ID A0A0G1B4C7_9BACT Unreviewed; 518 AA.
AC A0A0G1B4C7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 31.
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=UV38_C0002G0084 {ECO:0000313|EMBL:KKS68215.1};
OS candidate division TM6 bacterium GW2011_GWE2_42_60.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619076 {ECO:0000313|EMBL:KKS68215.1, ECO:0000313|Proteomes:UP000034453};
RN [1] {ECO:0000313|EMBL:KKS68215.1, ECO:0000313|Proteomes:UP000034453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS68215.1}.
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DR EMBL; LCEG01000002; KKS68215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1B4C7; -.
DR STRING; 1619076.UV38_C0002G0084; -.
DR PATRIC; fig|1619076.3.peg.426; -.
DR Proteomes; UP000034453; 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 333..427
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 34..129
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 518 AA; 58411 MW; 5C465DEB80BBCC82 CRC64;
MTFLILVAGG AACIVGLTLM VVAVGKTAKA QGIARSIELE RAAAQKEIAA EKREASFQLK
EEVHKRRIEF KNELKREQAE FERVQSKLTA QKEAFDEKER WINSTKMELQ QKERELSRLS
DQLRINQERV KVLQTDLTSR LEKLAYMTQE EARRVLFETL EAEVKHSHEK WLQKAEEEAR
LTARERSLHI IVDAMQRYSS DYVSSNTICI VTLPNDDMKG RIIGKEGRNI KVLEMTTGVD
IIIDDTPEII TISGFNPVRR EIARRTLEKL VTDGRINPTR IEETVADMER EVDEIIQSKG
KDAVARLNLH NVAQEIIMLL GQLHFRTSFS QDVLAHSIEV ATMARMLAEE LGFPRPDLAA
RAGLLHDIGK AVSSDHEGPH AQIGAEVARR CGEDPIVVNA IAAHHEEVAF KTLYDPLILI
ADTLSAARPG ARRETLAVYI KRLEKLEAIA GEFPGVKRAY ALQAGREIRI IVEEDILNDQ
ETSILALNVA KKVESELTFP GQIKVNVIRE KRAVEYAK
//
