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Database: UniProt
Entry: A0A1F7IFI0_9BACT
LinkDB: A0A1F7IFI0_9BACT
Original site: A0A1F7IFI0_9BACT 
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
//
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