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Database: UniProt
Entry: RNY_BACCN
LinkDB: RNY_BACCN
Original site: RNY_BACCN 
ID   RNY_BACCN               Reviewed;         520 AA.
AC   A7GRA8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=Bcer98_2430;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS22666.1; -; Genomic_DNA.
DR   RefSeq; WP_012094870.1; NC_009674.1.
DR   AlphaFoldDB; A7GRA8; -.
DR   SMR; A7GRA8; -.
DR   STRING; 315749.Bcer98_2430; -.
DR   GeneID; 56417970; -.
DR   KEGG; bcy:Bcer98_2430; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OrthoDB; 9803205at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd22431; KH-I_RNaseY; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 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   NCBIfam; TIGR00277; HDIG; 1.
DR   NCBIfam; TIGR03319; RNase_Y; 1.
DR   PANTHER; PTHR12826; RIBONUCLEASE Y; 1.
DR   PANTHER; PTHR12826:SF15; RIBONUCLEASE Y; 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; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 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_0000344817"
FT   TRANSMEM        4..24
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"
SQ   SEQUENCE   520 AA;  58691 MW;  6175E914A8B745AF CRC64;
     MSNTVWILIS ILLATVGAVV GFFVRKSIAE AKINGAANEA KRILDDANRE AEALKKEALL
     EAKDEIHTLR TEAELEIRDR RSELQKQENR LMQKEENLDR KDETLDKREQ MLEKKEESLV
     ARQQQIEELE SKVGELVQKQ QTELERISNL TREQAKSIIL GKVENELSHE IAAMVKESEV
     RAKEEADKKA KEILSLAMQR CAADHVAETT VSVVNLPNDE MKGRIIGREG RNIRTLETLT
     GIDLIIDDTP EAVILSGFDP IRRETARIAL DKLVQDGRIH PARIEEMVEK SRREVDEYIR
     EVGEQTTFEV GIHGLHPDLI KILGRLKYRT SYGQNVLKHS MEVAYLTGLM AAELGEDEKL
     ARRAGLLHDI GKAIDHEVEG SHVEIGVELA TKYKEHPVVI NSIASHHGDT EPTSIIAVLV
     AAADALSAAR PGARSETLEN YIRRLEKLEE ISESYEGVEK SFAIQAGREV RILVKPDTID
     DLEAHRLARD IRKRIENELD YPGHIKVTVI RETRAVEYAK
//
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