ID A0A0H4QJV5_9LACO Unreviewed; 521 AA.
AC A0A0H4QJV5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Ribonuclease Y {ECO:0000256|HAMAP-Rule:MF_00335};
DE Short=RNase Y {ECO:0000256|HAMAP-Rule:MF_00335};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00335};
GN Name=rny {ECO:0000256|HAMAP-Rule:MF_00335};
GN ORFNames=ABM34_12105 {ECO:0000313|EMBL:AKP68202.1};
OS Companilactobacillus ginsenosidimutans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1007676 {ECO:0000313|EMBL:AKP68202.1, ECO:0000313|Proteomes:UP000036106};
RN [1] {ECO:0000313|Proteomes:UP000036106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EMML 3041 {ECO:0000313|Proteomes:UP000036106};
RA Kim M.K., Im W.-T., Srinivasan S., Lee J.-J.;
RT "Lactobacillus ginsenosidimutans/EMML 3141/ whole genome sequencing.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {ECO:0000256|HAMAP-Rule:MF_00335}.
CC -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000256|HAMAP-
CC Rule:MF_00335}.
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DR EMBL; CP012034; AKP68202.1; -; Genomic_DNA.
DR RefSeq; WP_048706067.1; NZ_CP012034.1.
DR AlphaFoldDB; A0A0H4QJV5; -.
DR STRING; 1007676.ABM34_12105; -.
DR KEGG; lgn:ABM34_12105; -.
DR PATRIC; fig|1007676.4.peg.2450; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000036106; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 1.
DR CDD; cd22431; KH-I_RNaseY; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 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 NCBIfam; TIGR00277; HDIG; 1.
DR NCBIfam; TIGR03319; RNase_Y; 1.
DR PANTHER; PTHR12826; RIBONUCLEASE Y; 1.
DR PANTHER; PTHR12826:SF15; RIBONUCLEASE Y; 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; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00335};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00335};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00335}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 337..430
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 73..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 58488 MW; 0E96CE9CF31C027E CRC64;
MPNAIITLFF ALITLIVGAF FGYALCKDAY EKKLSQAKKT AEDIISDAKK SAKSLKKETL
LEAKDEAHKY REKMESELND RRNDVKKQEN RNLERQDILD RKDQSLEKRE ENIEKNENNI
SAKEKQLDEK DKQLTNTLDE QKAELIRVSN LTRDQARKII LDDLNKELTH ERATMINESG
EQARQYADKE AKSLIVAAIQ RSAADTVAET TVTTVTLPNE DMKGRIIGRE GRNIRTIESL
TGVDLIIDDT PEAVALSAFD PIRREIARMA LEKLIEDGRI HPARIEEMVD KARKDMDDHI
REIGEQTIYG LGISSVNPDL IKIIGRMQYR TSYGQNVLSH SIEVAKLSAV MAGELGEDVT
LAKRAGLLHD IGKAIDREVD GSHVEIGVDI ATKYKEPEVV VNTIASHHGD VEPTSLIATI
VAAADAISAA RPGARSESME NYIHRLEKLE EIANKHEGVD HCYAIQAGHE IRIMVKPEEI
SDDQAAILSR DVKNEIEENL EYPGHIKVTV VREVRKVELA K
//
