ID   RNY2_BDEBA              Reviewed;         527 AA.
AC   Q6ML54;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Ribonuclease Y 2 {ECO:0000255|HAMAP-Rule:MF_00335};
DE            Short=RNase Y 2 {ECO:0000255|HAMAP-Rule:MF_00335};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00335};
GN   Name=rny2 {ECO:0000255|HAMAP-Rule:MF_00335}; OrderedLocusNames=Bd2166;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(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; BX842651; CAE80003.1; -; Genomic_DNA.
DR   RefSeq; WP_011164605.1; NC_005363.1.
DR   AlphaFoldDB; Q6ML54; -.
DR   SMR; Q6ML54; -.
DR   STRING; 264462.Bd2166; -.
DR   EnsemblBacteria; CAE80003; CAE80003; Bd2166.
DR   KEGG; bba:Bd2166; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_7; -.
DR   OMA; THVELGV; -.
DR   OrthoDB; 1012190at2; -.
DR   Proteomes; UP000008080; 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; IPR017705; Ribonuclease_Y.
DR   InterPro; IPR022711; RNase_Y_N.
DR   PANTHER; PTHR12826:SF15; PTHR12826:SF15; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF12072; RNase_Y_N; 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..527
FT                   /note="Ribonuclease Y 2"
FT                   /id="PRO_0000344828"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          339..432
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   527 AA;  59273 MW;  E43CE541C9D5FE63 CRC64;
     MIAMIATAII GIVAGGGLGW ALHKFFRART LRLAREEAQD ILDEANEVVE LRNLEERERI
     QEIEMELWTK VEPEMLKSEG RIEDLQEVAN ERKAKADAIV QEEKKKLQDR EADVKVQEQA
     LRGQEAELGK LKEAQKALNQ ELVQKLTERL GTSAEEFKTQ LKNQMEEESR RRAARMIQET
     EADTKEHAES EAKRILSLVI DRFARPYCAE RGIGAVNFPD AHIRKLFCDP AGNNIKAVQD
     ACGCDIIVEE GMEMVGVAGF DPVRRELTRR TLERIFKEKK NINPDFIRKI AENQKKELFK
     NIKHDGDSLA KELKLEGLNA EIRQMMGSLR YRYSFTQNQY FHCGEVGWLA GLMAAELGID
     IKKARRVGML HDIGKSMDHT VEGGHAVIGA DFIAARGEAP DVVHAVKAHH FDEQPSTDHA
     FLVIAADAVS GARPGARRST IESYNQKVSE LQDIARSFPG VTDCFVLSGG RECRVMVNGK
     KVDDTQAMDL SRKIAARIEE ECNYPGSIKV VVVRETVVTE QTRKELA