RNY_ENDTX
ID RNY_ENDTX Reviewed; 518 AA.
AC B1GZX3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, 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=TGRD_322;
OS Endomicrobium trichonymphae.
OC Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC Endomicrobium.
OX NCBI_TaxID=1408204;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Complete genome of the uncultured termite group 1 bacteria in a single
RT host protist cell.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
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; AP009510; BAG13805.1; -; Genomic_DNA.
DR RefSeq; WP_015423332.1; NC_020419.1.
DR RefSeq; YP_001956266.1; NC_020419.1.
DR AlphaFoldDB; B1GZX3; -.
DR SMR; B1GZX3; -.
DR STRING; 471821.TGRD_322; -.
DR EnsemblBacteria; BAG13805; BAG13805; TGRD_322.
DR KEGG; rsd:TGRD_322; -.
DR PATRIC; fig|471821.5.peg.514; -.
DR HOGENOM; CLU_028328_1_0_0; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000001691; 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..518
FT /note="Ribonuclease Y"
FT /id="PRO_0000344971"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 207..270
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 333..427
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 518 AA; 58669 MW; 86B7E992855FEE0A CRC64;
MGNITVIVIT AFVASIVGYI LRLIYAKLNI RSVEQTSKRV IEEMKLIAET KAKEIILDAR
LIVDRERKEF EHKIKERRQF IQNMENKLNQ REESLDRKMD AVDKKEKNLS EREKDFSSKE
HLLSVKFSEV DKVKEEQKKF LERISGMTRE EAKKILISGM EEDAKQCAAV LLQKLEQEMR
ENADKKSKEI LSIAIQRVAA DHTADITTST IQISNDEIKG RIIGREGRNI KAFEHATGVD
LIVDDTPESI TISAFDGIRR QIAKIALERL IADGRIHPAR IEEVVKKVKK DMEQHLKETG
EQAVIEAGVP CSNLEIIKLL GKLKYRTSYG QSQLQHTLEV TWLAGAIAGE LGLDVMFCKK
AALLHDIGKA VDHEVEGTHH QISANIAKKY GESHKMINAI LSHHEGFEVP SSPEAFVIAT
ADAISAARPG ARKESVERYL KRLEKLEKVV KEFRGVSIAY AMQAGREVRI LVEPEKINDN
QTQILAHDIA KKIEQELEYP GQIKITVVRE TRVQEIAK