ID   RNY_DESPS               Reviewed;         521 AA.
AC   Q6AJ81;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=DP2870;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG37599.1; -; Genomic_DNA.
DR   RefSeq; WP_011190111.1; NC_006138.1.
DR   AlphaFoldDB; Q6AJ81; -.
DR   SMR; Q6AJ81; -.
DR   STRING; 177439.DP2870; -.
DR   EnsemblBacteria; CAG37599; CAG37599; DP2870.
DR   KEGG; dps:DP2870; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_7; -.
DR   OMA; PHAILGM; -.
DR   OrthoDB; 1012190at2; -.
DR   Proteomes; UP000000602; 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..521
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344865"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          211..271
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          337..430
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   521 AA;  58590 MW;  5774652DFC4EECD2 CRC64;
     MFFIEHPFVY LGLDLIVGCL IGFFLRKQLV ERQQQNIQAQ SKQIIENAII DAEQLKKEAL
     LQSKEEVYQI KQSLEAEVKL ERDDLKDEHR QLKKQRDNIK RENERFEKRQ SRHVVAEKAL
     ERRLREVDVK HEEADNEILK QRDELARIAG ITQDEAKKLL MESIESEAQM DAAKRLSKIE
     NEMKLEADRK ARSILALAIC RYAGDYVADK TVSMVPLPSD EMKGRIIGRE GRNIRAIEAA
     TGIDIIIDDT PEAVILSGFN PVRREVARLA LIQLISDGRI HPGRIEEVVE KVSKELDEVM
     CEAGEQATFD VGAHGVHVEL IKLLGRLRYR TSYGQNVLQH SLEVAFLCGI MAAELGIDVK
     MAKRAGLLHD IGKAVDHEVE GSHAVIGRDL AKKYGEPDEI VYAIGAHHAD QPPKSVLDIL
     VQAADALSGA RPGARKEMLQ SYVKRLEDLE AIANKFPGVD KSYAIQAGRD LRIIADAQKI
     SDAEATLLSR NIAASIEEKL TYPGQIRVTV IRETRSVEYA K