RNY_PSELT
ID RNY_PSELT Reviewed; 509 AA.
AC A8F8V8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=Tlet_2038;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) 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; CP000812; ABV34592.1; -; Genomic_DNA.
DR RefSeq; WP_012004068.1; NC_009828.1.
DR AlphaFoldDB; A8F8V8; -.
DR STRING; 416591.Tlet_2038; -.
DR EnsemblBacteria; ABV34592; ABV34592; Tlet_2038.
DR KEGG; tle:Tlet_2038; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_0; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000002016; 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.
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..509
FT /note="Ribonuclease Y"
FT /id="PRO_0000344965"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 199..259
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 325..418
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 509 AA; 58085 MW; C9848933B6D033BD CRC64;
MIILVAVVTA VISFGLGYVV AKSRIEQKNR KAQQDAVSLL KKAEQEAQEI KRKAIIEARE
EVHKIKEEIE EEKKRRDLEH RSLEERLLKR EEIISKREEL VDKKETALEQ LRVQLEAAKK
KIEQREKELD ERFTKLAGMT VEEARQIVID EARQKYEHDL AILYKKIKEN YEEEAEKEAK
KIIATAVQRY APEYIGEITV STVSLPSDDM KGRIIGREGR NIRTFEKITG VDLIIDDTPE
VVVLSSFNPI RREIARLTLE KLVTDGRIHP ARIEEMYEKS KQEMEKMIKE AGQEATFVTG
VTGLHPELIK LLGKLKFRTS YGQNVLDHSI EVAQLAALMA EELGLDVDRT RRGGLLHDIG
KALDHEVEGS HTEIGAEIAR RYGESDHIIN MIMSHHGEQE PVCPESVLVA AADALSAARP
GARRESLETY IRRLVKMEKI AMSFKNVEKA YAIQAGREVR VIVEPEKIDD VEADKMAYEI
AKKIEEEVEY PGVLKVVVIR EKRSIAYAK