ID   RNY_LISMO               Reviewed;         520 AA.
AC   P0DJP2; P0A4Q6; Q9L738;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 52.
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=lmo1399;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL591979; CAC99477.1; -; Genomic_DNA.
DR   PIR; AG1249; AG1249.
DR   RefSeq; NP_464924.1; NC_003210.1.
DR   RefSeq; WP_003721904.1; NZ_CP023861.1.
DR   AlphaFoldDB; P0DJP2; -.
DR   SMR; P0DJP2; -.
DR   STRING; 169963.lmo1399; -.
DR   PaxDb; P0DJP2; -.
DR   EnsemblBacteria; CAC99477; CAC99477; CAC99477.
DR   GeneID; 61170453; -.
DR   GeneID; 67410849; -.
DR   GeneID; 984906; -.
DR   KEGG; lmo:lmo1399; -.
DR   PATRIC; fig|169963.11.peg.1438; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   PhylomeDB; P0DJP2; -.
DR   BioCyc; LMON169963:LMO1399-MON; -.
DR   Proteomes; UP000000817; 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..520
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000163780"
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