ID A0A0G1KU79_9BACT Unreviewed; 506 AA.
AC A0A0G1KU79;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
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=UW86_C0008G0020 {ECO:0000313|EMBL:KKT87161.1};
OS Microgenomates group bacterium GW2011_GWA1_Microgenomates_45_10.
OC Bacteria.
OX NCBI_TaxID=1618493 {ECO:0000313|EMBL:KKT87161.1, ECO:0000313|Proteomes:UP000034781};
RN [1] {ECO:0000313|EMBL:KKT87161.1, ECO:0000313|Proteomes:UP000034781}
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:KKT87161.1}.
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DR EMBL; LCJY01000008; KKT87161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KU79; -.
DR PATRIC; fig|1618493.3.peg.277; -.
DR Proteomes; UP000034781; 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 322..415
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 34..118
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 506 AA; 56806 MW; 91461DCB781ECC02 CRC64;
MNQTLVVALF VLLGVAVGYF TRQQVASRLK GKQGEKLEEE AQKARTQAQE IILEAKDKAA
SLIDEARQEE KERKLSITKL EERLIEKEGA LSTKEKEIEE VKKGLTSKEG DLENLRKDFE
GTRARIQEDL AKISGMKPEE AKKKLIDEVK DQYREDLVQV LHELSHDRKE EVEKKSMEIM
TAAMQRYARS HVSDVTTSIF TLPSEDLKGK IIGREGRNIR AIERLTGTEL IIDETPETII
ISSFDPMRRE IARLALAKLV KDGRIQPAKI EERVEEAKAE IEKRMYEIGE EAAFETGIFD
LPKEIIHLLG RLNFRTSFGQ NVLTHSIEMA HLAGMIAAEL GADVEVAKRG ALLHDIGKAI
DHEVEGTHVE LGRKILSKYG VSEAVVKAME SHHDDYPFST SESFIVAAVD ALSAARPGAR
RGTLEHYIKR LDDLEKVASS FDGVQQAYAV SAGRELRIFV IPEKIDDFGA LQLARDIAGK
IKSDLNYPGE IKVNVIRETR AVEYAR
//
