ID   RNG_HAEIN               Reviewed;         491 AA.
AC   P45175;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Ribonuclease G;
DE            Short=RNase G;
DE            EC=3.1.26.-;
GN   Name=rng; OrderedLocusNames=HI_1353;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: An endonuclease that acts in the processing of the 5'-end of
CC       16S rRNA and 23S rRNA. It prefers 5'-monophosphorylated substrates and
CC       cleaves single-stranded sites rich in A and U residues; contributes to
CC       tRNA processing and mRNA turnover. {ECO:0000250|UniProtKB:P0A9J0}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P21513};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513};
CC   -!- SUBUNIT: Homodimer, in equilibrium with possible higher multimers.
CC       {ECO:0000250|UniProtKB:P0A9J0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J0}.
CC   -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC23000.1; -; Genomic_DNA.
DR   PIR; F64118; F64118.
DR   RefSeq; NP_439504.1; NC_000907.1.
DR   RefSeq; WP_010869189.1; NC_000907.1.
DR   AlphaFoldDB; P45175; -.
DR   SMR; P45175; -.
DR   STRING; 71421.HI_1353; -.
DR   PRIDE; P45175; -.
DR   EnsemblBacteria; AAC23000; AAC23000; HI_1353.
DR   KEGG; hin:HI_1353; -.
DR   PATRIC; fig|71421.8.peg.1406; -.
DR   eggNOG; COG1530; Bacteria.
DR   HOGENOM; CLU_003468_5_3_6; -.
DR   OMA; TKGPRIS; -.
DR   PhylomeDB; P45175; -.
DR   BioCyc; HINF71421:G1GJ1-1378-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 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; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR30001; PTHR30001; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00757; RNaseEG; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cytoplasm; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Reference proteome; RNA-binding; rRNA processing;
KW   rRNA-binding; tRNA processing; tRNA-binding.
FT   CHAIN           1..491
FT                   /note="Ribonuclease G"
FT                   /id="PRO_0000097384"
FT   DOMAIN          40..129
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
FT   BINDING         348
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
SQ   SEQUENCE   491 AA;  55928 MW;  3CFD0E9ACB39FA37 CRC64;
     MDAVELLMNV TPNETRIALV ETGMLREVHI ERQAKRGIVG NIYKGRVTRV LPGMQSAFVD
     IGLEKAAFLH AADIVSHTEC VDENEQKQFK VKSISELVRE GQDIVVQVVK EPLGTKGARL
     TTDITLPSRH LVFMPENSHV GVSQRIESEE ERARLKALVE PFCDELGGFI IRTATEGASE
     EELRQDAEFL KRLWRKVLER KSKYPTKSKI YGEPALPQRI LRDFIGTNLE KIRIDSKLCF
     GEVKEFTDEF MPELSDKLVL YSGNQPIFDV YGVENAIQTA LDKRVNLKSG GYLIIEQTEA
     MTTIDINTGA FVGHRNLEET IFNTNIEATK AIAHELQLRN LGGIIIIDFI DMQTDEHRNR
     VLQSLCDALS KDRMKTNVNG FTQLGLVEMT RKRTRESLEH VLCDECPTCH GRGRVKTVET
     VCYEIMREII RVYHLFSSEQ FVVYASPAVS EYLINEESHG LLPEVEMFIG KRVKVKTEQF
     YNQEQFDVVV M