ID A0A1F5FHS9_9BACT Unreviewed; 477 AA.
AC A0A1F5FHS9;
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=A2368_00860 {ECO:0000313|EMBL:OGD79140.1};
OS Candidatus Collierbacteria bacterium RIFOXYB1_FULL_49_13.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1817728 {ECO:0000313|EMBL:OGD79140.1, ECO:0000313|Proteomes:UP000176682};
RN [1] {ECO:0000313|EMBL:OGD79140.1, ECO:0000313|Proteomes:UP000176682}
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:OGD79140.1}.
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DR EMBL; MFAM01000026; OGD79140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5FHS9; -.
DR Proteomes; UP000176682; 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 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 294..386
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 18..70
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 477 AA; 53912 MW; 414F5484E2707DB4 CRC64;
MADITPQKPD PKLIALAQAQ AREIILEAKD EVLKLKDQAR QESVRLSREI DQKRQLLFQD
KQEIARLQAR LEERDRLTAQ QSQIIQTRLK EIEELKIKQI KALEKVSDMS QTQAKEQVLA
EVAKRSTAEA AKLIKASTEK AHEEAEVKAK EILVDAMYSG ATDYVAEYTV TTVKIPDEET
KGRIIGKEGR NIRTFEKVTG VDIDLDEQGV IKLSCFDSIR RETARVALER LIKDGRIHPT
HIEEFVDKAR RDIDKYIFQE GERLCHSVGV YDLPRDIIAA LGKFKYRTSY GQNMIAHTLE
ETRIGIKLAS EAKANVEIVK LGCLLHDIGK VITDEEGSHV ELGVRFLKKY NIPQAAIDCV
AQHHEDEEFT SIESVLVYIS DAISGSRPGA RYENYEEYVQ RLQKLEEIAT KHAGVKDAFA
IQAGREIRVI VDPRELNDDL AAKLALDIKD EVKASMTYPG TITVTVIRET RNTQVAA
//