ID   RNY_LISM4               Reviewed;         520 AA.
AC   G2JZ15; P0A4Q6; Q9L738;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=LMRG_00851;
OS   Listeria monocytogenes serotype 1/2a (strain 10403S).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=393133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=10403S;
RA   Wang H.W., Lee F., Yan B.S., Shaio M.F., Kuo S.C., Wang Y.M., Yao C.W.;
RT   "Construction and characterization of recA-deficient attenuated mutants of
RT   Listeria monocytogenes: cloning and sequence analysis of L. monocytogenes
RT   recA gene.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10403S;
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M.,
RA   Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D.,
RA   Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B., Chen Z.,
RA   Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L.,
RA   Lui A., MacDonald J., Mehta T., Montmayeur A., Neiman D., Park D.,
RA   Pearson M., Priest M., Richards J., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Listeria monocytogenes strain 10403S.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; AF228345; AAF34762.1; -; Genomic_DNA.
DR   EMBL; CP002002; AEO06384.1; -; Genomic_DNA.
DR   RefSeq; WP_003721904.1; NC_017544.1.
DR   AlphaFoldDB; G2JZ15; -.
DR   SMR; G2JZ15; -.
DR   EnsemblBacteria; AEO06384; AEO06384; LMRG_00851.
DR   GeneID; 61170453; -.
DR   GeneID; 67410849; -.
DR   KEGG; lmt:LMRG_00851; -.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   Proteomes; UP000001288; 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; RNA-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..520
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000419035"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          210..273
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          336..429
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          76..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  58318 MW;  E0BB35564B0CEB8A CRC64;
     MTIAITIISS LLFLIVGLVV GSLIFKSSTE KKLAAARGTA ELIVEDAKKE AETTKKEALL
     EAKEENHRLR TEIENELRGR RTETQKAENR LLQREENLDR KDTSLSKREA TLERKEESIS
     KRQQQIEEKE SKLAEMIQAE QTELERISAL SKEEAKSIIL NQVEEELTHD TAIMVKESEN
     RAKEESDKKA KNILSLAIQR CAADHVAETT VSVVTLPNDE MKGRIIGREG RNIRTLETLT
     GIDLIIDDTP EAVILSGFDP IRREIARIAL EKLVQDGRIH PARIEEMVDK ARKEVDEHIR
     EVGEQATFEV GIHSIHPDLI KILGRLRYRT SYGQNVLNHS LEVSKLAGIL AGELGEDVTL
     AKRAGLLHDI GKAIDHEIEG SHVEIGVELA TKYKENDVVI NSIASHHGDT EATSVIAVLV
     AAADALSAAR PGARSETLEN YIRRLEKLEE ISESYDGVEK SYAIQAGREV RIIVEPDTID
     DLSSYRLARD IRKRIEEELD YPGHIKVTVI RETRAVEYAK