ID   RNY_MAGMM               Reviewed;         516 AA.
AC   A0L5J3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=Mmc1_0715;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK43236.1; -; Genomic_DNA.
DR   RefSeq; WP_011712396.1; NC_008576.1.
DR   AlphaFoldDB; A0L5J3; -.
DR   SMR; A0L5J3; -.
DR   STRING; 156889.Mmc1_0715; -.
DR   EnsemblBacteria; ABK43236; ABK43236; Mmc1_0715.
DR   KEGG; mgm:Mmc1_0715; -.
DR   eggNOG; COG1196; Bacteria.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_5; -.
DR   OMA; PHAILGM; -.
DR   OrthoDB; 1012190at2; -.
DR   Proteomes; UP000002586; 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;
KW   Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..516
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344905"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          206..269
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          332..425
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          98..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  58431 MW;  F5A39B6C3AEE37FE CRC64;
     MDILLLMVGL LLGAGGVFVM LRNQSNQALV ERDARIDLLQ KQAQEQVRNA AKEVELAMKG
     ERIQIREELE SELRSRREEV DSHQVRLDKR ESQLDRKIEQ VDRRDQELDQ RRGQLDKEQK
     KVEERQQHFE RLIVDADKKL EEIAGLTRDE AKSRIQAELV DRARHEASRQ LKQIEDDTRA
     QAQKKAQEVI CSAIQRFAGE FVVDRTVSVV QLPTDEMKGR IIGREGRNIR ALEAATGCDL
     IIDDTPEAVV ISGFNPVRRQ VARRALEELV GDGRIHPARI EEVVRKARKV VSQEIREAGE
     QAVYDVGISN MHPEIIKLLG TLKFRTSYTQ NVLAHSVEVA HFAGIMAEEM GLDGKLARRC
     GLLHDIGKAV DHDNPGSHAV LGGELCKKYK EDDTVTNAVW SHHFDIEPNS VYGPLTNAAD
     ALSAARPGAR RENVETYIRR LEELERIATE FKGVEKAYAI QAGRELRVMV AYDRVNDEGS
     MLLAREIAQQ VESEMTYPGE IKVTVIREMR ASEIAR