ID F8KWD9_PARAV Unreviewed; 512 AA.
AC F8KWD9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN Name=rng {ECO:0000313|EMBL:CCB85337.1};
GN OrderedLocusNames=PUV_03870 {ECO:0000313|EMBL:CCB85337.1};
OS Parachlamydia acanthamoebae (strain UV7).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Parachlamydia.
OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB85337.1, ECO:0000313|Proteomes:UP000000495};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UV7;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S.A., Horn M.;
RT "Unity in variety -- the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 0:0-0(2011).
RN [2] {ECO:0000313|EMBL:CCB85337.1, ECO:0000313|Proteomes:UP000000495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC {ECO:0000256|ARBA:ARBA00005663}.
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DR EMBL; FR872580; CCB85337.1; -; Genomic_DNA.
DR RefSeq; WP_006340241.1; NC_015702.1.
DR AlphaFoldDB; F8KWD9; -.
DR STRING; 765952.PUV_03870; -.
DR KEGG; puv:PUV_03870; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_0; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000000495; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd04453; S1_RNase_E; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR004659; RNase_E/G.
DR InterPro; IPR048583; RNase_E_G_thioredoxin-like.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00757; RNaseEG; 1.
DR PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR PANTHER; PTHR30001:SF0; RIBONUCLEASE G; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR Pfam; PF20833; RNase_E_G_Thio; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCB85337.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000495};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 38..141
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 512 AA; 59387 MW; C27BEAD33D3FC7B5 CRC64;
MDEILLNIES KELRYAHLRN GQLYNLIVER KRERQLAGNI YKGSVTNILH NIQSAFIDIN
EGENGFIHIS DILENTKKFE QVYDMDFDLD YDIKGLDDKQ QKKQDIEEVM KIDQPVLVQV
VKEPIGSKGA RLTSNISLAG RYLVLLPNSS HRGVSRKIED RNARERLKKL IRAFEMPTDM
GLICRTASAR ATPEMLIAEA TDLLSTWHTI MENFHKSSGP SLLYAESDLI KRAVITAVDK
RFERILVDDY AVYQSCKNLY SRYASEHALR IEYYRDNVPM FERFNVEREI DKTLRRKIWL
PSGGYLFFDR TEAMYTIDVN SGRSSNNKVD VEESLVRINL EAADEIARQL RLRNIGGLVI
CDFIDMRYRK NQRRVLDRLK ECMKEDSAKC TILGMSEFGL VEMTRQRNRE SLIQTIFTTC
PYCSGRGLVK THESVSIEIE RALKKAIAHN QQFALKLVVH PELDHYLASI DKRFLLKIAE
GLNARLEFDV NDNLHLNEFH FYSTITDKKV EV
//
