RNY_AQUAE
ID RNY_AQUAE Reviewed; 558 AA.
AC O67622;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=aq_1732;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07588.1; -; Genomic_DNA.
DR PIR; D70449; D70449.
DR RefSeq; NP_214188.1; NC_000918.1.
DR RefSeq; WP_010881125.1; NC_000918.1.
DR AlphaFoldDB; O67622; -.
DR SMR; O67622; -.
DR STRING; 224324.aq_1732; -.
DR PRIDE; O67622; -.
DR EnsemblBacteria; AAC07588; AAC07588; aq_1732.
DR KEGG; aae:aq_1732; -.
DR PATRIC; fig|224324.8.peg.1335; -.
DR eggNOG; COG1418; Bacteria.
DR eggNOG; COG3599; Bacteria.
DR HOGENOM; CLU_028328_1_0_0; -.
DR InParanoid; O67622; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000000798; 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..558
FT /note="Ribonuclease Y"
FT /id="PRO_0000163763"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 248..311
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 374..467
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 558 AA; 64329 MW; FCA1163ED060C2F1 CRC64;
MDVLSILLIL VAVGVGIFVG RQFLGQKQAP APTYQPVPSP QILEEAKSKA EEIIKEAKEK
AEVILKEAKE SAEKIVREAE EKAEKLIREA KEEVERIKEE VERRKKELKE REENVLAKER
HLDRRWEALE KREEELLHRE RELKDFERSL ERWRDEIRHK EEELKHMKEE VEELKKKELE
ELQRIAKLTL EEARQEIIKK VEEEAKKDAV KLMKVIEEDA KRRAEFEAKK IIATATQRLA
PQIAVNYTTT TVELPSNEFK GRIIGREGRN IRTFEILTGV DLIIDDTPDI VTISSFDPLR
REIAKEALQR LIADGRIHPA RIEEVVDEVK REFDEKIRKI GEETVYELDL HDINPGLYYY
IGKLYFRTSY SQNVLLHSKE VAYIAGLMAE ELGLDAKLAR RAGLLHDIGK AISHELGGSH
TDIGVELARK YGEPDAVINA IRAHHEEEPV RYPEVALVCA ADALSAARPG ARRETLEAYI
RRLEKLEEIV KSFKGVANAY AVQAGREVRV IVNPEEISDE EAYLLSKEIP KKIEEELDFP
GQIKVVVIRE TRHVEYAK