RNY_HELPJ
ID RNY_HELPJ Reviewed; 529 AA.
AC Q9ZL83;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 123.
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=jhp_0697;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06283.1; -; Genomic_DNA.
DR PIR; A71899; A71899.
DR AlphaFoldDB; Q9ZL83; -.
DR SMR; Q9ZL83; -.
DR STRING; 85963.jhp_0697; -.
DR EnsemblBacteria; AAD06283; AAD06283; jhp_0697.
DR KEGG; hpj:jhp_0697; -.
DR eggNOG; COG1418; Bacteria.
DR OMA; PHAILGM; -.
DR Proteomes; UP000000804; 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..529
FT /note="Ribonuclease Y"
FT /id="PRO_0000163775"
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; 60398 MW; 6689FA0406796941 CRC64;
MSSGLIYISL EVLVACLITA LIMYYVMKKI YYARGQAILK GASAKAKLME FQAKSFVEAE
EMRMKSQECK LQQQYENKNL QLQTHFDKKE AHLKHLEAQH KEFVRDEKRY LEKEKKELEK
ERQILEQERE NFKKQRAICK EAQAKALDAM LNYMAYTKDE IKSMILEQLE EELEAQKSAL
IRRYEKEAKE EGKKKSYAIL AEATARFAGD YATENLTSRI ALPCSDYVGR VIGKDGKNIE
AFKKISGVDI EFSEDSSELC LSSFNIYRRE VASETIKILI EDGRIQPNRI EEVYHRVARN
MEKELLSEGE SVVLELELGT MEDELKILIG KMRYRFSFGQ NALQHSKEVA LLAGLIAEQL
GGDKKLARRA GILHDIGKAL TQELGRDHVN LGVEVCKRHK EDPVVINAIY AHHGHEEIMS
VECASVCAAD ALSAGRPGAR RKSDEEYAKR MQALEEIALE FDGVEKAYAM ESGRELRVIV
KSNQVRDNQV PIIARKIAKR IEESTQYVGE VGVQVVRENR FKTTATLKQ