RNY_SALTO
ID RNY_SALTO Reviewed; 588 AA.
AC A4X4U3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=Strop_1427;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(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; CP000667; ABP53893.1; -; Genomic_DNA.
DR RefSeq; WP_011905325.1; NC_009380.1.
DR AlphaFoldDB; A4X4U3; -.
DR STRING; 369723.Strop_1427; -.
DR EnsemblBacteria; ABP53893; ABP53893; Strop_1427.
DR KEGG; stp:Strop_1427; -.
DR PATRIC; fig|369723.5.peg.1454; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_11; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000000235; 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..588
FT /note="Ribonuclease Y"
FT /id="PRO_0000344931"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 278..359
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 404..497
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 588 AA; 64480 MW; D33418F99333E41D CRC64;
MNGFDAVLLV AVLLLTVVVV GAVLVGVRAV RGLAGTSRPD DPAFIAEKDR QEQSLAALRS
AAEEANSTID AAKSAAAAAR TEAAAARAEA KAARAEARRV LDGARAEAEA ILERVHKQAE
TEAEQLRTAA RRSGEREAAV LAVTTRDQAA EVERRAVRMD DRERLHTEEV ERLAERDRQL
SAANAALEAR ESALAERDRE LEQAEQRRRR ELERVAGLTA EAARGELVEA IEAQAKREAA
LRVRDIEAEA RSTGEERARH IVVDAIQRVA SEQTAESVVS VLHLPGDEMK GRIIGREGRN
IRTFESITGV NLIIDDTPEA VLLSCFDPVR REVGRLTLEK LVLDGRIHPH RIEEVHDLAR
QEVAQLCQRA AEDALVEVGI TEIHPELVGL LGRLRYRTSY GQNVLKHLVE SAHIAGIMAA
ELRLDVPTIK RCAFLHDIGK ALTHEVEGSH AIVGADVARR YGESEDVVHA IEAHHNEVPP
QTVEAVLTQA SDACSGGRPG ARRESLEAYV RRLERIEEIA GGKLGVERVF AMQAGREVRV
MVRPDDVDDL SASMLARDVA KQIEEELTYP GQIRVTVVRE SRVTEIAR