ID A0A1F7IFI0_9BACT Unreviewed; 433 AA.
AC A0A1F7IFI0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
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=A2954_02025 {ECO:0000313|EMBL:OGK42114.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_37_12.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802056 {ECO:0000313|EMBL:OGK42114.1, ECO:0000313|Proteomes:UP000177698};
RN [1] {ECO:0000313|EMBL:OGK42114.1, ECO:0000313|Proteomes:UP000177698}
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:OGK42114.1}.
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DR EMBL; MGAG01000004; OGK42114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7IFI0; -.
DR STRING; 1802056.A2954_02025; -.
DR Proteomes; UP000177698; 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 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 248..340
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..63
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 433 AA; 49602 MW; E9A856E98399F5C6 CRC64;
MEENLEIERN LSRREQQLGE KETNLNKEKG FIDNQRQTLE KIKKEYEERR EAILLKLEKV
SQMTKDQARE LLLSGWEEKL KGDIAKRIKQ SEEDIKKSVE EKAKEILIDS MRYGATDYVS
EYTLSVINLP NEDFKGRIIG KDGRNIRAFE LATGVDVDLE EEGVIRLSSF DAIKRETAKI
SLERLIKDGR IQPERIEEIV NKTKEEIDKV IFKAGEELAH KVGIFNLPSE VTHFLGKFKY
RFSYGQNMIL HTLEETRIGI ALAHELKADV NVVKLGCLLH DIGKVITDKE GSHVDLGVEL
LKKYRFPQNI VDCVAAHHED IPFPSIESII VYISDAVSGG RPGARHEDFD QYLKRIKTIE
DAAKNKKGVR EAYALQAGRE LRVVVKPDEI SDDDVTILAN KIKDELEQKF DVFPGQIKVT
VVREYRAEAT TKI
//