RNY_PELPD
ID RNY_PELPD Reviewed; 521 AA.
AC A1AU84;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Ppro_3312;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000482; ABL00905.1; -; Genomic_DNA.
DR RefSeq; WP_011737122.1; NC_008609.1.
DR AlphaFoldDB; A1AU84; -.
DR STRING; 338966.Ppro_3312; -.
DR PRIDE; A1AU84; -.
DR EnsemblBacteria; ABL00905; ABL00905; Ppro_3312.
DR KEGG; ppd:Ppro_3312; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_7; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000006732; 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 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.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease;
KW Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..521
FT /note="Ribonuclease Y"
FT /id="PRO_0000344919"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 211..271
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 337..430
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 521 AA; 57686 MW; 613C0880BAE08343 CRC64;
MQVSIWMLVI TVLAAVAAYF AGSRVNKKDS GLIVKQSEEL AAKMIDDARR EAETITKEAD
LKARAEIIEA KAGHDREITE KKKDLQILEK RLQQKEENLD KKFGLIEQKE LDMLKKEQSF
VAREQNLAAK SEELSRASDV QQAKLEEISG MSASEAKKEL MTSMEDEAKH DAAKRIKAIE
EEARETADKK AKEIISLAVQ RYAGEYVAEK TVSVVPLPSD EMKGRIIGRE GRNIRALEAA
TGIDLIIDDT PEAVILSGFN PVRREVARMS LEKLIGDGRI HPGRIEEVVA KATEEVDLGI
KEAGERAAFD LGVHGIHPEI IKLIGRLKYR TSYTQNIYQH SLEVAFICGI MAAELGINVK
QAKRAGLLHD LGKAVDHEVE GSHAVIGADL ARKYGESAKI VHAIMAHHED EKPNSVLAVL
VQAADALSGA RPGARREMME TYVKRLDDLE RIATSFGGVT NSFAIQAGRE IRVMVSSDHV
TDEQSLIMAR DIAKKIEAEM TYPGQIKVNV IRETRAVEYA R