RNY_HELPH
ID RNY_HELPH Reviewed; 529 AA.
AC Q1CTB0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=HPAG1_0745;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF84812.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1CTB0; -.
DR SMR; Q1CTB0; -.
DR EnsemblBacteria; ABF84812; ABF84812; HPAG1_0745.
DR KEGG; hpa:HPAG1_0745; -.
DR HOGENOM; CLU_028328_1_0_7; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000008835; 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 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..529
FT /note="Ribonuclease Y"
FT /id="PRO_0000344886"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 216..297
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 342..435
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 529 AA; 60238 MW; 1FFF380C04E00A16 CRC64;
MSSGLIYISL EVLVACLITA LIMYYVMKKI YYARGQAALK SASAKAKLME FQAKSFVEAE
EVRMKSQECK LQQQYENKNL QLKTHFEKKE VHLKHLEAQH KEFVRDEKRY LEKEKKELEK
ERQILEQEKE NFKKQRVVCK EAQAKALDAM LNYMAYTKDE IKNMILEQLE EELEAQKSAL
IRRYEKEAKE EGKKKSYAIL AEATARFAGN YATENLTTRI ALPCSDYIGR VIGKDGKNIE
AFKKVSGVDI EFSEDSSELC LSSFNLYRRE VASETLKILI EDGRIQPNRI EEVYHRVARN
LEKELLSEGE SVVLELELGA MEDELKILIG KMRYRSSFGQ NALQHSKEVA LLAGLIAEQL
GGDKKLARRA GILHDIGKAL TQELGRDHVN LGVEVCKRHK EDPVVINAIY AHHGHEEILS
VECASVCAAD ALSAGRPGAR RKSDEEYAKR MQALEEIALE FDGVEKAYAM ESGRELRVIV
KSNQVRDNQV PIIARKIAKK IEESAQYVGE VGVQVVRENR FKTTATLKQ