RNY_CLOK5
ID RNY_CLOK5 Reviewed; 514 AA.
AC A5N857;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=CKL_1446;
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(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; CP000673; EDK33488.1; -; Genomic_DNA.
DR AlphaFoldDB; A5N857; -.
DR STRING; 431943.CKL_1446; -.
DR EnsemblBacteria; EDK33488; EDK33488; CKL_1446.
DR KEGG; ckl:CKL_1446; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000002411; 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..514
FT /note="Ribonuclease Y"
FT /id="PRO_0000344851"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 204..289
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 330..423
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 514 AA; 58329 MW; A476EB0DF5439386 CRC64;
MNYMIIYEII AGILIVVAIL IHFNIMKNKV AAIKSQTIYE SNRLKEEAKK EAQSQKKEAI
LEAKEEVHKL RNDLERESRD RRMEIQRLEK RVLQREELLD KKNDVLEKRE SSLDKKQQEI
DKVQAKVEEL YQKQREELER LSGLSSEEAK DILLEEVNKE IKHESAMMIK EVETKAKEEA
DKRAREIITS AIQRCAADHV AETTVHVVTL PNDEMKGRII GREGRNIRTL ETLTGVDLII
DDTPEAVILS GFDPIRREVA RIALEKLIID GRIHPARIEE MVEKAEKELE NDIKEEGEQA
TFETGVHGLH IELIKLLGRL KYRTSYGQNV LKHSVEVAYL AGLMASEIGI DPTIAKRAGL
LHDIGKAVDH EVEGPHAVIG AEIAKKYRES PVVVNAIGAH HGDLEFQSLE DVLVQAADAI
SAARPGARRE TLEAYIKRLE KLEKIANTCE GVEKSYAIQA GRELRIMVKP EDIDDAGALE
MARNIVKKIE EELEYPGQIK VNVIRETRAI EYAK