ID A0A1Q7EBD1_9CHLR Unreviewed; 510 AA.
AC A0A1Q7EBD1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=AUH39_01275 {ECO:0000313|EMBL:OLC10700.1};
OS Chloroflexi bacterium 13_1_40CM_67_9.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805082 {ECO:0000313|EMBL:OLC10700.1, ECO:0000313|Proteomes:UP000187329};
RN [1] {ECO:0000313|EMBL:OLC10700.1, ECO:0000313|Proteomes:UP000187329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(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:OLC10700.1}.
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DR EMBL; MNEQ01000019; OLC10700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7EBD1; -.
DR Proteomes; UP000187329; 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; 3.30.300.20; -; 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; IPR015946; KH_dom-like_a/b.
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 326..419
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 67..129
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 510 AA; 56518 MW; 888A5D044310AB14 CRC64;
MPDILVVGLV ALVAGLVGFG IALVLRRSFA LASETTARAN ADRLLAEARA RQNQIILEAK
DEALKVAKTA ESENRERRAE LQRYEGRLDK KDEQLDQKIA QVDERDRRLG QKEQDLEGER
TKIAQLQDEQ RTELARVASL TMEEARGLLL ERVEEEMRDI TGRKVRELEV DARERADERA
RDIITMALQR YAAEHTAEHS VTVVALPSDD MKGRIIGREG RNIRTLETLT GVDLIIDDTP
EAVVVSGFDP IRREVAKRAL ERLLVDGRIH PARIEEMVGK ARTEIDQVMK EAAEAAIYEV
GIGGLNPDLV KLLGRLHFRT SYGQNVLRHS IEVAHVAGML ASETGYDPQT MKRAGLLHDI
GKAIDHEVEG PHTVIGGELL KRYGFPQAVI DGVVGHHGDV EPVTMVGTLI SAADAISAAR
PGARSEIVSN YIQRLQELES VANSFPGVEK AFAIQAGREV RVVVKPDQLD DLATARLSRD
IAQKIQDTLQ YPGQVKITVI RETRAVEYAK
//
