RNC_MYCGF
ID RNC_MYCGF Reviewed; 655 AA.
AC D3FI09;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=MGF_2505;
OS Mycoplasma gallisepticum (strain F) (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=708616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F;
RX PubMed=20123709; DOI=10.1128/iai.01172-09;
RA Szczepanek S.M., Tulman E.R., Gorton T.S., Liao X., Lu Z., Zinski J.,
RA Aziz F., Frasca S. Jr., Kutish G.F., Geary S.J.;
RT "Comparative genomic analyses of attenuated strains of Mycoplasma
RT gallisepticum.";
RL Infect. Immun. 78:1760-1771(2010).
CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC primary rRNA transcript to yield the immediate precursors to the large
CC and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when
CC they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA
CC of type II CRISPR loci if present in the organism (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR EMBL; CP001873; ADC31272.1; -; Genomic_DNA.
DR RefSeq; WP_011113742.1; NC_017503.1.
DR AlphaFoldDB; D3FI09; -.
DR SMR; D3FI09; -.
DR KEGG; mgf:MGF_2505; -.
DR PATRIC; fig|708616.3.peg.339; -.
DR HOGENOM; CLU_418462_0_0_14; -.
DR OMA; EHKNINT; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; -; 1.
DR HAMAP; MF_00104; RNase_III; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF14622; Ribonucleas_3_3; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR TIGRFAMs; TIGR02191; RNaseIII; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Nuclease; RNA-binding; rRNA processing; rRNA-binding;
KW tRNA processing.
FT CHAIN 1..655
FT /note="Ribonuclease 3"
FT /id="PRO_0000416606"
FT DOMAIN 432..556
FT /note="RNase III"
FT DOMAIN 582..649
FT /note="DRBM"
FT REGION 1..400
FT /note="Unknown"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..655
FT /note="RNase 3"
FT COMPBIAS 19..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 476
FT /evidence="ECO:0000255"
FT ACT_SITE 545
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 655 AA; 75387 MW; BABBEDB7BAF8E4BE CRC64;
MENLEKNTKK KIKKPNNFKK NNKDKTEELK DKPTPRMFKM TPKSSKFLHQ LGVTGRKHTE
KPVPLNDPDY EKKIREIQAK EAKKIRSDEV VNNNSKKQNN NKQAKKKANK NKKQKGNNNN
FQNNKKPENW KQKPAANNQV KAIPNSEKST AKTAINLIIK RTFETLKQNN LIAPNLKQNP
NKKDKPQQPN VAAKNNNQKE VKKPYNNFVN NQKNHNKNNA GNKGDNKQPT KPLNQSKLSK
STIVELPFTP NFTSNQPKPT QKEDSKKVKA KKAENSQPQE SNKQVKKLEV KTNQQKQDQT
KKKQPKENKN QQIKAVNLNN NQQKTNNNNQ KNSVDKSEND NNKKKSEANQ KQENLNPNNN
NKKKEDSKNE SNNIPLINKN ISDQQIVKIS NYIKDNYPVI YADLKEKNRL GFNSNLDDDK
LIVYANYEAK DLELLLKKFK VVTNNIGLYE EALTHNSYAN EMHLKYNYQR LEFLGDAIIN
KIVAEYLFNH SDSSEGEMTK DRIKIIQSNT LIKAATQLEL INYIRVGEGL KIAPLSPKIL
EDIFEAFIGA MYLDQGEYAV RKILNDTIIG YYQKGQLTEN TDYKSIFQEI IHSTGLNMKI
HYERTYDRQK NLHTVSLYAG GIMYGEGKDS STHKAEIKAA KEAISKFRGL LKLEK
