RNY_THESQ
ID RNY_THESQ Reviewed; 507 AA.
AC B1LAG5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=TRQ2_0962;
OS Thermotoga sp. (strain RQ2).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC unclassified Thermotoga.
OX NCBI_TaxID=126740;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RQ2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga sp. RQ2.";
RL Submitted (MAR-2008) 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; CP000969; ACB09313.1; -; Genomic_DNA.
DR AlphaFoldDB; B1LAG5; -.
DR PRIDE; B1LAG5; -.
DR EnsemblBacteria; ACB09313; ACB09313; TRQ2_0962.
DR KEGG; trq:TRQ2_0962; -.
DR HOGENOM; CLU_028328_1_0_0; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000001687; 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; RNA-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Ribonuclease Y"
FT /id="PRO_0000344967"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 197..282
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 323..416
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 507 AA; 58040 MW; 0C093F8A74969E4B CRC64;
MLWYIVAGAG GLLIGYLIAN YQINQKLRKA KEDAQTIIEK AEKEANEIKK KAIIEGREEV
HRLREEFEKE RSRREEELRA LEERLLKREE LLTRKEENLE KREQQVEELK ANLEEKMREV
EEKEKRIDEE LKRLAGMTVE EARELILEEA RQRYEHDLAK LYKEMKEQVE EEAEKEAKKV
IAFAVQRYAP DYVGEITVST VSLPSDDMKG RIIGREGRNI RTFEKITGVD LIIDDTPEVV
VLSCFNPLRR EIARITLEKL VADGRIHPAR IEEMYEKAKQ EVEKAIKEAG QEATFKAGVM
GLHPELVKLL GKLKYRTSYG QNVLNHSIEV ALLAGYMASE LGLNADKARR GGLLHDIGKA
VDQELEGSHT TIGAELARRY GEKEDIINMI LSHHGEEEPM TPEAVLVAAA DALSAARPGA
RRESLENYIK RLMKLEEIAK SFKYVEKAYA IQAGREIRVI VEPDKVDDAL AEKLAYDISK
KIEEELEYPG VLKVVVIREK RSVAYAK