ID A0A1G2F138_9BACT Unreviewed; 506 AA.
AC A0A1G2F138;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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=A3H02_01460 {ECO:0000313|EMBL:OGZ31713.1};
OS Candidatus Niyogibacteria bacterium RIFCSPLOWO2_12_FULL_41_13.
OC Bacteria; Candidatus Niyogibacteria.
OX NCBI_TaxID=1801726 {ECO:0000313|EMBL:OGZ31713.1, ECO:0000313|Proteomes:UP000176787};
RN [1] {ECO:0000313|EMBL:OGZ31713.1, ECO:0000313|Proteomes:UP000176787}
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
CC Single-pass membrane protein {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:OGZ31713.1}.
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DR EMBL; MHMS01000023; OGZ31713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2F138; -.
DR STRING; 1801726.A3H02_01460; -.
DR Proteomes; UP000176787; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
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 Membrane {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}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00335};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00335}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 322..415
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 38..139
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 506 AA; 57084 MW; B15A9818785276F2 CRC64;
MTLDLWIIIP LIGGIVLGYF LRQTKAKLDK SSLELKTQQV LLDAKTKAEE RLEEAKKKAE
EIVEEARKEE KELKLGFQKL ETKLAEKEIL IENQKQKIED EKKRIEGQIE TIEAKKAELE
KSEELKRKEL EKLSGLSAEE AKKALFIEAE KKYQTDLLSH LQKLEMNGEE QLKNKSREII
LSIIQRLATS TASEITTSTV SIPSEDLKGR IIGKEGRNIR ALERAAGVEL IVDDTPGVII
ISSFDPLRRH IAKIALENLI LDGRIQPVRI EEAVSKAQLE IEKLVKEAGE QAAYEVGVMN
LEPKLLNILG RLKFRTSYGQ NVLQHSIEAA HLAGMLASEL GADVNVSKTA ALLHDIGKAM
DHEIQGSHVE IGKRILEKFG VDKKIILAAI AHHGDYPYET LESIVVQTAE AISASRPGAR
RDTLENYLRR LEDLEKIALN FEGVDKAYAL QAGREIRIFI NPEKISDYQA KILCRQIADQ
IEKDLKYPGE IKVHLIRENR IVEFAR
//