CGH1_CAEEL
ID CGH1_CAEEL Reviewed; 430 AA.
AC Q95YF3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=ATP-dependent RNA helicase cgh-1;
DE EC=3.6.4.13;
DE AltName: Full=Conserved germline helicase 1;
GN Name=cgh-1; ORFNames=C07H6.5;
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 [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 [2]
RP PROTEIN SEQUENCE OF 21-28; 34-61; 111-121; 158-178; 188-215 AND 333-342,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11546739; DOI=10.1242/dev.128.17.3221;
RA Navarro R.E., Shim E.Y., Kohara Y., Singson A., Blackwell T.K.;
RT "cgh-1, a conserved predicted RNA helicase required for gametogenesis and
RT protection from physiological germline apoptosis in C. elegans.";
RL Development 128:3221-3232(2001).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH CAR-1.
RX PubMed=16221731; DOI=10.1242/dev.02060;
RA Boag P.R., Nakamura A., Blackwell T.K.;
RT "A conserved RNA-protein complex component involved in physiological
RT germline apoptosis regulation in C. elegans.";
RL Development 132:4975-4986(2005).
RN [5]
RP INTERACTION WITH IFET-1, AND SUBCELLULAR LOCATION.
RX PubMed=23264733; DOI=10.1242/jcs.119834;
RA Sengupta M.S., Low W.Y., Patterson J.R., Kim H.M., Traven A.,
RA Beilharz T.H., Colaiacovo M.P., Schisa J.A., Boag P.R.;
RT "ifet-1 is a broad-scale translational repressor required for normal P
RT granule formation in C. elegans.";
RL J. Cell Sci. 126:850-859(2013).
RN [6]
RP INTERACTION WITH OMA-1.
RX PubMed=25261697; DOI=10.1534/genetics.114.168823;
RA Spike C.A., Coetzee D., Nishi Y., Guven-Ozkan T., Oldenbroek M.,
RA Yamamoto I., Lin R., Greenstein D.;
RT "Translational control of the oogenic program by components of OMA
RT ribonucleoprotein particles in Caenorhabditis elegans.";
RL Genetics 198:1513-1533(2014).
CC -!- FUNCTION: Probable RNA helicase required for oocyte and sperm function.
CC Also required to prevent the physiological germline apoptosis mechanism
CC killing essentially all developing oocytes.
CC {ECO:0000269|PubMed:11546739, ECO:0000269|PubMed:16221731}.
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 car-1 in a germline ribonucleoprotein complex
CC (PubMed:16221731). Interacts with ifet-1 (PubMed:23264733). Interacts
CC with oma-1, which is a component of a ribonucleoprotein complex, in an
CC RNA-dependent manner (PubMed:25261697). {ECO:0000269|PubMed:16221731,
CC ECO:0000269|PubMed:23264733, ECO:0000269|PubMed:25261697}.
CC -!- INTERACTION:
CC Q95YF3; Q21740: edc-3; NbExp=5; IntAct=EBI-314525, EBI-314602;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11546739}.
CC Note=Cytoplasmic when associated with pgl-1. Associates with P granules
CC and this localization is dependent on ifet-1.
CC {ECO:0000269|PubMed:11546739, ECO:0000269|PubMed:23264733}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to two germline precursors
CC Z2 and Z3 in L1 stage hermaphrodites, and is detectable specifically in
CC the gonad at low levels into the L3 stage. Expression is significantly
CC higher during the early L4 stage. In adults, expression remains gonad-
CC specific and was not apparent in the somatically derived uterus.
CC Expressed in germ granules (P granules); when associated with pgl-1.
CC {ECO:0000269|PubMed:11546739}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC subfamily. {ECO:0000255}.
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DR EMBL; FO080423; CCD63592.1; -; Genomic_DNA.
DR RefSeq; NP_498646.1; NM_066245.5.
DR PDB; 7DTJ; X-ray; 2.40 A; A=247-420.
DR PDB; 7DTK; X-ray; 1.85 A; A/B=20-248.
DR PDBsum; 7DTJ; -.
DR PDBsum; 7DTK; -.
DR AlphaFoldDB; Q95YF3; -.
DR SMR; Q95YF3; -.
DR BioGRID; 41269; 50.
DR DIP; DIP-25457N; -.
DR IntAct; Q95YF3; 23.
DR STRING; 6239.C07H6.5; -.
DR iPTMnet; Q95YF3; -.
DR EPD; Q95YF3; -.
DR PaxDb; Q95YF3; -.
DR PeptideAtlas; Q95YF3; -.
DR EnsemblMetazoa; C07H6.5.1; C07H6.5.1; WBGene00000479.
DR GeneID; 176061; -.
DR KEGG; cel:CELE_C07H6.5; -.
DR UCSC; C07H6.5.1; c. elegans.
DR CTD; 176061; -.
DR WormBase; C07H6.5; CE00839; WBGene00000479; cgh-1.
DR eggNOG; KOG0326; Eukaryota.
DR GeneTree; ENSGT00940000170366; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q95YF3; -.
DR OMA; TYEDRHT; -.
DR OrthoDB; 583315at2759; -.
DR PhylomeDB; Q95YF3; -.
DR Reactome; R-CEL-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:Q95YF3; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000479; Expressed in adult organism and 8 other tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:WormBase.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:WormBase.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0000932; C:P-body; IDA:WormBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; 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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISS:WormBase.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0007276; P:gamete generation; IMP:WormBase.
DR GO; GO:0016071; P:mRNA metabolic process; IMP:WormBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:WormBase.
DR GO; GO:0017148; P:negative regulation of translation; IMP:WormBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0033962; P:P-body assembly; IMP:WormBase.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; ATP-binding; Cytoplasm; Developmental protein;
KW Differentiation; Direct protein sequencing; Helicase; Hydrolase;
KW Nucleotide-binding; Oogenesis; Reference proteome; RNA-binding;
KW Spermatogenesis.
FT CHAIN 1..430
FT /note="ATP-dependent RNA helicase cgh-1"
FT /id="PRO_0000239936"
FT DOMAIN 74..244
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 254..414
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 43..71
FT /note="Q motif"
FT /evidence="ECO:0000255"
FT MOTIF 192..195
FT /note="DEAD box"
FT /evidence="ECO:0000255"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:7DTK"
FT TURN 135..139
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:7DTK"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:7DTK"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7DTJ"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:7DTJ"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:7DTJ"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:7DTJ"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:7DTJ"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:7DTJ"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:7DTJ"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:7DTJ"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:7DTJ"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:7DTJ"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:7DTJ"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:7DTJ"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:7DTJ"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:7DTJ"
FT HELIX 389..398
FT /evidence="ECO:0007829|PDB:7DTJ"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:7DTJ"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:7DTJ"
SQ SEQUENCE 430 AA; 48713 MW; 0C31C5597DD8B5D4 CRC64;
MSGAEQQQIV PANNGDENWK AGLNLPAKDR RFKTADVTDT KGVEFEDFCL GRDLLMGIFE
KGWEKPSPIQ EASIGVALTG QDILARAKNG TGKTGAYCIP VIEKIQPALK AIQAMVIVPT
RELALQTSQI CVELSKHIQL KVMVTTGGTD LRDDIMRLNG TVHLVIATPG RILDLMEKGV
AKMEHCKTLV LDEADKLLSQ DFQGILDRLI NFLPKERQVM LYSATFPNTV TSFMQKHMHK
PYEINLMEEL TLLGVTQYYA FVQEKQKVHC LNTLFRKLQI NQSIIFCNST QRVELLAKKI
TEIGYSCYYI HSKMAQNHRN RVFHDFRQGN CRNLVCSDLL TRGIDIQAVN VVINFDFPRN
AETYLHRIGR SGRFGHLGVA INLITYEDRH TLRRIEQELR TRIEPIPKTV DPKLYVADQQ
LVDAADETTA
