ID A0A0G1P0I5_9BACT Unreviewed; 510 AA.
AC A0A0G1P0I5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 29.
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=UW90_C0012G0008 {ECO:0000313|EMBL:KKT89879.1};
OS Candidatus Yanofskybacteria bacterium GW2011_GWB1_45_11.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619026 {ECO:0000313|EMBL:KKT89879.1, ECO:0000313|Proteomes:UP000034368};
RN [1] {ECO:0000313|EMBL:KKT89879.1, ECO:0000313|Proteomes:UP000034368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT89879.1}.
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DR EMBL; LCKD01000012; KKT89879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1P0I5; -.
DR PATRIC; fig|1619026.3.peg.485; -.
DR Proteomes; UP000034368; 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 56..133
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 158..186
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 510 AA; 57118 MW; 7E040E0E375F5881 CRC64;
MLSGLNPLIA AISALLPGMV IGYLIRQVIV SRRTSLAESK AQQLLADSKS KAQDIVLDAK
NQAIKLLEDA KKEEKERHQQ TAKIENLLTR KEAELDHKSK EIEKERENLK LKLAELQNIK
LELEKSKEIQ IQELERISQL NRETAKVELI STLEKEYQND LYEKIKKLEQ ENKEELEKKA
REILTLAIQR YSGSHIADAT TTVVSLPSDE VKGKIIGKEG RNIKTIERLT GVDVIIDDTP
EALVVSGFDP VRRQVAKLAI DKLIADGRIH PAKIEEMVEK AKEEINARIK EAGEAALFET
GIGPIDPKLT YLLGRLAFRT SFGQNVLLHS IEMTHIAGML AAELGIDVAT AKKGALFHDI
GKAVDHEVQG THVEIGRKIL QKFGMDQKVI MAMEAHHEEY PYVSLESRIV QAADAISGAR
PGARKDTVEI YLKRLEELER IAASFDGVEK SYAIQAGREL RIFVTPMAID DLGAIKLAKD
IAKKIEDEMK YPGEIKVNVI RETRAIEYAR
//
