ID   RNY_STRSV               Reviewed;         537 AA.
AC   A3CPX8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=SSA_1852;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN45233.1; -; Genomic_DNA.
DR   RefSeq; WP_002893506.1; NC_009009.1.
DR   RefSeq; YP_001035783.1; NC_009009.1.
DR   AlphaFoldDB; A3CPX8; -.
DR   SMR; A3CPX8; -.
DR   STRING; 388919.SSA_1852; -.
DR   EnsemblBacteria; ABN45233; ABN45233; SSA_1852.
DR   GeneID; 61535375; -.
DR   KEGG; ssa:SSA_1852; -.
DR   PATRIC; fig|388919.9.peg.1757; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   OrthoDB; 1012190at2; -.
DR   Proteomes; UP000002148; 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..537
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344949"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          227..287
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          353..446
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          112..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  60272 MW;  5FEF01F5D0E18555 CRC64;
     MDLFPIIMSV FAAIIGLVIG YVSVSAKMKS SKEAAELTLL NAEQEATNLR GQAEREADLI
     VKEAKRETSS LKKEALLEAK EEARKYREQV DAEFKSERQE LKQIESRLTE RASTLDRKDD
     NLSNKEKALE QKEQSLSDKS KHIDAREEQV AELEKQKAAE LERVASLSQT EARDIILTQT
     EDKLSKEIAT RIRDAEQDIK ERSDKVAKNI LVQAMQRIAG DYVAEQTNST VHLPDDSMKG
     RIIGREGRNI RTFESLTGID VIIDDTPEVV TLSGFDPIRR EIARMTMEAL LKDGRIHPAR
     IEELVEKNRL EIDNRIREYG EAAAYEIGAP NLHPDLMKIM GRLQFRTSYG QNVLRHSIEV
     AKLSGIIAAE LGENANLARR AGFLHDIGKS IDREVEGSHV EIGTELARKY KEHPVVVNTI
     ASHHGDVEAE SVIAVIVAAA DALSAARPGA RSESLESYIK RLQDLEEIAN SFKGVKNSFA
     LQAGREIRIM VQPDKIKDDK ITILAHDVRE KIENNLEYPG NIKVTVIREM RAVDYAK