ID A0A0G1U9U9_9BACT Unreviewed; 510 AA.
AC A0A0G1U9U9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
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=UY21_C0015G0012 {ECO:0000313|EMBL:KKU90897.1};
OS Microgenomates group bacterium GW2011_GWA1_48_10.
OC Bacteria.
OX NCBI_TaxID=1618496 {ECO:0000313|EMBL:KKU90897.1, ECO:0000313|Proteomes:UP000034718};
RN [1] {ECO:0000313|EMBL:KKU90897.1, ECO:0000313|Proteomes:UP000034718}
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:KKU90897.1}.
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DR EMBL; LCPD01000015; KKU90897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1U9U9; -.
DR PATRIC; fig|1618496.3.peg.813; -.
DR Proteomes; UP000034718; 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 326..418
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..106
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 57678 MW; 70B0EAABE8DB6F90 CRC64;
MSLFSRLSTT LNKPKREVKY PKTQEKKAPI TRTSSSQLGA TSQQAIFQAQ TQAREIVFSA
KEEAIKIKSQ AEDEDRKLRA ELIELERRLA QKEESLDTRL RSLEDREKKT TETEKSLAEK
QIEVEKIRAD QLTRLQKIAS LSVEEAKEKI IAAVEEKSRN EAGRVAKGIL DEAKEQASAK
AREILVSEML HGATDYVAEY TVSIVSVGSE EVKGRIIGKE GRNIRAFEQA TGVDVELDEE
GVIRLSSFDS IRREIARVAL ERLIRDTRIQ PARIEEVVAQ VRKEIERIMF DEGEKLCHTV
GVYNLPRPIV EMLGRFKYRF SYGQNMILHT LEETKVGIAI TSEIGADVNV VRLGCLLHDI
GKVIESEEGS HVTLGADFLR KMGIPEKVVA CVEEHHEDKP FSSVESMIVY LADAISGSRP
GARYEDLEKY LARMKQLEEI CKSFPGVNDA WVFQAGREVR VLVDPEKMTD NEAVILAQKI
KERVESEIKE FPGQIKLTVI RELRITETAK
//
