RNY_STAA3
ID RNY_STAA3 Reviewed; 519 AA.
AC Q2FHF2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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};
DE AltName: Full=Conserved virulence factor A;
GN Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; Synonyms=cvfA;
GN OrderedLocusNames=SAUSA300_1179;
OS Staphylococcus aureus (strain USA300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=367830;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300;
RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA Perdreau-Remington F.;
RT "Complete genome sequence of USA300, an epidemic clone of community-
RT acquired meticillin-resistant Staphylococcus aureus.";
RL Lancet 367:731-739(2006).
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; CP000255; ABD21731.1; -; Genomic_DNA.
DR RefSeq; WP_001050913.1; NZ_CP027476.1.
DR AlphaFoldDB; Q2FHF2; -.
DR SMR; Q2FHF2; -.
DR PRIDE; Q2FHF2; -.
DR EnsemblBacteria; ABD21731; ABD21731; SAUSA300_1179.
DR KEGG; saa:SAUSA300_1179; -.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000001939; 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_0000294067"
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; 58512 MW; 076DE375A553FFA3 CRC64;
MNLLSLLLIL LGIILGVVGG YVVARNLLLQ KQSQARQTAE DIVNQAHKEA DNIKKEKLLE
AKEENQILRE QTEAELRERR SELQRQETRL LQKEENLERK SDLLDKKDEI LEQKESKIEE
KQQQVDAKES SVQTLIMKHE QELERISGLT QEEAINEQLQ RVEEELSQDI AVLVKEKEKE
AKEKVDKTAK ELLATAVQRL AADHTSESTV SVVNLPNDEM KGRIIGREGR NIRTLETLTG
IDLIIDDTPE AVILSGFDPI RREIARTALV NLVSDGRIHP GRIEDMVEKA RKEVDDIIRE
AGEQATFEVN AHNMHPDLVK IVGRLNYRTS YGQNVLKHSI EVAHLASMLA AELGEDETLA
KRAGLLHDVG KAIDHEVEGS HVEIGVELAK KYGENETVIN AIHSHHGDVE PTSIISILVA
AADALSAARP GARKETLENY IRRLERLETL SESYDGVEKA FAIQAGREIR VIVSPEEIDD
LKSYRLARDI KNQIEDELQY PGHIKVTVVR ETRAVEYAK