ID   RNY_CLOBH               Reviewed;         513 AA.
AC   A5I4H8; A7G5M9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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};
GN   OrderedLocusNames=CBO2404, CLC_2250;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(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; CP000727; ABS37103.1; -; Genomic_DNA.
DR   EMBL; AM412317; CAL83950.1; -; Genomic_DNA.
DR   RefSeq; WP_011986783.1; NC_009698.1.
DR   RefSeq; YP_001254899.1; NC_009495.1.
DR   RefSeq; YP_001388094.1; NC_009698.1.
DR   AlphaFoldDB; A5I4H8; -.
DR   GeneID; 5186659; -.
DR   KEGG; cbh:CLC_2250; -.
DR   KEGG; cbo:CBO2404; -.
DR   PATRIC; fig|413999.7.peg.2380; -.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   PRO; PR:A5I4H8; -.
DR   Proteomes; UP000001986; 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..513
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344846"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          203..288
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          329..422
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   513 AA;  58113 MW;  76B163DA0696B301 CRC64;
     MGPTKYIIIA VVIIIICVIL GLYIVDKKAK EKLSEASKEA RRLKEEAERD AEAKKKEAIL
     EAKEEAHKLR AEVERENRER RNEVQRLERR IIQKEEALDK KSEALENKEE ALNKKQQKIE
     DVETHMEELH EKQRTELERI SGLTTEQAKE FLLEQVRKEV KHETAVMIKE IETKAKEEAD
     KRAREVITYA IQRCAADHVA ETTVHVVNLP NDEMKGRIIG REGRNIRTLE TLTGVDLIID
     DTPEAVILSG FDPIRREVAR IALEKLIVDG RIHPARIEEM VEKAKKEVEI SIKEEGEQAT
     FETGIHGLHI ELIRLLGRLK YRTSYGQNVL KHSIEVSHLA GLMASELGID PTLAKRVGLL
     HDIGKAVDHE VEGPHAIIGS EIAKKYRESA LVVNAIGAHH GDMEPQSLEA ILVQAADAIS
     AARPGARRET LEAYIKRLEK LEEIANECEG VEKSYAIQAG REIRIMVKPE VLDDTGCIEM
     ARNIVKQIES ELEYPGQIKV NVIRETRAIE YAK