ID A0A0G1SBK8_9BACT Unreviewed; 509 AA.
AC A0A0G1SBK8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=UX89_C0018G0007 {ECO:0000313|EMBL:KKU66909.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_16.
OC Bacteria.
OX NCBI_TaxID=1618842 {ECO:0000313|EMBL:KKU66909.1, ECO:0000313|Proteomes:UP000034117};
RN [1] {ECO:0000313|EMBL:KKU66909.1, ECO:0000313|Proteomes:UP000034117}
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 -!- 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:KKU66909.1}.
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DR EMBL; LCNX01000018; KKU66909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1SBK8; -.
DR STRING; 1618842.UX89_C0018G0007; -.
DR PATRIC; fig|1618842.3.peg.769; -.
DR Proteomes; UP000034117; Unassembled WGS sequence.
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 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 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}.
FT DOMAIN 325..418
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 59..93
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 509 AA; 56689 MW; A137842FF81BB7CF CRC64;
MSLKIVVLLA SLVGIVGVVL GYYLRLIISL GKRGSMELEI KEMMLKAREE AKKITEGAEA
KANEALATAR SEMKEREEKL KKSEERIIKK EDTLDQRQTD IDKEVENIKV KIAEVKTVKE
KVVALEVSKQ GELEKLARLS ETEAKAELIK SVEKRYEEDL LVRMQKLEKF GEEQLERKAQ
GILSSAIQRL GNSVSADVLT TMVTIPNDEI KGKVIGKEGR NIKAFERATG VEVIVDDTPG
AITISSFDPV RRQVARVALE NLILDGRIQP AKIEQMVEKA HEEINKIIKE KGQQAVYECG
VLNLDPRIVA ILGRLHFRTS YGQNVLQHSI EMAHIAGILA EELKASVPIA KAGALLHDIG
KAVDHEVQGT HVEIGRRILQ KFGADEAIVK AMQAHHGEYP YETIESIIVQ TADAISGSRP
GARRDSVENY LKRLGDLEAI SKSFPGVEKA YALQAGREIR VFVTPTEISD LDAKKMAQEI
AGRIEKELKY PGEIKVTVIR ELRTIEYAR
//
