ID A0A1F7KGQ9_9BACT Unreviewed; 471 AA.
AC A0A1F7KGQ9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
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=A2209_03235 {ECO:0000313|EMBL:OGK67041.1};
OS Candidatus Roizmanbacteria bacterium RIFOXYA1_FULL_41_12.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802082 {ECO:0000313|EMBL:OGK67041.1, ECO:0000313|Proteomes:UP000178450};
RN [1] {ECO:0000313|EMBL:OGK67041.1, ECO:0000313|Proteomes:UP000178450}
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 -!- 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:OGK67041.1}.
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DR EMBL; MGBG01000002; OGK67041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7KGQ9; -.
DR Proteomes; UP000178450; 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 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 289..381
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 31..97
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 471 AA; 54039 MW; F2DD15C937A719C0 CRC64;
MFDLVFKFFP NLKRERDLIL DEAHKRADRL TIQAQSKLSE LSRQIASLEK KISLDEERLK
VERQELDKTK EGLKQEQQQL ADEKIAVEKK KQELLKKFEK LAGLTPEQAR ENLLAHWEQK
LSSDIAQRIR EAKEQIKKES EEKGKEILID AMRFGATDYV VEYTLSTITL SSDEYKGRII
GKEGRNIRSF ELATGVEVDL DEEGVVKLSS FDPVKREIAR VSLESLIKDG RIQPQRIEEV
VSKTRSEIGK IIYKEGEKLC YEVGVYNLPK EIVELLGRFK YRFSYGQNMI QHTLEETRIG
VALAHELKAD VNVVRLACLL HDIGKVIVDK EGSHVQLGVE LLKKHRFPAS IVEAVETHHE
DKDFTSTEGI IVYLADAVSG GRPGARREDV TAYIKRINEM ENFIKAKEGV HDVAVLQAGR
EIRVIINPQK LSDEQTIVFC EKLRQDLQKY YSSIPGQIKL TAIREFRVTN K
//
