RNY_ROSCS
ID RNY_ROSCS Reviewed; 535 AA.
AC A7NHM5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Rcas_0856;
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-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; CP000804; ABU56972.1; -; Genomic_DNA.
DR RefSeq; WP_012119402.1; NC_009767.1.
DR AlphaFoldDB; A7NHM5; -.
DR SMR; A7NHM5; -.
DR STRING; 383372.Rcas_0856; -.
DR PRIDE; A7NHM5; -.
DR EnsemblBacteria; ABU56972; ABU56972; Rcas_0856.
DR KEGG; rca:Rcas_0856; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_0; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000000263; 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; 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..535
FT /note="Ribonuclease Y"
FT /id="PRO_0000344927"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 225..285
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 351..444
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 535 AA; 60151 MW; F15B5FA4B0D76583 CRC64;
MFEPVATARQ RAVACCTFTT EQEDVVQWLV WALPALVIGL AIGAGIGILI YKNSVQSQIR
QIEAEARLQL EATRSEQKDL ILRATDEALR LRTEAEAQIR EARAALAKQE ERLQRKEENL
DRKIEGLERR ERQLQQRERQ MEQLHQEAEH LRQQQRAELE RISALSQEEA RAIILKRVED
ETRDEAARRI REIEKTMHEE ADKLARKVIS MAIQRCASDY VAEVTVSTVA LPSEELKGRI
IGREGRNIRA FEQLTGVDII VDDTPEAVTL SCHDPVRREV ARLALIKLLK DGRIHPTRIE
EVVHKTQQEV DQVMREEGER VAYEANVQGL HPDLIKLLGR LKYRTSYGQN VLQHSLECAL
LAAHIAAEIG ANINVAKTAA LLHDIGKAVD HEVQGPHALI GAEIARRLGK SPAIVHAIAA
HHNDEEPQTV EAWLVQAVDA ISGGRPGARR ETLDLYIKRL EALETVATSF SGVQRAFAVQ
AGREVRVMVQ PDAIDDLGSI HLARDVAKKI EESLQYPGQI KVTVIRETRA VDYAR