ID A0A1G1Q6A3_9BACT Unreviewed; 519 AA.
AC A0A1G1Q6A3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=A3G88_02790 {ECO:0000313|EMBL:OGX49631.1};
OS Omnitrophica WOR_2 bacterium RIFCSPLOWO2_12_FULL_63_16.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801871 {ECO:0000313|EMBL:OGX49631.1, ECO:0000313|Proteomes:UP000177516};
RN [1] {ECO:0000313|EMBL:OGX49631.1, ECO:0000313|Proteomes:UP000177516}
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:OGX49631.1}.
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DR EMBL; MHHE01000007; OGX49631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1Q6A3; -.
DR STRING; 1801871.A3G88_02790; -.
DR Proteomes; UP000177516; 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; 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 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 335..428
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
SQ SEQUENCE 519 AA; 58151 MW; F3B8ABE5B79FA170 CRC64;
MTILAVLVIL GVGGLLFLAG YGLRLLVGRR QLGSAERHAK EVLEQAARDA KTVLHKGELD
AKEFLNTLRK DFEGETRDRR NEIAQLEKRL HQREEVLDRK LDVLDRKDKE LTDRARQLGT
REQALKTKED QLSQLIAEEN EKLKSVASLT SEQAKQLLLS RIDQECRSEA GLVIKRIEEE
TRKDAQAIAR KVLVETMQRC AAEFSVESTT AAVPLPNEEM KGRIIGREGR NIKAFELATG
VDLIVDDTPD VVTLSSFDLM RREIARAALE RLMADGRIHP ARIEEIVEKV KREFDQSVQQ
EGEKALAELN LHGMHAELVK LLGRLRYRTS YGQNCLLHLK ESAFICGMIA AELGLDQRMA
KRCALMHDIG KAVSHEVEGP HALIGAELAK RYGEPPEVVH SIEAHHEDVV PSTVYAVLTI
VADSISGSRP GARGDTLEAY VKRLQTLEHL CDSFKGVAKA YAIQAGREVR VMVQPERVTD
LEAIALAREI KKKVESAIEF PGQIKITVIR ETRTIEYAR
//
