ID A0A1F7HGC6_9BACT Unreviewed; 401 AA.
AC A0A1F7HGC6;
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=A3F29_00140 {ECO:0000313|EMBL:OGK29842.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPHIGHO2_12_FULL_33_9.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802045 {ECO:0000313|EMBL:OGK29842.1, ECO:0000313|Proteomes:UP000177199};
RN [1] {ECO:0000313|EMBL:OGK29842.1, ECO:0000313|Proteomes:UP000177199}
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:OGK29842.1}.
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DR EMBL; MFZV01000056; OGK29842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7HGC6; -.
DR Proteomes; UP000177199; 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; 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 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 216..308
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
SQ SEQUENCE 401 AA; 45204 MW; BC3BBF8D3A875FBF CRC64;
MADDNKTSKD DTLLDKKINE ITDKLKDKTN ITSEEAKNYV ISLWETKLKE EVAKKIRFAE
EEVKAKAEET AKQILIDAMR FGATDYVAEY TLSTVNIPSD DFKGRIIGKD GRNIRAFELA
SGVDVDLEEP GVIKLSSFDS VKREVARQAL EQLIRDGRIQ PGRIEEIVNK TREDLEKIMF
KAGEELAFKV GAHNLPNEML SALGRFKFRY SYGQNMILHT LEETRIGIAL AHELKVDIET
VRLGCLFHDI GKVISDKEGS HVELGVEFLK KHNFPEAVIG CVAAHHEDIP FPSIEAIIVY
ISDAISGGRP GARHEDFQEY LKRIKTIEDV AKENEGVDDA YALQAGRELR VIVKPSKISD
EEASILASKI RDELEKKFDV FPGQIKITVI REFRAESTTK I
//