ID   RNY_GRAFK               Reviewed;         520 AA.
AC   A0M2K0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=GFO_1875;
OS   Gramella forsetii (strain KT0803).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gramella.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL66845.1; -; Genomic_DNA.
DR   RefSeq; WP_011709753.1; NC_008571.1.
DR   AlphaFoldDB; A0M2K0; -.
DR   SMR; A0M2K0; -.
DR   STRING; 411154.GFO_1875; -.
DR   EnsemblBacteria; CAL66845; CAL66845; GFO_1875.
DR   KEGG; gfo:GFO_1875; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_10; -.
DR   OMA; PHAILGM; -.
DR   OrthoDB; 1012190at2; -.
DR   Proteomes; UP000000755; 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..520
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344883"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          210..295
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          336..429
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   520 AA;  57730 MW;  1BF0E09523198FE7 CRC64;
     MEILIIVIAA VVGLALGFAI AKMLEKKQAS GTIASAKKEA GSILKEAKAE GESIKKDKIL
     QAKEKFIELK SEHEKVILSR DKKINDAEKR IKDKESHVSN ELGKNKKLNK DLEEKVADYD
     HRLDFLEKKQ EDIDKLHNSK VQQLEVISGL SAEDAKAQLI ESLKDTAKAD AMSIIQDTVE
     EAKLTAQQEA RKIIINTIQR IGTEEAIENC VSVFNLESDD VKGRIIGREG RNIRALEAAT
     GVEIIVDDTP EAIILSCFDS VRREVARLSL HKLVTDGRIH PARIEEVVKK TRKQIEEEII
     DIGKRTVIDL GIHGLQPELI KMVGRMKYRS SYGQNLLQHS REVAKLCGVM AAELGLNPKL
     AKRAGLLHDI GKVPETETEV PHAILGMQWA EKHGEKPEVC NAIGAHHDEI EMNSLLSPIV
     QVCDAISGAR PGARRQVLDS YIQRLKDLEE IAFGFGGVKK AYAIQAGREL RVIVESEKVS
     DEKASNLSFE ISQKIQTDMT YPGQVKITVI RETRAVNVAK