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 25-MAY-2022, entry version 94.
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; Firmicutes; 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 EnsemblBacteria; ABS22666; ABS22666; Bcer98_2430.
DR GeneID; 56417970; -.
DR KEGG; bcy:Bcer98_2430; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000002300; 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_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