RNY_FINM2
ID RNY_FINM2 Reviewed; 513 AA.
AC B0S1D0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=FMG_0752;
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
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; AP008971; BAG08170.1; -; Genomic_DNA.
DR RefSeq; WP_012290605.1; NC_010376.1.
DR AlphaFoldDB; B0S1D0; -.
DR SMR; B0S1D0; -.
DR STRING; 334413.FMG_0752; -.
DR PRIDE; B0S1D0; -.
DR EnsemblBacteria; BAG08170; BAG08170; FMG_0752.
DR KEGG; fma:FMG_0752; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000001319; 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;
KW Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Ribonuclease Y"
FT /id="PRO_0000344873"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 203..288
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 329..422
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 78..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 57650 MW; EB0BD1B9BDF80FDF CRC64;
MSTTTSLIIA ILAGILGIVI GFFFRKSLAE KKIRSAEDYA VKIIEDANKD AETKKKELLV
EAKDEIFKMK SDLDRENKSR LKEISRQEDR LNSKEENLER KNASLEKKHK KLDSELKKAD
DMQLKIQSLI DEKELELEKV AGLTSDEAKN IVLERVKTET IREQAAIIKE IESKTKEESE
KFAREIISTS IQRYAADQVA ESTVSVVNLP NDDMKGRIIG REGRNIRAFE TLTGVDLIID
DTPEAVVLSA FDPVRREIAR IALEKLIVDG RIHPTRIEEM VEKARKDVDN TIREKGEEAC
DETNVHGLHP ELIKILGKLH YRTSYGQNVL KHSIEVSNIA GMLASELGVN VKLAKRGGLL
HDLGKAIDHE IEGPHVELGV NAAKRFKEPK DVINCIEAHH GDVEPTCIES ILVQSADAIS
AARPGARRES MENYIQRLEN LEQIANSFDG IESSYAIQAG REIRIMVKPD VIDESSMVIL
AKDVAHKIES ELEYPGQIKV NVIRENRVSD YAK