ID A0A173DY92_9CHLA Unreviewed; 510 AA.
AC A0A173DY92;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=M787_000870 {ECO:0000313|EMBL:ANG65880.1};
OS Chlamydia gallinacea 08-1274/3.
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=1143323 {ECO:0000313|EMBL:ANG65880.1, ECO:0000313|Proteomes:UP000019147};
RN [1] {ECO:0000313|EMBL:ANG65880.1, ECO:0000313|Proteomes:UP000019147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=08-1274/3 {ECO:0000313|EMBL:ANG65880.1,
RC ECO:0000313|Proteomes:UP000019147};
RX PubMed=24461712; DOI=10.1016/j.syapm.2013.12.004;
RA Sachse K., Laroucau K., Riege K., Wehner S., Dilcher M., Creasy H.H.,
RA Weidmann M., Myers G., Vorimore F., Vicari N., Magnino S.,
RA Liebler-Tenorio E., Ruettger A., Bavoil P.M., Hufert F.T.,
RA Rossello-Mora R., Marz M.;
RT "Evidence for the existence of two new members of the family Chlamydiaceae
RT and proposal of Chlamydia avium sp. nov. and Chlamydia gallinacea sp.
RT nov.";
RL Syst. Appl. Microbiol. 37:79-88(2014).
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; CP015840; ANG65880.1; -; Genomic_DNA.
DR RefSeq; WP_021828583.1; NZ_CP015840.1.
DR AlphaFoldDB; A0A173DY92; -.
DR STRING; 1143323.M787_000870; -.
DR GeneID; 81477855; -.
DR KEGG; cgz:M787_000870; -.
DR eggNOG; COG1530; Bacteria.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000019147; 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 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..132
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 510 AA; 59037 MW; ED519DD8D7ADC021 CRC64;
MENDILLNIE SKEIRYAHLK NGQLFDLIIE RKKVRQLKGN IYRGRVTNIL RNIQSAFINI
DERENGFIHI SDVLENSKKF EQMFDMDFDV LPKASEEQAE APIEELLKLD SPVLVQVVKE
PIGTKGARLT SNISIPGRYL VLLPNSPHRG VSRKIEDPHM RDQLKQLIRS FEMPQDMGLI
CRTASVLAST EALINEAHDL LSTWKGILEK FYATDQPCLL YEETDILKKA VITCIDKNYK
RLLVDDYTTY QKCKRMVKKY SPDSSVKIEY YRDSIPMFER FNIEKEIDKA TKRKIWLSSG
GYLFFDKTEA MHTIDVNSGR STQLESGVEE TLVQINLEAA EEIARQLRLR NIGGLVIIDF
IDMKSRKNQR RVLERLKEHM KYDAARCTIL SMSEFGLVEM TRQRNRESLM QTLFTTCPYC
SGNAIIKTPE SVVIEIERAM KKVINHKEHK HLCLVVHPEI ASYMKQEKND DELINLAKQL
KAKLQINTSD SLHLNHYQFF SLVTGESVEL
//
