ID   RNY_DESVV               Reviewed;         519 AA.
AC   A1VAZ2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=Dvul_0585;
OS   Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=391774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP4;
RX   PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA   Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA   He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA   Stahl D.A.;
RT   "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT   plasticity.";
RL   Environ. Microbiol. 11:2244-2252(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; CP000527; ABM27608.1; -; Genomic_DNA.
DR   RefSeq; WP_010939940.1; NC_008751.1.
DR   AlphaFoldDB; A1VAZ2; -.
DR   SMR; A1VAZ2; -.
DR   PRIDE; A1VAZ2; -.
DR   EnsemblBacteria; ABM27608; ABM27608; Dvul_0585.
DR   KEGG; dvl:Dvul_0585; -.
DR   HOGENOM; CLU_028328_1_0_7; -.
DR   OMA; PHAILGM; -.
DR   Proteomes; UP000009173; 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; IPR028987; ATP_synth_B-like_membr_sf.
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   SUPFAM; SSF81573; SSF81573; 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..519
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344869"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          209..272
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;  58247 MW;  FD8FFB1B63EE2477 CRC64;
     MGLMIFAYIA IGAVLGAGTG YLLHRYVSAK RIGDANELAK RIVEEARKEA QAQKKEILLQ
     GQDEIFNQKR ELENEFKERE RELKARDRKL EEQGERLEEK LEKATQKEHE VLAIEKELTR
     KERRLATLEE ELEGKIAEQD HRLEEVSGLT AEEARARIME EVEARTRHES AKMIRVIEME
     ARETADRKAK EILASAIQRY AGDYVGEQTV TAVTLPSEDM KGRIIGREGR NIRALEAATG
     VDLIIDDTPE TVILSAYSPL RRQVAKMALE RLIQDGRIHP ARIEDIVRKC EQELEVQVRE
     VGEQATFDAG VHGIHPDIIK LLGQLRYRTS FSQNVLQHSL EVSALCGMMA AELGMDIKKA
     KRAGLLHDIG KAVDHEVEGP HALIGADIAK KYGEGKDIIH AIAAHHEDQP PKTALAVLVQ
     AADSISGARP GARKELLENY VKRLEDLENI ATGFEGVSKV YAIQAGREIR VMVNSENVDD
     DQTYMLCKDI AAKIEKNLTY PGQIRVTVIR ERRAVGYAK