ID A0A1G2C7Q2_9BACT Unreviewed; 507 AA.
AC A0A1G2C7Q2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=A2128_01920 {ECO:0000313|EMBL:OGY97388.1};
OS Candidatus Liptonbacteria bacterium GWC1_60_9.
OC Bacteria; Candidatus Liptonbacteria.
OX NCBI_TaxID=1798645 {ECO:0000313|EMBL:OGY97388.1, ECO:0000313|Proteomes:UP000176349};
RN [1] {ECO:0000313|EMBL:OGY97388.1, ECO:0000313|Proteomes:UP000176349}
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:OGY97388.1}.
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DR EMBL; MHKV01000013; OGY97388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2C7Q2; -.
DR Proteomes; UP000176349; 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 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 323..416
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 73..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 57282 MW; CF24ABD417B3B3BB CRC64;
MDYNQILWAV FALAGIVAGY AVRHVLGAKS ASSLEQKVKL QLEEAKNKAK EIVLEAKDKA
AASFEEVKKE ERERKAQLDR TEERLAKKDE GLRGDEQRLA ERQSAFERRD EELKKAKQEV
EEARARAEKE LEKLSGLTVE EARARLIKDV EENYRQDVAL AVQKLERDRR DELEKKSVEI
MTVAIQRYAR SHVSELTTSS FQLPSEELKG KIIGREGRNI RALERATGVE FVIDETPDTI
LISSFDPLRR EIARMALEKL IKDGRIQPAR IEERVEEARQ EIAKRMQEIG EAAAFEVGIY
DLPKEIIQLL GRLHFRTSYG QNVLIHSVEM AHISAMMAAD LKANVEVAKK GALLHDIGKA
IDHDVEGTHV ELGRKILKKY GIDELVIRAM ESHHEEYPFS TPESYIVTAA DALSAARPGA
RRDSVENYIK RLQDLEALAV GFPGVKGAYA LSAGREVRVF VLPEKIDDFG ALQLARDIAG
KIEAELKYPG EIKVNVIREM RAVEYAR
//