ID A0A1F7ING4_9BACT Unreviewed; 492 AA.
AC A0A1F7ING4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=A3B40_00060 {ECO:0000313|EMBL:OGK44909.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_37_16.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802058 {ECO:0000313|EMBL:OGK44909.1, ECO:0000313|Proteomes:UP000178040};
RN [1] {ECO:0000313|EMBL:OGK44909.1, ECO:0000313|Proteomes:UP000178040}
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:OGK44909.1}.
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DR EMBL; MGAI01000019; OGK44909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ING4; -.
DR Proteomes; UP000178040; 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 307..399
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 31..164
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 492 AA; 56808 MW; 87E178F9AF83362E CRC64;
MVDLKNLIRS ILREELQEAK VEKQKEDPSL KQQTKELVLK AQEEALKIKQ EAEREVRKTM
QESLDIERRL ATREEQLEEK ERQIGSEKAF VEKQKQSLEQ LKKEYEEKRE IILQKLEKVA
QMTKDQAKQL LISGWEEKLK TEIAKKIKQK DEEIKQKVDE KAKEILIDAM RYGATDYVAE
YTLSVINLPN EDFKGRIIGK DGRNIRAFEL ATGVDVDLEE EGVIRLSSFD AIKREVARQS
LERLIKDGRI QPERIEEIVK KTKQEVDKII SRAGEELAHN VGVFNLPQEI VHLLGKFKYR
YSYGQNMILH TLEETRIGVS LAHELKVDVN TVKLGCLLHD IGKVITEKEG SHVELGVELL
KKYRFPQKII DCVAAHHEDI PFTSVESVIV YISDAVSGGR PGARHEDFEQ YLKRIKTIED
TAKSKKGVKE TYALQAGREL RVIVKPEEVS DEEATILSEK IREELEKKFD IFPGQIKVTV
IREYRAEATT KI
//
