ID   RNY_CAMJD               Reviewed;         517 AA.
AC   A7H2G9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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};
GN   OrderedLocusNames=JJD26997_0520;
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000768; ABS43601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H2G9; -.
DR   EnsemblBacteria; ABS43601; ABS43601; JJD26997_0520.
DR   KEGG; cjd:JJD26997_0520; -.
DR   HOGENOM; CLU_028328_1_0_7; -.
DR   OMA; PHAILGM; -.
DR   Proteomes; UP000002302; 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; 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; PF12072; RNase_Y_N; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   TIGRFAMs; TIGR00277; HDIG; 1.
DR   TIGRFAMs; TIGR03319; RNase_Y; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease; RNA-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..517
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344837"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          207..273
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          333..426
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   517 AA;  58144 MW;  C41A37CB2EED04D1 CRC64;
     MIESLIALIA AIVGLGIGYL VAKKINDAKY EIFVEQAKAK AKAIEYEAEL ILKDAKNSIL
     NAELEVKKKY EEKTHKIQKD FNQKLDDLFK KEQKLQQEEE KLKEDKEYLC KSQKHIQDLQ
     SDVDKLKNKY QEKLDDVLKI LEHSTRLTQN EAKEIILKKV EENSREQIAH IVRKYEEEAK
     NEAKRKANFI IAQATSRFAG EFAAERLINV INIKNDELKG RIIGKEGRNV KTLEMVLGVD
     IIIDDTPGAI IVSCFNLYRR AIATKVIELL VEDGRIQPAR IEEIHEKVCK EFDSAILEEG
     EIIVMDLGLN KIHPEIVKLI GKLKYRASYG QNALAHSLEV AHLAGIIAAE CGGDENLARR
     AGILHDIGKA LTHDFEGSHV DLGAELCNRY KEHPVVINAI YAHHGHEEAT SIESAAVCAA
     DTLSAARPGA RREVLEAFLK RVSELEDIAK SKEGIKNAYA INAGREIRII ANAQLVNDDE
     SVLLAKEIAA EIQEKMQYPG EIKVNVIREL RAIEYAK