ID   RNY_STRMU               Reviewed;         535 AA.
AC   Q8DVK7;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Ribonuclease Y {ECO:0000255|HAMAP-Rule:MF_00335};
DE            Short=RNase Y {ECO:0000255|HAMAP-Rule:MF_00335};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00335};
GN   Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; OrderedLocusNames=SMU_475;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC       {ECO:0000255|HAMAP-Rule:MF_00335}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00335};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00335}.
CC   -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000255|HAMAP-
CC       Rule:MF_00335}.
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DR   EMBL; AE014133; AAN58223.1; -; Genomic_DNA.
DR   RefSeq; NP_720917.1; NC_004350.2.
DR   RefSeq; WP_002263046.1; NC_004350.2.
DR   AlphaFoldDB; Q8DVK7; -.
DR   STRING; 210007.SMU_475; -.
DR   PRIDE; Q8DVK7; -.
DR   DNASU; 1027977; -.
DR   EnsemblBacteria; AAN58223; AAN58223; SMU_475.
DR   GeneID; 66818051; -.
DR   KEGG; smu:SMU_475; -.
DR   PATRIC; fig|210007.7.peg.417; -.
DR   eggNOG; COG1418; Bacteria.
DR   eggNOG; COG4372; Bacteria.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   PhylomeDB; Q8DVK7; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   HAMAP; MF_00335; RNase_Y; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR006675; HDIG_dom.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR017705; Ribonuclease_Y.
DR   InterPro; IPR022711; RNase_Y_N.
DR   PANTHER; PTHR12826:SF15; PTHR12826:SF15; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF12072; RNase_Y_N; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   TIGRFAMs; TIGR00277; HDIG; 1.
DR   TIGRFAMs; TIGR03319; RNase_Y; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease;
KW   Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..535
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000163796"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          225..285
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          351..444
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          110..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  60343 MW;  C33991D8FEBF1DC4 CRC64;
     MLNILLTLVF SLIGLVIGYA VISARLKKAK ETAELTLLNA EQDAVNARSK AEMDAEHIKK
     TAERESKAYK KELLIEAKEE ARKYREEIEK EFKSERQELK QMDARLTERA ASLDRKDENL
     SSKEQLLDSK EQSLSDKSRH IDERELQVKQ LEVKKAEELE KIASLSQEQA RGIILSETEK
     NLAHDIANRI KEAEREIKDR TDKTAKDLLA QAMQRLAGDY VAEQTITTVH LPDDSMKGRI
     IGREGRNIRT LESLTGIDII IDDTPEVVVL SGFDPIRREI ARMTLEALIQ DGRIHPARIE
     ELVEKNRLEM DNRIREYGEA AAFEIGAPNL HPDLIKLMGR LQFRTSYGQN VLRHSVEVGK
     LAGLLASELG ENVDLARRAG FLHDIGKAID REVEGSHVEI GTEFARKYKE NPVVINTIAS
     HHGDVEAQSV IAVLVAAADA LSSARPGARN ESMENYIKRL RDLEEIATSF DGVQNSYALQ
     AGREIRIMVQ PEKLSDDDVT ILAHKVREKI ENNLDYPGNI KVTVIRELRA IDYAK