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Database: UniProt
Entry: A0A1Y4M3T9_9FIRM
LinkDB: A0A1Y4M3T9_9FIRM
Original site: A0A1Y4M3T9_9FIRM 
ID   A0A1Y4M3T9_9FIRM        Unreviewed;       519 AA.
AC   A0A1Y4M3T9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=B5F12_08010 {ECO:0000313|EMBL:OUP63504.1};
OS   Pseudoflavonifractor sp. An176.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Pseudoflavonifractor.
OX   NCBI_TaxID=1965572 {ECO:0000313|EMBL:OUP63504.1, ECO:0000313|Proteomes:UP000196146};
RN   [1] {ECO:0000313|Proteomes:UP000196146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An176 {ECO:0000313|Proteomes:UP000196146};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC       {ECO:0000256|HAMAP-Rule:MF_00335}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00335}.
CC   -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000256|HAMAP-
CC       Rule:MF_00335}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUP63504.1}.
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DR   EMBL; NFKO01000016; OUP63504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4M3T9; -.
DR   Proteomes; UP000196146; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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|HAMAP-Rule:MF_00335};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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|HAMAP-Rule:MF_00335};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196146};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00335}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00335};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00335}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT   DOMAIN          335..428
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   COILED          25..145
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   519 AA;  58306 MW;  EA40D48913B34F77 CRC64;
     MNVNIVVVVI AVLVALVIGG GVGIAVGYNR RKAVAEREIG SAEEEARRVI NEAIKSAESK
     KREATVEAKE EILKARNEFE QEVKDRRNEL QRQENRVNQK EENLDRKMEN LERKEDVLAA
     RSAELDQDRA ELDTIKERQT QLLEQISGLT CEEAKRYLIE QLEEEVTHEE ALKIKEIQAR
     FKEEADTYAR EQIALAIQRC AADHVAEATV SVVPLPNDEM KGRIIGREGR NIRTLETMTG
     VDLIIDDTPE AITVSCFDPV RREIARLALE KLILDGRIHP TRIEEMVEKA KREVDATIKA
     EGERAVFETN VHGLSPELVK LLGRQRYRTS YGQNVLNHSI EVALLAGLLA AEIGADVNQA
     KRAGLLHDLG KSIDHEVEGS HVQIGVELAR KYRESEAVIH AIEAHHGDVE AKTIVACLVQ
     AADAISAARP GARKENVEYY IKRLEKLEEL SSSFPGVDKA YAIQAGREVR VMIKPEEVSE
     DRMVILAREI AKKIEDELEY PGQIKVNLIR ETKAIEYAK
//
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