RNY_STRT1
ID RNY_STRT1 Reviewed; 535 AA.
AC Q5M171;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=str0397;
OS Streptococcus thermophilus (strain CNRZ 1066).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=299768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNRZ 1066;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV61999.1; -; Genomic_DNA.
DR RefSeq; WP_011225535.1; NC_006449.1.
DR AlphaFoldDB; Q5M171; -.
DR SMR; Q5M171; -.
DR GeneID; 66898320; -.
DR KEGG; stc:str0397; -.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
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..535
FT /note="Ribonuclease Y"
FT /id="PRO_0000344954"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 225..285
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 351..444
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 103..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 60397 MW; C242D02962AB0BC7 CRC64;
MINMIILVVF ALIGLVVGYS AISIKLSKAK EQAETILLKA EQDAVNLRSQ AEHDADHLRV
TAERESKAQR KELLLEAKEK ARKYREDIEE EFKSERQELK QMENRLTERA TSLDRKDENL
SSKELALEKK EQSLADKSKH LNEREENVTQ LEAEKQAELE RIGQMTIAEA REVILTETEN
NLTHEIATRI KDAEAQIKDT VDKKAKNLLA QAMQRLSGDY VTEQTVTTVH LPDDNMKGRI
IGREGRNIRT LESLTGIDVI IDDTPEVVVL SGFDPIRREI ARMTLEALIK DGRIHPARIE
ELVEKSRKEM DNRIREYGEE AAYEIGAMNL HPDLIKIMGR LQFRTSYGQN VLRHSVEVGK
LAGIMASELG ENVALARRAG FLHDMGKAID KEVEGSHVEI GTEFARKYKE HPVVVNAIAS
HHGDVEPESV IAVIVAAADA LSSARPGARN ESVENYVKRL RDLEEIASSF DGVQTSFALQ
AGREIRIMVH PNKISDDEVT ILSHKIREQI EKNLDYPGNI KVTVIREFRA VDYAK