ID A0A1F6FFJ7_9BACT Unreviewed; 507 AA.
AC A0A1F6FFJ7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
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=A3G90_00970 {ECO:0000313|EMBL:OGG84642.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_12_FULL_45_26.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798525 {ECO:0000313|EMBL:OGG84642.1, ECO:0000313|Proteomes:UP000177325};
RN [1] {ECO:0000313|EMBL:OGG84642.1, ECO:0000313|Proteomes:UP000177325}
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:OGG84642.1}.
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DR EMBL; MFMM01000001; OGG84642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6FFJ7; -.
DR STRING; 1798525.A3G90_00970; -.
DR Proteomes; UP000177325; 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 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 323..416
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 36..84
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 113..175
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 507 AA; 56729 MW; 1513D5DD3CA28A7E CRC64;
MPQTFAIALA MLLLGVATGY YFRYLHALSK KRSLEIDIKE REVNAEKKAL ETIEKAEAKA
ATIEQEAKQE RKNQEEKLSQ KETHLLKREE MLDSRQIDLD SQKELIQTKI TEIKSFKAQL
DERKNDIEKK LEEVAGLTQE QALEKVIARV EAEHSEDLRA RVEKLDRQSD EAYEAKASNI
LLAAIHRVGN NIPSNVMTSH VEIPSDDLKG KVIGKEGRNV RAFERATGVD VLIDETPGYI
VLSSFDPIRR EIARVALEVL LKDGRIQPAK IEEAVELARK EVATIVRKMG EKAAYEAGVP
NLHPDLISIL GRLHFRTSYG QNVLWHSVEM AHMAAIIAEE VGADVAVARA GALLHDIGKT
VSHEVAGTHV EIGIRILEKY GVDHQVVLAM RAHHEEYPYE TPESIIVQVA DAISGGRPGA
RRDSIENYVK RLTDLEAIAT TLKGVDRAFA IAAGREIRVL VNPEDMTDFE THALARTIAT
TIEAKLRYPG EIKVHVIRET RVVSYAR
//
