ID   RNY_DESRM               Reviewed;         512 AA.
AC   A4J5T7;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Dred_1919;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) 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; CP000612; ABO50440.1; -; Genomic_DNA.
DR   RefSeq; WP_011878251.1; NC_009253.1.
DR   AlphaFoldDB; A4J5T7; -.
DR   SMR; A4J5T7; -.
DR   STRING; 349161.Dred_1919; -.
DR   PRIDE; A4J5T7; -.
DR   EnsemblBacteria; ABO50440; ABO50440; Dred_1919.
DR   KEGG; drm:Dred_1919; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   OrthoDB; 1012190at2; -.
DR   Proteomes; UP000001556; 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..512
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344866"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          202..265
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          328..421
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   512 AA;  57724 MW;  EEB0FFA69084330E CRC64;
     MEFQIILVVI ISALVGLVIG FFIRKNIAEG KITSAEAQAK RILEEAEKNA EGKKREAIVM
     AKEEVLKLRN EMEREIRDRR NELQRLERRL LQKEETLDRK MDSMEKKEES LSRKEADIEN
     TKAELTNVLN RQLAELERVS GLSSEEARQI LLNDVEKELQ HDMAVMIKDF ENRAKEEADK
     KARDIISSAI QRCAADHVAE ATVAVIPLPN DEMKGRIIGR EGRNIRAFET LTGIDLIIDD
     TPEAVILSGF DPIRREVARL ALERLISDGR IHPARIEEMV EKAQKDVEVQ IREAGEQATF
     ETGVHGLHPE LVKLLGRLKF RTSYGQNVLK HSIEVCHLAG LMAAELGIDV KLAKRAGLLH
     DIGKAVDHEV EGPHVAIGVN LCQKYKESPE VIHAIAAHHG DEEPRTIEAV LVQAADAISA
     ARPGARRETL ESYIKRLQKL EEIAGTFEGV EKSFAIQAGR EIRIMVKPDK IDDLAAIRLV
     RDIAKKIENE LDYPGQIKVI IIRETRYVEY AK