ID   RNY_SYNWW               Reviewed;         515 AA.
AC   Q0AXJ1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Swol_1254;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68563.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0AXJ1; -.
DR   SMR; Q0AXJ1; -.
DR   STRING; 335541.Swol_1254; -.
DR   PRIDE; Q0AXJ1; -.
DR   EnsemblBacteria; ABI68563; ABI68563; Swol_1254.
DR   KEGG; swo:Swol_1254; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   Proteomes; UP000001968; 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..515
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344959"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          205..290
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          331..424
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   515 AA;  58197 MW;  19F6BFD21581682A CRC64;
     MIEIDLTSFV IITLSLAVGL TGGYYGRRFL AESRIRTAEE EVAKMLDEAA KEVEAKKKEI
     LLEAKDEIHR NRQDAEKDIR ERRRELDRVE RRIIQKEEMI DKKTENMEKK EQVLLEKEKE
     TEKTQQDLQM VLSQQLKELE RLSGLSSEEA KELLLYNVSQ QIRQETAVLI RNIENEAKEE
     ADKKAKNIVS LAIQKCAADV VSESTVSVVP LPNDEMKGRI IGREGRNIRT FEALSGVDLI
     IDDTPEAVIL SSFDPIRREV ARVALGNLVS DGRIHPARIE EMVEKARKEI EQEIREVGEQ
     AAFEVGVHGL HPELIKLLGR LKYRTSYGQN VLRHSVEVAH LAGIMAAELE VDIMLAKRSG
     LLHDIGKAVD HEVSGPHVEI GVDLAKKYRE NKDVIHGIEA HHGDIEPETV EAVLVQAADA
     ISASRPGARR ETLETYIKRL EKLENVAESF SGVDRTFAIQ AGREIRIIVK PEEIDDLHSI
     NLARDIAAKI EQDLDYPGQI KVVVIRETRS VEYAK