RNY_NITSB
ID RNY_NITSB Reviewed; 522 AA.
AC A6Q3V4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Ribonuclease Y {ECO:0000255|HAMAP-Rule:MF_00335};
DE Short=RNase Y {ECO:0000255|HAMAP-Rule:MF_00335};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00335};
GN Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; OrderedLocusNames=NIS_1053;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {ECO:0000255|HAMAP-Rule:MF_00335}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00335};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00335}.
CC -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000255|HAMAP-
CC Rule:MF_00335}.
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DR EMBL; AP009178; BAF70163.1; -; Genomic_DNA.
DR RefSeq; WP_012082426.1; NC_009662.1.
DR AlphaFoldDB; A6Q3V4; -.
DR SMR; A6Q3V4; -.
DR STRING; 387092.NIS_1053; -.
DR EnsemblBacteria; BAF70163; BAF70163; NIS_1053.
DR KEGG; nis:NIS_1053; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_7; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000001118; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.30.1370.10; -; 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 PANTHER; PTHR12826:SF15; PTHR12826:SF15; 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; SSF54791; 1.
DR TIGRFAMs; TIGR00277; HDIG; 1.
DR TIGRFAMs; TIGR03319; RNase_Y; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease;
KW Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Ribonuclease Y"
FT /id="PRO_0000344912"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 212..278
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 338..431
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 522 AA; 59107 MW; 653094B40ADA5EAC CRC64;
MWVEILVGSS AAIISGAAGY LLSKKIEKDK LKIYEEQARA KAKAIEHEAE KILQNAQVQV
KEAELELKRD FEKKLEELKR DYEERFNELM EKEMSLKQMF KDELKHITLE KQEIKAEREE
INRLKNEYEE LKKRYQEKYQ EVLEALQQQA GLTLEEAKNL ILQKAEEESR LEIANIVRKY
EEEAKREAKR RANYIIAQAT TRFAGEFAAE RLINTVSIPS EDIKGRIIGK EGRNIKTLEM
LLGVDIIIDD TPNAIILSSF NLYRRAIATK VIELLVEDGR IQPSRIEEIY EKVKEEFDQQ
LLEEGENIVI DLGIGLIHPE IVKLIGRLKF RASYGQNALG HSLEVAHLAG IMAAEMGGDE
VMAKRAGLLH DIGKALTHEY SGSHVDLGAE ICKRYKEPDV VINAIYAHHG HEEPRSIEAA
AVCAADTLSA ARPGARREVL EAFLKRVQAI EEIALSKPGV KKAYAINAGR EVRVIVNADL
VNDNEAVLLA KEIAKDIETG VQYPGEIKVN VIRENRAIEY AR