RNY_LIGS1
ID RNY_LIGS1 Reviewed; 521 AA.
AC Q1WT14;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=LSL_1129;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99937.1; -; Genomic_DNA.
DR RefSeq; WP_011476179.1; NC_007929.1.
DR RefSeq; YP_536020.1; NC_007929.1.
DR AlphaFoldDB; Q1WT14; -.
DR SMR; Q1WT14; -.
DR STRING; 362948.LSL_1129; -.
DR EnsemblBacteria; ABD99937; ABD99937; LSL_1129.
DR KEGG; lsl:LSL_1129; -.
DR PATRIC; fig|362948.14.peg.1202; -.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000006559; 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..521
FT /note="Ribonuclease Y"
FT /id="PRO_0000344898"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 211..274
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 337..430
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 521 AA; 58290 MW; A003542E91CB1EFE CRC64;
MIIAITILAI AIATLVIGFA LGVAYRKRSY EQALDVATQT ATGIIETAKK EAAASKKEAI
IEAKEENHRY RSEIESELKE RRSEIQRQEN RLLQREEILD RKDTALDKRE DVLEKKEAQL
DSDQKVVTKQ KEQASLLVKE QQDKLEEIAA LTRPEAKELI LNETKEELIH ERAVMIKESE
EETKATVDRK AKSLIAQAIQ RSAADMVSET TVSVVNLPND EMKGRIIGRE GRNIRTLETL
TGIDLIIDDT PEAVVLSGFD PVRREIAKMA LERLIQDGRI HPARIEEMVD KATKDMDAKI
REIGEEVIFD LGIHSMHPDL IKTIGRLNYR TSYGQNVLNH SIEVAKISGI LAAELGEDVI
LAKRAGLLHD IGKAVDHEIE GSHVELGVEL TKKYNESETV VNTIASHHGD TEPKSVIAVL
VAAADAISAA RPGARSESLE NYIHRLEKLE DISNEFKGVQ KSYAIQAGRE VRVIVQPNEV
SDLEATVLAR DIRMKIEDEL EYPGHIKVTV IRETRAVEYA K