PGL1_CAERE
ID PGL1_CAERE Reviewed; 779 AA.
AC E3M3V1;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Guanyl-specific ribonuclease pgl-1 {ECO:0000305};
DE EC=4.6.1.24 {ECO:0000269|PubMed:26787882};
DE AltName: Full=P granule abnormality protein 1;
GN Name=pgl-1 {ECO:0000312|EMBL:EFO90587.1};
GN ORFNames=CRE_08178 {ECO:0000312|EMBL:EFO90587.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641;
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5COW, ECO:0007744|PDB:5CV3}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 203-464, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND DOMAIN.
RX PubMed=26787882; DOI=10.1073/pnas.1524400113;
RA Aoki S.T., Kershner A.M., Bingman C.A., Wickens M., Kimble J.;
RT "PGL germ granule assembly protein is a base-specific, single-stranded
RT RNase.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:1279-1284(2016).
CC -!- FUNCTION: Guanyl-specific endoribonuclease which cleaves the
CC phosphodiester bond in single-stranded RNA between the 3'-guanylic
CC residue and the 5'-OH residue of adjacent nucleotide, resulting in the
CC formation of a corresponding 2',3'-cyclic phosphate intermediate
CC (PubMed:26787882). Essential role in male and female postembryonic
CC germline development; maternally provided protein maintains a
CC population of proliferating germ cells and zygotic expression is
CC required for correct oogenesis (By similarity). Together with the P-
CC granule component pgl-3, is involved in the formation of P-granules (By
CC similarity). Together with pgl-3, probably recruits other granule
CC components such as pos-1, mex-3 and glh-1 to P-granules (By
CC similarity). In addition, may act redundantly with pgl-3 to protect
CC germ cells from excessive germline apoptosis during normal oogenesis
CC and development of the two gonadal arms (By similarity). This may in
CC part be through regulating the localization of sir-2.1 which is
CC involved in germ cell apoptosis (By similarity). May protect somatic
CC cells from excessive apoptosis during normal development (By
CC similarity). {ECO:0000250|UniProtKB:Q9TZQ3,
CC ECO:0000269|PubMed:26787882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'-
CC guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA
CC fragment].; EC=4.6.1.24; Evidence={ECO:0000269|PubMed:26787882};
CC -!- COFACTOR:
CC Note=Does not require metal ions for catalytic activity.
CC {ECO:0000250|UniProtKB:Q9TZQ3};
CC -!- SUBUNIT: Homodimer (PubMed:26787882). Interacts with pgl-2 and pgl-3;
CC this association is not required for P-granule localization of either
CC pgl-2 or pgl-3 (By similarity). Interacts with ife-1 (By similarity).
CC Interacts with prmt-1; the interaction is direct (By similarity).
CC Interacts with nmad-1 (By similarity). Interacts with P granule
CC components meg-1, meg-3 and meg-4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9TZQ3, ECO:0000269|PubMed:26787882}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q9TZQ3}. Note=Localizes to P granules in
CC germline precursor cells. Localizes to P granules in germ cells at all
CC stages of development except in spermatogenesis. Co-localizes with pgl-
CC 3 in P-granules, but localization in P-granules is not dependent on an
CC association with pgl-3. {ECO:0000250|UniProtKB:Q9TZQ3}.
CC -!- DOMAIN: The dimerization domain also acts as a hinge; changes in its
CC structure probably impact oligomerization and RNA-binding.
CC {ECO:0000305|PubMed:26787882}.
CC -!- DOMAIN: The RNA-binding RGG-box is required for the recruitment of some
CC P-granule components such as pos-1 and probably mRNA, but is
CC dispensable for granule formation. {ECO:0000250|UniProtKB:Q9TZQ3}.
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DR EMBL; DS268423; EFO90587.1; -; Genomic_DNA.
DR RefSeq; XP_003109222.1; XM_003109174.1.
DR PDB; 5COW; X-ray; 1.60 A; A=203-464.
DR PDB; 5CV3; X-ray; 3.17 A; A=203-464.
DR PDBsum; 5COW; -.
DR PDBsum; 5CV3; -.
DR AlphaFoldDB; E3M3V1; -.
DR SMR; E3M3V1; -.
DR STRING; 31234.CRE08178; -.
DR EnsemblMetazoa; CRE08178.1; CRE08178.1; WBGene00079876.
DR GeneID; 9821253; -.
DR CTD; 9821253; -.
DR eggNOG; ENOG502QVYU; Eukaryota.
DR HOGENOM; CLU_362575_0_0_1; -.
DR InParanoid; E3M3V1; -.
DR OMA; FESANER; -.
DR OrthoDB; 1081147at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:WormBase.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046589; F:ribonuclease T1 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:WormBase.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; Endonuclease;
KW Hydrolase; Lyase; Nuclease; Oogenesis; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..779
FT /note="Guanyl-specific ribonuclease pgl-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000443016"
FT REGION 203..464
FT /note="Involved in dimerization"
FT /evidence="ECO:0000269|PubMed:26787882"
FT REGION 563..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..772
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250|UniProtKB:Q9TZQ3"
FT REGION 718..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 453
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9TZQ3"
FT HELIX 217..223
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 228..245
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 251..273
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:5COW"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 300..318
FT /evidence="ECO:0007829|PDB:5COW"
FT TURN 343..347
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 355..373
FT /evidence="ECO:0007829|PDB:5COW"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 391..410
FT /evidence="ECO:0007829|PDB:5COW"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:5COW"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 429..442
FT /evidence="ECO:0007829|PDB:5COW"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:5COW"
FT HELIX 448..463
FT /evidence="ECO:0007829|PDB:5COW"
SQ SEQUENCE 779 AA; 84661 MW; C7EC30361F67FCFE CRC64;
MENNKRGVVE AKGIKSHYFQ TLANYVSNNL ELLHNNPKQA NSFAASVFGS TAPIDEKDLL
DLLVPSDANA DALAAGMDCC LLLGEKYRPH FDAAVQQLAR LGRTHDVATV IDDEKKFTAL
SKKTKLKKTD EAKILQAFFK IHSTEDEEKF EAISELCQLD LDFDAYVFIK ALTLENEENQ
ELVETIKDNL VEAWNKSNPL LVKLLLEGVK EQDPVDKFTY LLLQPLTEAT LSDAVNFIVE
KYSAELPDEG DASLVVRSQL GCQFFFLVTR TLAHDQRELA KLVQTLIPRP VRLEVFPGLQ
RSVFKSSVFL GHHIIQIFMG CEFCSIQSIK NTMFSAKKPF QDWSFVGLAQ DFECPWRRLA
IAELLKKFSV SVVEKVFDNP VALIPQHESD NEALIELVTN ALRFALWIVE FYETETNEKS
IKELAFLDHS SKTLLIESFT KFLQGKDVKD QDHLKRIIDA LEKSRTQETK SNLEYSREEI
KTKMPSSSSA KAQVLHGLNT SAAAGLIVPS LSLLEIPVDE VDSTSHLTTS KDIGQGVFVK
AQDTVTEKQK EAPLVAQQTA FHHEPQTATL VPPSPNEESM AAESISTDGW DSPTKSVVLP
LDDMILEEEE RDALKPDSVN SHRSEETTPV PEQLPQETSE RVTSPPPGER SRTAWGDGDA
TPMILATPTN DYKVSGFGGA KLAKGFGTMG STGGGFGGGG GGGSYGGRGG YGGGDRGGRG
GGFGGGDRGG RGGYGGGDRG GRGGGYGGGD RGGYGQRGGY VAGGDRGGRG GYRGGGGNF
