RNY_FERNB
ID RNY_FERNB Reviewed; 517 AA.
AC A7HMK7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=Fnod_1293;
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1;
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., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-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; CP000771; ABS61140.1; -; Genomic_DNA.
DR RefSeq; WP_011994449.1; NC_009718.1.
DR AlphaFoldDB; A7HMK7; -.
DR SMR; A7HMK7; -.
DR STRING; 381764.Fnod_1293; -.
DR PRIDE; A7HMK7; -.
DR EnsemblBacteria; ABS61140; ABS61140; Fnod_1293.
DR KEGG; fno:Fnod_1293; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_0; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000002415; 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..517
FT /note="Ribonuclease Y"
FT /id="PRO_0000344872"
FT TRANSMEM 4..24
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; 58829 MW; 50872E795B96B62A CRC64;
MEWLIYIVIL FVGIAAGAFF GISVGRKRAE EALEKKLKAA KEDAESIIKS AEKEASEIKK
KAIIEAREEA HQIREEIEKE RKKREEEIKQ LEERLLKREE MLSKREELID KRENYVENLK
IELESKAKEI EEKAKEIERR FIELAGITHE QAREIVLQEA REKYEHEIAK FFVQIKTRYE
DEADKYAKKI IADAIQRYAP EYIGEVTIST VALPNDDMKG RLIGREGRNI RTFEKITGVD
LIIDDTPEMV TLSSFNPLRR EVARRTIEKL VQDGRIHPAR IEEMYEKAKA EVEREIKEAG
QDAVITVGVG GLHPEIIKLL GRLKFRTSYG QNVLAHSVEV AQIAGLLAAE LGLNVDKAKR
GGLLHDIGKA IDHEVEGSHT DIGAEMLKRY GESDEIINMV MAHHGQEEPI TPEAAIVAAA
DAISAARPGA RREDVENYIK RLMKLEEIAK SYKYVENAYA IQAGREIRVI VQPDKTDDAT
IEKLAHDIAT RIENELQYPG VLKVVVIREK RSVSYAK