RNY_THEFY
ID RNY_THEFY Reviewed; 501 AA.
AC Q47RS4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=Tfu_0805;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(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; CP000088; AAZ54843.1; -; Genomic_DNA.
DR RefSeq; WP_011291252.1; NC_007333.1.
DR AlphaFoldDB; Q47RS4; -.
DR SMR; Q47RS4; -.
DR STRING; 269800.Tfu_0805; -.
DR EnsemblBacteria; AAZ54843; AAZ54843; Tfu_0805.
DR KEGG; tfu:Tfu_0805; -.
DR eggNOG; COG1418; Bacteria.
DR eggNOG; COG1566; Bacteria.
DR HOGENOM; CLU_028328_1_0_11; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
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; 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; 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.
PE 3: Inferred from homology;
KW Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease; RNA-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="Ribonuclease Y"
FT /id="PRO_0000344963"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 190..256
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 316..409
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 501 AA; 55188 MW; AF9F48EED95E5AE2 CRC64;
MDGVADLVVI ALLGALTLLT AGHVLALRSR SRAVAAQAQQ WADRIRADAE NAARSHQDRL
LAEAAAYRAE LDRREQRIAA QEQRIERELR RLDAARRQLD ERTAQLDQRA AELARLAEER
RAVLEQAAAL TAEEAKAALV ADIVDQAKRE AAVLVRAIER DARTNGEARA RRIISLAIQR
LAGEQTSESV VRAVPLPEEA MKGRIIGREG RNIRAFETVT GVDLIVDDTP GVVLLSCFHP
LRRETARLTL EKLVADGRIN PHRIEEAYEA SRREVEQQCV RAGEDALLEV GISDMHPELV
ALLGQLRYRT SYGQNVLAHL VESAHLAGMM AAELGADVPL AKRCALLHDI GKALTHEVEG
SHAVIGAQLA RRYGECEEVA HAIEAHHNEV EARTVEAVLT QAADAISGGR PGARRASMES
YVKRLQRMEE IAYAVSDGVE KVFVMQAGRE IRVMVQPEAV DDVQAQVIAR DIAKRVEEEL
TYPGQVRVTV IRESRAVETA R