RNY_STAES
ID RNY_STAES Reviewed; 519 AA.
AC Q8CSS7;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 111.
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}; Synonyms=cvfA;
GN OrderedLocusNames=SE_0964;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04561.1; -; Genomic_DNA.
DR RefSeq; NP_764519.1; NC_004461.1.
DR RefSeq; WP_001829512.1; NZ_WBME01000001.1.
DR AlphaFoldDB; Q8CSS7; -.
DR STRING; 176280.SE_0964; -.
DR DNASU; 1057669; -.
DR EnsemblBacteria; AAO04561; AAO04561; SE_0964.
DR GeneID; 50018902; -.
DR KEGG; sep:SE_0964; -.
DR PATRIC; fig|176280.10.peg.938; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000001411; 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; RNA-binding;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..519
FT /note="Ribonuclease Y"
FT /id="PRO_0000163792"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 209..269
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 335..428
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 519 AA; 58697 MW; F8B73CCD5EFE0C10 CRC64;
MNLLSLLLIL LGIILGVVVG YIVARNLLHQ KQVQARQTAD DIVSYANKEA DNIKKEKLLE
AKEENQILKE QAENELRERR GELQRQETRL LQKEENLDRK SDLLDKKDEI LEQKESKLEE
RQQQVDAKES SVQTLIMKHE QELERISGLT QEEAVKEQLQ RVEEELSQDI AILVKEKEKE
AKEKVDKTAK ELLATTVQRL AAEHTTESTV SVVNLPNDEM KGRIIGREGR NIRTLETLTG
IDLIIDDTPE AVILSGFDPI RREIARTALV NLVSDGRIHP GRIEDMVEKA RKEVDDIIRD
AGEQATFEIN VHNMHPDLVK ILGRLNYRTS YGQNVLKHSI EVAHLSGMLA AELGEDVTLA
KRAGLLHDVG KAIDHEVEGS HVEIGVELAK KYNENNIIIN AIHSHHGDVE PTSIISILVA
AADALSAARP GARKETLENY IRRLERLETL SESYDGVEKA FAIQAGREIR VVVSPEEIDD
LKSYRLARDI KNQIEEELQY PGHIKVTVVR ETRAIEYAK