ID   RNY_CUTAK               Reviewed;         542 AA.
AC   Q6A900;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 117.
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=PPA1014;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT82766.1; -; Genomic_DNA.
DR   RefSeq; WP_002515617.1; NC_006085.1.
DR   AlphaFoldDB; Q6A900; -.
DR   SMR; Q6A900; -.
DR   STRING; 267747.PPA1014; -.
DR   PRIDE; Q6A900; -.
DR   EnsemblBacteria; AAT82766; AAT82766; PPA1014.
DR   KEGG; pac:PPA1014; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_11; -.
DR   OMA; PHAILGM; -.
DR   Proteomes; UP000000603; 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   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..542
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344924"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          229..289
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          355..449
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          52..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  59585 MW;  AD0986080EB799C6 CRC64;
     MLIALIAVSV LAVAAIIGSL ADRRAIGRRA ERAESERDVK ALELSRSQER LSRASQDLAD
     SRKDVAKARA ELESSRTRAS DEARRADNAD QARRSAEALL EINRRSVEEL TERDHRLQEA
     RRHLEEGLDK IEQDRLELAE RSSQLDERDA ELDRRHGQIV TELERVAGMS LDEARDELVE
     HLGREARVFA ENSARAIVTE ATASAEAKAR HIVAEVIQRC SSEMVADTVV SVVPLPSNEM
     KGRVIGREGR NIRTFEQVTG VTVIIDDTPE IVLLSCFDPM RREVARQALT DLVEDGRIHP
     ISIERAHQRA VDRIEDMCLD AAADALSRAG IDDIDDRLLP ILGSLRFRTS YGQQVLDHCV
     ECARLAANLA AEIGADIEIC RRAAFLHDLG KSLTPGVEGS SHAAIGAELA RRYGESEEVI
     HAIAAHHDEI DPVSVTDFIV KAADAISAAR PGARRESLEA HVRRMDTIEE IATSFPGVVR
     AFALQAGREM QILVDPGAVD DHQASRLARQ IALAIGEQVT VPGRTRVTVI RSFQAIETVG
     DA