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RNY_CAMJ8
ID   RNY_CAMJ8               Reviewed;         517 AA.
AC   A8FMR4;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=C8J_1152;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
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; CP000814; ABV52751.1; -; Genomic_DNA.
DR   RefSeq; WP_002853829.1; NC_009839.1.
DR   AlphaFoldDB; A8FMR4; -.
DR   KEGG; cju:C8J_1152; -.
DR   HOGENOM; CLU_028328_1_0_7; -.
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; 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_0000344839"
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;  57993 MW;  7303A874742CC49B CRC64;
     MIESLIALIA AIVGLGIGYL VAKKINDAKY EIFVEQAKAK AKAIEYEAEL ILKDAKNSIL
     NAELEVKKKY EEKTHKIQKD FNQKFDDLSK KEQKLQQEEE KLKEDKEYLC KSQKHIQDLQ
     SDVDKLKNKY QEKLDDVLKI LEHSTGLTQN EAKEIILKKV EENSREQIAH IVRKYEEEAK
     NEAKRKANFI IAQATSRFAG EFAAERLINV INIKNDELKG RIIGKEGRNV KTLEMVLGVD
     IIIDDTPGAI IVSCFNLYRR AIATKVIELL VEDGRIQPAR IEEIHEKVCK EFDSAILEEG
     ETIVMDLGLN KIHPEIVKLI GKLKYRASYG QNALAHSLEV AHLAGIIAAE CGGDENLARR
     AGILHDIGKA LTHDFEGSHV DLGAELCKRY KEHPVVINAI YAHHGHEEAT SIESAAVCAA
     DTLSAARPGA RREVLEAFLK RVSELEDIAK SKEGIKNAYA INAGREIRVI ANAQLVNDDE
     SVLLAKEIAA EIQEKMQYPG EIKVNVIREL RAVEYAK
 
 
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