ID   RNY_MALP2               Reviewed;         469 AA.
AC   Q8EVM0;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, 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};
GN   Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; OrderedLocusNames=MYPE5440;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC44333.1; -; Genomic_DNA.
DR   RefSeq; WP_011077366.1; NC_004432.1.
DR   AlphaFoldDB; Q8EVM0; -.
DR   SMR; Q8EVM0; -.
DR   STRING; 272633.26454003; -.
DR   EnsemblBacteria; BAC44333; BAC44333; BAC44333.
DR   KEGG; mpe:MYPE5440; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_0_0_14; -.
DR   OrthoDB; 1012190at2; -.
DR   Proteomes; UP000002522; 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   PANTHER; PTHR12826:SF15; PTHR12826:SF15; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   TIGRFAMs; TIGR00277; HDIG; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease;
KW   Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..469
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000163783"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          149..209
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          276..369
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   469 AA;  54165 MW;  5596E1BEDB05187A CRC64;
     MQQNTVTLIL VGVIIFLFIS LFFYVIYSFV QKKKNRNFKQ IKIQPKKNNK ITPTSDQKLK
     ADEFISIINK KREILNHQRA DYLKIKETQE SYQQLQEVIS EYQKKLNLEK IKLIDQMEKE
     IKDNLNEKAV YYMINAMEQH AEDIISSKFS FTIKLENEGM KGKIIGKDGR NKRHFEQTTK
     TDLIIEPNMP AITISSPNPI RREKAKRTME KLLETKNMDI AKISLFYKEV EEGFEQTCYE
     IGKDALENKL HIFDIDKKMY PIVGQLNFRT SYSQNVLLHC VEAAVLAANI AQKLNIDPIK
     AKKAAFFHDI GKAVDFEIDN DHVNSGVELA KKFNFEDYII NAIESHHNKV SPKTVYAALV
     KVVDKLSASR PGARFVSNDE YFKRIEELEK ICKSFEGVSD AYVIKSGREI EVIIDPSLVS
     DDECKILIKD IKFKLEDSDL VNKQPIQITL IRKFTQSITT LGSASRLRT