RNY_LAWIP
ID RNY_LAWIP Reviewed; 520 AA.
AC Q1MQ71;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=LI0802;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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; AM180252; CAJ54856.1; -; Genomic_DNA.
DR RefSeq; WP_011526885.1; NC_008011.1.
DR AlphaFoldDB; Q1MQ71; -.
DR SMR; Q1MQ71; -.
DR STRING; 363253.LI0802; -.
DR KEGG; lip:LI0802; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_7; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000002430; 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;
KW Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Ribonuclease Y"
FT /id="PRO_0000344901"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 209..272
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 335..429
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 520 AA; 58605 MW; 72D6CE642815DDE6 CRC64;
MSFILVLCTV SSLFVGGGTG IFLYKKVSKK YIGDAKELAI RIVEEARKEG QAQKKEILLQ
GQNEIFNQKK EFEFDFKQRE KELSIKDKKL QVQSERLEER LERAAEKEHE ILKVEKELSI
KERNLLTLEE QLKSRIDEQE KQLQKISGLT VEEAKQSLFE EVKNRSRHES AKMMRLIEAE
AVETANRKAK EIIANAIQRY AGDYVSEHTV TAVTLPSEDM KGRIIGREGR NIRALESATG
VDFIIDDTPE TVVLSAYSPM RRQVAKMALE RLIQDGRIHP ARIEEIVRKC EEDLAIQVRE
IGEQATFDIG VYGIHPELIR ILGQLNYRTS YTQNVLRHSI EVASLCGMMA AELGVDIKKA
KRAGLLHDIG KAVDHEVEGS HAIIGAELAK KFNETEEIVH AIEAHHEEKG KPETALAILV
QASDCLSGAR PGARLELLES YVKRLEHLEN IAGEFEGVSK AYAIQAGREV RVMVDADSIG
DDQTYLLCKD IAGRIEESLT YPGQIRVTVI REHRAVGYAK