ID   RNY_PELTS               Reviewed;         498 AA.
AC   A5D2N5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=PTH_1302;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
CC   -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC       {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; AP009389; BAF59483.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D2N5; -.
DR   SMR; A5D2N5; -.
DR   STRING; 370438.PTH_1302; -.
DR   EnsemblBacteria; BAF59483; BAF59483; PTH_1302.
DR   KEGG; pth:PTH_1302; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_0_0_9; -.
DR   OMA; PHAILGM; -.
DR   Proteomes; UP000006556; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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   Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding.
FT   CHAIN           1..498
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344921"
FT   DOMAIN          188..273
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          314..407
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   498 AA;  56041 MW;  CBCB7F5AF610DFF3 CRC64;
     MAFCAGYFLR KYLAEAKIAS AEAQAKKILE EAEKEAEAKK REAILEAKEE VLKLRNDMER
     ENRERRLELQ RLERRLVQKE ETLDRKVDAI EKKEDALNRK EAEIDAIKAQ LNEIYKKQLS
     ELERISGMTS EEAKQALLSD IEKEIQHEAA MLIKEIESKA REEGEKRARD IISLAIQRCA
     ADHVAEATVS VIPLPSDEMK GRIIGREGRN IRAFETLTGI DLIIDDTPEA VILSGFDPIR
     REVARIALEK LIVDGRIHPA RIEEMVEKAQ KEVNVQIRDA GEQAVFETGV HGLHPELVTL
     LGRLKFRTSY GQNVLKHSIE VAHLAGLMAS EIGVDIQMAK RAGLLHDIGK AVDHEVEGPH
     VAIGIDLAKK YREAQEIIHA IAAHHGDEEP KSIIAVLVQA ADAISAARPG ARRETLEAYI
     KRLTKLEEIA NSFDGVEKSY AIQAGREVRI MVKPEKIDDL GAIRLVREIT KKIENELDYP
     GQIKVVIIRE TRVVEYAK