ID A0A1F8AS31_9BACT Unreviewed; 414 AA.
AC A0A1F8AS31;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
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=A3E44_06140 {ECO:0000313|EMBL:OGM54563.1};
OS Candidatus Woesebacteria bacterium RIFCSPHIGHO2_12_FULL_41_24.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802510 {ECO:0000313|EMBL:OGM54563.1, ECO:0000313|Proteomes:UP000178603};
RN [1] {ECO:0000313|EMBL:OGM54563.1, ECO:0000313|Proteomes:UP000178603}
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:OGM54563.1}.
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DR EMBL; MGGW01000013; OGM54563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8AS31; -.
DR Proteomes; UP000178603; 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 229..321
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 3..47
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 414 AA; 46595 MW; 9C261EB0BCF2FBC8 CRC64;
MSSDDVKLIL EEIKKDRNRL ERKEKDLKEI EEKLTSKLEK VASLTRDEAK KELLDVIQKN
LTVDIAKKIR QGEERIKLEA RDKAREILAD AMKHGATTYV AEYTVSTVSV DSEEAKGRII
GREGRNIRSF EKETGVEIEL DEGNVIRLSS FDSIRREIAR RSLEILLKDT RIQPSRIEEV
VRQVKSQMED ILLEEGKKIV QECGVFNLPI EVIKLIGRFK FRTSYGQNLG LHTIEETKIG
VAIAAEIGAN TEVVRLGCLL HDIGKVVTDV EGNHVDAGVT TVKRFGFPKE VVAAVSEHHE
DKPFSSTESV IVWIADAISG SRPGARYEPY ENYVKRMTKI EEISGSFSGV EQAIAFQAGR
DVRIIVRPEE VEEDKLTVLA NDIARRLEKE AEYAGQVKVT VIRETRAQAT TAAK
//
