RNY_PETMO
ID RNY_PETMO Reviewed; 517 AA.
AC A9BEV4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Pmob_0083;
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX NCBI_TaxID=403833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000879; ABX30832.1; -; Genomic_DNA.
DR AlphaFoldDB; A9BEV4; -.
DR SMR; A9BEV4; -.
DR STRING; 403833.Pmob_0083; -.
DR EnsemblBacteria; ABX30832; ABX30832; Pmob_0083.
DR KEGG; pmo:Pmob_0083; -.
DR eggNOG; COG1193; Bacteria.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_0; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000000789; 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; RNA-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..517
FT /note="Ribonuclease Y"
FT /id="PRO_0000344922"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 207..267
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 333..426
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 517 AA; 59401 MW; E29C767775066199 CRC64;
MEILVYIIIG IAIFILSLLV GINIGNRRMI STLATKKEEL EVEIKNKQKE IEKMLKNAEE
EAKALKQKEL LEAKEEIHRL RQEFDSEAKQ QREELKANEE RLIRKEESLA KKEENLEKLK
EKLEVQHENV LKLEKELETK LNEIAKMTEE EARQVVINEA RDKYEREIAQ KFKEIKDHYE
EESKKYARWV ITTAIQRYAS DVTNEITTST VALPTDDMKG RIIGREGRNI RTFEKLTGTD
LIIDDTPEIV VISSFNPLRR EIAKRTLEML VADGRIHPAR IEELYEKSKN EIQEYIKEVG
KEAVMRVGIK QPHLEIIKLL GRLKFRTSYG QDVLEHSIEV AQFAGMMASE LGLNVELAKR
AALLHDLGKA VDHEVEGSHA IVGGQIAKRY GEKLEVVNAI QYHHNEVDPM TPEAVLVAAS
DALSASRPGA RKETLENYIR RIEQLEEIAK SFRYVDKAYA IQAGRELRII VQPDKVEDEI
AEKLAHDISV QIEEKVQYPG VIKVTVIREK RSISYAS