RNY_ALKMQ
ID RNY_ALKMQ Reviewed; 475 AA.
AC A6TRJ1;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Amet_2657;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {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; CP000724; ABR48809.1; -; Genomic_DNA.
DR AlphaFoldDB; A6TRJ1; -.
DR STRING; 293826.Amet_2657; -.
DR EnsemblBacteria; ABR48809; ABR48809; Amet_2657.
DR KEGG; amt:Amet_2657; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_0_0_9; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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 Endonuclease; Hydrolase; Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..475
FT /note="Ribonuclease Y"
FT /id="PRO_0000344808"
FT DOMAIN 165..228
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 291..384
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 34..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 54276 MW; 974C42EEF26C5016 CRC64;
MAKKIKDDAD KNAETTKKEV LLEAKEEIHK LRNEFERESR ERRNELQRVE RRLMQKEESL
DKKSETLEQK DDRLSRKLRD LETKEEEIKL LYNKEVQKLE ELSGLTSQQA RELLLSDVEK
EVKYEAAMMV KDIETKAKDD ADKKAREIIT LAIQKCAADH VAETTVTVVQ LPNDEMKGRI
IGREGRNIRT LETLTGIDLI IDDTPEAVIL SGFDPIRREV ARIALEKLIA DGRIHPARIE
EMVEKAKKEV ENILKEEGEQ ATFDTGVHGL HPELIRLLGR LKYRTSYGQN VLKHAIEVSH
LAGLMATELG ADPKLAKRAG LLHDIGKAVD HEVEGTHIEI GMELLRKYKE TKDVIHAMST
HHGDFEPETI EAILVTAADA ISAARPGARR ETLESYIKRL EKLEDIANNY DGVEKSFAIQ
AGREIRIIVK PEVYNDDEIY MFAREITKKI EADLEYPGQI KVNVIRETRA IEYAK