ID A0A1F5FPA5_9BACT Unreviewed; 428 AA.
AC A0A1F5FPA5;
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=A2572_01620 {ECO:0000313|EMBL:OGD81439.1};
OS Candidatus Collierbacteria bacterium RIFOXYD1_FULL_40_9.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1817731 {ECO:0000313|EMBL:OGD81439.1, ECO:0000313|Proteomes:UP000179237};
RN [1] {ECO:0000313|EMBL:OGD81439.1, ECO:0000313|Proteomes:UP000179237}
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:OGD81439.1}.
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DR EMBL; MFAQ01000044; OGD81439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5FPA5; -.
DR Proteomes; UP000179237; 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 246..337
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 5..60
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 428 AA; 48311 MW; 63E50EBD7CEBDEE2 CRC64;
MEVRAKSLAQ KQQQLISEEN ELKKQKQALE NAQKQADELK ENLKTQADQM VKKLEKIASL
TTEAAKKELL SQVEKRSSME IARVIKETEE MAKAQASDKA REILVDSMRS GATDYVAEYT
ISTVPIPDEE TKGRIIGKDG RNIRIFEKVS GCDVSMDDSP DEVKLSSFDP VRREIARQTL
IHLIKDGRIH PARIEEYFER AKRDVEQIMF QEGQKLCHAV GVYNMHRDIV STLGRFKFRT
SYGQNMISHT LEETRIGIKI ASEIGANVDI VRMGCLLHDI GKVIDGEGNH IELGVNYLKK
YNLPQPIVDC VAQHHEDEEF SSIESMLVYI SDAISGSRPG ARHENTEDYG KRIRQLEEIA
RKHPEVDEAY AISAGREVRV IVNPQKASDA QLTILAQAIR DEIRDTMAFP GTVKVNVIRE
TRAAEIAS
//