RNY_BORGP
ID RNY_BORGP Reviewed; 510 AA.
AC Q661B6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
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=BG0516;
OS Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS PBi) (Borrelia bavariensis).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=290434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX PubMed=15547252; DOI=10.1093/nar/gkh953;
RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT "Comparative analysis of the Borrelia garinii genome.";
RL Nucleic Acids Res. 32:6038-6046(2004).
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; CP000013; AAU07355.1; -; Genomic_DNA.
DR RefSeq; WP_011193817.1; NZ_CP028872.1.
DR AlphaFoldDB; Q661B6; -.
DR SMR; Q661B6; -.
DR STRING; 290434.BG0516; -.
DR EnsemblBacteria; AAU07355; AAU07355; BG0516.
DR GeneID; 66542694; -.
DR KEGG; bga:BG0516; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_12; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000002276; 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..510
FT /note="Ribonuclease Y"
FT /id="PRO_0000344830"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 198..258
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 324..419
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 510 AA; 57990 MW; 12D46D172F7D8818 CRC64;
MIYIIFSSIF AGFILGFLVR VFLGRLSLLD LEKNLTKVRV ESQLEIENER KQIIANAKSQ
MLKEKNQQDR DIRDRKNEIV NLEKRLLQRE ETLDKRISAL DKQQSRVDFK IKEFEQKEKA
IREKEADLVK RLENISGLTR EDARKIVIEK VEHESRRDAQ VIINKSEQEA QLLADKVAKD
ILVSTMQRIV TEVSSEFTVA SVELPNDEMK GRIIGKEGRN IRALETLIGA DIIIDDTPEA
VVISCFDPIR KELAKRTLER LVTDGRIHPA RIEEVVYNVT NEINSIIQEE GEKVVFDLNI
HGLDKRLIRG LGRLYFRSSY GQNVLSHSKE TAIIGEILAK EMKLDPIVVK RACLLHDIGK
GMESISENSE GHAITGAELA QSCGESEIVV NAIAAHHNEV KPESLEAIVV QIADAISASR
PGARRESLNN YINRLKRLED IAYSFEGVQK CYAIQAGREV RIIVDNVLVN DEKSILLARD
IAKKIEAEMR YPGKIKVTII RETRVIEYAR