ID A0A1G2F617_9BACT Unreviewed; 510 AA.
AC A0A1G2F617;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=A2V69_02925 {ECO:0000313|EMBL:OGZ33001.1};
OS Candidatus Portnoybacteria bacterium RBG_13_40_8.
OC Bacteria; Candidatus Portnoybacteria.
OX NCBI_TaxID=1801990 {ECO:0000313|EMBL:OGZ33001.1, ECO:0000313|Proteomes:UP000177810};
RN [1] {ECO:0000313|EMBL:OGZ33001.1, ECO:0000313|Proteomes:UP000177810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGZ33001.1}.
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DR EMBL; MHMT01000008; OGZ33001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2F617; -.
DR STRING; 1801990.A2V69_02925; -.
DR Proteomes; UP000177810; 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 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..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 326..419
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 34..122
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 510 AA; 57327 MW; C9B20572C297462D CRC64;
MIIGLIPLMV AIGVLVAGSI LGYLARQSIA KRQADTAEAR IDKLVTEAKA QAQEIILKAK
DKAVKALDEI KQEEIRREGE FRKTKQHLER KEEILEGKST SLDKEENELR LKVERVREIK
TELGRLKDEE IDRLEKISKL SQEEAKKEIL KLIEDKNKEE IFAKIQKLEK DGKEELEKKA
RDIMVSALQR YASSQASDIT TTTVNLPNDE IKGKIIGREG RNIKTLERLT GVEVIIDETP
ETLLISGFDP VRRQIAKMSL EKLIADGRIQ PARIEEVVEK TKDEIDKKMK EAGETAAYDV
GIVGLDSRLV NLLGRLTFRT SFGQNVLLHS IESAHLAGML ASELGADVAI VKKAALLHDI
GKAVDHEIQG SHVDIGIKIL QKFGIDKKVI DAMKSHHEDY PFETIEASIV QAAEAISAAR
PGARKENLEN YIKRLEELEK IATDFQGVEK AYAIQAGREI RVFVNPEKID DLGAYKLAKD
IAQEIEKELK YPGEIKVNVI RETRVIEYAR
//