RNY_CLOPE
ID RNY_CLOPE Reviewed; 511 AA.
AC Q8XJT1;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
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=CPE1672;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB81378.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000016; BAB81378.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003459753.1; NC_003366.1.
DR AlphaFoldDB; Q8XJT1; -.
DR STRING; 195102.gene:10490936; -.
DR EnsemblBacteria; BAB81378; BAB81378; BAB81378.
DR GeneID; 29570974; -.
DR KEGG; cpe:CPE1672; -.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000000818; 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..511
FT /note="Ribonuclease Y"
FT /id="PRO_0000163771"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 201..286
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 327..420
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 511 AA; 57681 MW; DF65E9021EC53EF6 CRC64;
MVVGILIGII ILGVVGFIQY TLIQKASKNR VESLEKEASL TLEEAKREAE STKKEAILEA
KEEVHKLRAD LDKETRDRRN EIQRFERRLI QREESLDKKG EMLEKREDSI NKKSIEIQEL
EERVQNLYGE QRAELERISN LSSEDARTLL LDEVRREIKH ESAMLIKELE TKAKEEADKK
SREIITTAIQ RCAADHVSET TVHVVALPND EMKGRIIGRE GRNIRTLETL TGVDLIIDDT
PEAVILSSFD PIRREVARIA LEKLIVDGRI HPARIEEMVE RAIKDVENDI KEEGEQATFE
TGVHGLHPEI IKLLGRLKYR TSYGQNVLKH SIEVSYLAGL MASELGLDVN LARRAGLLHD
IGKGVDQEYE GPHAVIGGEL AKKYHESPAV VNAIAAHHGD TEMQTLEAVL VQAADAISAA
RPGARRETLE AYIKRLEKLE EIATSYEGVE KSYAIQAGRE IRIMVKPDQV DDAGAIEMAR
NIVKKIEEQL EYPGQIKINV IRETRAVDYA K