL SSFGVQSSVF SRRSCRMSEL
EAKPTIISED QRIAVRSEIG GSFSGFDDKV DNVFHSNNNL HGSPSTTELE CPGIMNPRFL
VGRSLNSRSR AVTRGSKRTS NVKENEGSIH RSDDQVSTEN CSAKDEERDR DSGGVSSYGN
KRSDEFCGTS PILEAKGFGI SNTCFNCKKY GHRATECSAP QRECANCGDP NHRANECASW
SKNGVQEPTK VTYVPVVDKM EEVFSMLKIN AGDFFDKFFD ASVQLVSRGQ PVTIQPCKSF
SDSDIPQSMR RNVERAGYTR TTPIQQYTLP LVADGKDILA CAQTGSGKTA AFLLPIMSRL
ILEKDLNYGA EGGCYPRCII LTPTRELADQ IYNEGRKFSY QSVMEIKPVY GGINVGYNKS
QIMKGCTIIV GTIGRVKHFC EDGAIKLDKC RYLVLDEADR MIDSMGFGPE IEQIINYKNM
PKNDKRQTMM FSATFPSSVQ EAARKLLRED YTMITIDKIG AANKCVIQEF ELCDRTSKVD
KLLKLLGIDI DTYTTEKNSD VFVKKTIVFV AQQKMADTLA SIMSAAQVPA ITIHGAREQK
ERSAALKLFR SGAKPVLIAT AVVERGLDIK GVDHVINYDM PNNIDDYIHR IGRTGRVGNS
GRATSFISLA DDVQILPQLV RTLADAEQVV PSWMKEAAGG TSNPNKFEKS IDTEEPEEAW
