ID   RNY_STRS2               Reviewed;         537 AA.
AC   A4VZM7;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=SSU98_0408;
OS   Streptococcus suis (strain 98HAH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98HAH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(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; CP000408; ABP91566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4VZM7; -.
DR   SMR; A4VZM7; -.
DR   KEGG; ssv:SSU98_0408; -.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
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; RNA-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..537
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344951"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          227..287
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          353..446
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          112..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  60539 MW;  4F3ACAB413A476D3 CRC64;
     MNIITVVVTL VSALIGLVLG YFAISLKMKS AKETAELTLL NAEQEASNVR GRAEEQAEVI
     LKTAERDRQT LKKELLLEAK EEARKYREEI AEEFKSERQE LKQIESRLTE RATSLDRKDD
     NLTNKEKTLE QKEQSLTDKA KHIDEREQEV VKLEEQKALE LERVAALSQE EAKEIILTDT
     RDKLTHEIAT RIKEAEREVK ERSDKMAKDL LAQAMQRISG EYVAEQTITS VHLPDDAMKG
     RIIGREGRNI RTFESLTGID VIIDDTPEVV VLSGFDPIRR EIARMTMETL LQDGRIHPAR
     IEELVEKHRV EMDNRIREYG EAAAYEVGAP NLHPDLIKIM GRLHFRTSYG QNVLRHSIEV
     AKLAGVLAAE LGENVNLARR AGFLHDVGKA IDREVDGSHV EIGTELAKKY KENPIVINAI
     ASHHGDVEAT STIAVIVAAA DALSAARPGS RRESMEAYIK RLQDLEEIAN SFEGIKQSYA
     IQAGREIRII VHPNKVTDDQ ITILAHDVRE KIENNLDYPG NIKITVIRET RATDVAK