RNY_SYNAS
ID RNY_SYNAS Reviewed; 521 AA.
AC Q2LRA0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=SYNAS_07310;
GN ORFNames=SYN_02979;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(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; CP000252; ABC76610.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LRA0; -.
DR STRING; 56780.SYN_02979; -.
DR EnsemblBacteria; ABC76610; ABC76610; SYN_02979.
DR KEGG; sat:SYN_02979; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_7; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000001933; 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..521
FT /note="Ribonuclease Y"
FT /id="PRO_0000344960"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 211..277
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 337..430
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 521 AA; 58834 MW; 0A4D80F404CFAF2F CRC64;
MLNYTVIAFI MLGLIAIGLA IGYFLKFRLS QKRLESSENL ALRIIDEAKK EAETIKKEAV
LQTKENLLKL KAEFEKETRE RKLDLDNLER RIRSKEENLD KRIDSMSQKE NAIEVREKNL
LSKEMQLNEK HDKLSRMIGE QKEKLEQIAD ITSEEAKDFL IRSMEAAAKR DAAMLIRKIE
EDAKREADKK SREIIAYAVQ RYAGDYVAEN TVSVVNLPND EMKGRIIGRE GRNIRAIEAA
TGIDLIVDDT PEAVVLSSFD PIRREVAKIS LERLITDGRI HPGRIEDIVK KVRLEVDSII
KETGERVSFD VGVHDIHPEL INLLGSLKYR TSYSQNVLQH SIDVAHLTGM MAAELKMNIK
EAKRAGLLHD IGKAVDHKIE GTHAAIGADY AKRFGESQRI VQAIAAHHDD GRTNTLLGVL
VQAADTLSAA RPGARREMLE TYVKRLEELE NIANSFNGVD KCFAIQAGRE IRILVGSEKL
SDNDAMMLCK DIVKKIESEL TYPGQIKVTV IRETRVSDFA K