ID M2Q325_9FIRM Unreviewed; 516 AA.
AC M2Q325;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=HMPREF9943_00458 {ECO:0000313|EMBL:EMD17305.1};
OS Eggerthia catenaformis OT 569 = DSM 20559.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Eggerthia.
OX NCBI_TaxID=999415 {ECO:0000313|EMBL:EMD17305.1, ECO:0000313|Proteomes:UP000011758};
RN [1] {ECO:0000313|EMBL:EMD17305.1, ECO:0000313|Proteomes:UP000011758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT 569 {ECO:0000313|EMBL:EMD17305.1,
RC ECO:0000313|Proteomes:UP000011758};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Mathney J., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lactobacillus catenaformis F0143.";
RL Submitted (FEB-2013) 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:EMD17305.1}.
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DR EMBL; AGEJ01000008; EMD17305.1; -; Genomic_DNA.
DR RefSeq; WP_004801659.1; NZ_KB446646.1.
DR AlphaFoldDB; M2Q325; -.
DR STRING; 999415.HMPREF9943_00458; -.
DR PATRIC; fig|999415.3.peg.453; -.
DR eggNOG; COG1418; Bacteria.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000011758; 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; 1.20.5.620; F1F0 ATP synthase subunit B, membrane domain; 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:UP000011758};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 332..425
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 66..135
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 516 AA; 58046 MW; 10F54EAB5B50E2D9 CRC64;
MDITIGVIIL VSGIVLGMIA YYVLVKMKIT KSSNDAKKIV DDANSKAENI VKEANLDAKT
QAYEYKLEAE KEIKAERLEL DKFENKLLER EHNIDRRDIA LQGKEDNLDQ KAQQLEKKQT
ELGKLEKQLK TQIDEKIVEL EKIAAMTAQE ARDELFRQVE QRMENELTAY IKEQEEEAKS
KASLYAKDII ADAINRYSQE EVVERTVKVV SLPSEEMKGR IIGREGRNIR AIENATGAEL
IIDDTPEVIT VSCFDPVRRE IARLSLEKLI KDGRIQPGRI EEVVEKTKKE IEETIYKAGE
DTIFNLGLSK FKKEEIMMIG KLKYRTSYGQ NGLQHSAEVA HFAGIMAAEL GLNQQLAKRA
GLLHDIGKAM DHEMEGSHVE LGAKFARKMG ESPIVINAIA SHHGDVPPTS VISVLVAAAD
TLSAARPGAR SETIENYIQR LEKLEEISKG FAGVDKVFAM QAGREIRVIV NPEKIDDLKA
HKLARDVREK IENELTYPGH IKITVVREIR ANEIAK
//
