GLH2_CAEEL
ID GLH2_CAEEL Reviewed; 974 AA.
AC Q966L9; Q27376;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ATP-dependent RNA helicase glh-2;
DE EC=3.6.4.13;
DE AltName: Full=Germline helicase 2;
GN Name=glh-2; ORFNames=C55B7.1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=Bristol N2;
RX PubMed=8943022; DOI=10.1073/pnas.93.24.13837;
RA Gruidl M.E., Smith P.A., Kuznicki K.A., McCrone J.S., Kirchner J.,
RA Roussell D.L., Strome S., Bennett K.L.;
RT "Multiple potential germ-line helicases are components of the germ-line-
RT specific P granules of Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13837-13842(1996).
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 KGB-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).
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 (via C-terminus) with kgb-1.
CC {ECO:0000269|PubMed:12435362}.
CC -!- INTERACTION:
CC Q966L9; O44408: kgb-1; NbExp=2; IntAct=EBI-1571876, EBI-319489;
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; U60194; AAB03337.1; -; mRNA.
DR EMBL; U60449; AAB03510.1; -; Genomic_DNA.
DR EMBL; FO080958; CCD68088.1; -; Genomic_DNA.
DR RefSeq; NP_491876.1; NM_059475.5.
DR AlphaFoldDB; Q966L9; -.
DR SMR; Q966L9; -.
DR BioGRID; 37812; 5.
DR IntAct; Q966L9; 1.
DR STRING; 6239.C55B7.1; -.
DR iPTMnet; Q966L9; -.
DR EPD; Q966L9; -.
DR PaxDb; Q966L9; -.
DR PeptideAtlas; Q966L9; -.
DR EnsemblMetazoa; C55B7.1.1; C55B7.1.1; WBGene00001599.
DR GeneID; 172361; -.
DR KEGG; cel:CELE_C55B7.1; -.
DR UCSC; C55B7.1.2; c. elegans.
DR CTD; 172361; -.
DR WormBase; C55B7.1; CE09012; WBGene00001599; glh-2.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000157507; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q966L9; -.
DR OMA; NCHDEAK; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; Q966L9; -.
DR SignaLink; Q966L9; -.
DR PRO; PR:Q966L9; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001599; Expressed in reproductive system and 5 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: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; IDA:WormBase.
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 GO; GO:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
DR GO; GO:0016070; P:RNA metabolic process; ISS:WormBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; 6.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00343; ZnF_C2HC; 6.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57756; SSF57756; 3.
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; 6.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..974
FT /note="ATP-dependent RNA helicase glh-2"
FT /id="PRO_0000055090"
FT DOMAIN 583..767
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 803..950
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 257..274
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 282..299
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 371..388
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 396..413
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 453..470
FT /note="CCHC-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 473..490
FT /note="CCHC-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 212..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 552..580
FT /note="Q motif"
FT MOTIF 710..713
FT /note="DEAD box"
FT COMPBIAS 232..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 596..603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 120
FT /note="G -> S (in Ref. 1; AAB03510/AAB03337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 974 AA; 100396 MW; 13225A843BFEBFA1 CRC64;
MSDDWDNNTA AAKTISFGSN PSGFGGGSGF GSGNTGGFGS GNAGGTGFGS SNNGGSGFGG
NNNVGPRFGN GNAGGTGFGS GNAGGTGFGS GNAGGTGFGS GNAGGTGFGS GNAGGTGFGG
GNAGGTGFGS GNAGGTGLGS GNAGGTGFGS GNAGGTGFGS GNAGGTGFGS GKAGGTGFGS
GKAGGTGFGG NSNSGSGFGS GLTNGFGSGN NHESGFGGGK SGGFGGGNSG GSGFGSGGNS
NGFGSGGGGQ DRGERNNNCF NCQQPGHRSN DCPEPKKERE PRVCYNCQQP GHNSRDCPEE
RKPREGRNGF TGGSSGFGGG NGGGTGFDSG LTNGFGSGNN GESGFGSGGF GGNSNGFGSG
GGGQDRGERN NNCFNCQQPG HRSNDCPEPK KEREPRVCYN CQQPGHNSRD CPEERKPREG
RNGFTSGFGG GNDGGFGGGN AEGFGNNEER GPMKCFNCKG EGHRSAECPE PPRGCFNCGE
QGHRSNECPN PAKPREGAEG EGPKATYVPV EDNMEEVFNM QKISEGLMFN KFFDAEVKIT
SDKKPVGVKT CKTFSEANLG ETMKKNVAHA GYTKTTPIQQ YTLPLIHQGH DIMACAQTGS
GKTAAFLLPI MARLIDENDL NTAGEGGCYP RCIILTPTRE LTDQIYNEGR KFAYQTMMEI
RPVYGGLAVG YNKGQIEKGA TIIVGTVGRI KHFCEEGTIK LDKCRFFVLD EADRMIDAMG
FGTDIDTIVN YESMPKKENR QTLMFSATFP DSVQEAARNH LKEGYIMLAI DKIGAANKCV
LQEFEKCDRS EKKDKLLEIL GIDIDSYTTE KNSEVYTKKT IVFVSQRAMA DTLASILSSA
QVPAITIHGA REQRERSEAL RQFRNGSKPV LIATAVAERG LDIKGVDHVI NYDMPDNIDD
YIHRIGRTGR VGNAGRATSF ISEDCNLLSE LVRVLSDADQ LVPEWMQGAS GGNFGASFGF
ESSVPTQKQD EDCW
