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Database: UniProt
Entry: M8E4A9_9BACL
LinkDB: M8E4A9_9BACL
Original site: M8E4A9_9BACL 
ID   M8E4A9_9BACL            Unreviewed;       508 AA.
AC   M8E4A9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Ribonuclease Y {ECO:0000256|HAMAP-Rule:MF_00335};
DE            Short=RNase Y {ECO:0000256|HAMAP-Rule:MF_00335};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00335};
GN   Name=rny {ECO:0000256|HAMAP-Rule:MF_00335};
GN   ORFNames=I532_00780 {ECO:0000313|EMBL:EMT54096.1};
OS   Brevibacillus borstelensis AK1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT54096.1, ECO:0000313|Proteomes:UP000012081};
RN   [1] {ECO:0000313|EMBL:EMT54096.1, ECO:0000313|Proteomes:UP000012081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK1 {ECO:0000313|EMBL:EMT54096.1,
RC   ECO:0000313|Proteomes:UP000012081};
RA   Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA   Sivakumar N.;
RT   "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC       {ECO:0000256|HAMAP-Rule:MF_00335}.
CC   -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000256|HAMAP-
CC       Rule:MF_00335}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMT54096.1}.
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DR   EMBL; APBN01000001; EMT54096.1; -; Genomic_DNA.
DR   AlphaFoldDB; M8E4A9; -.
DR   STRING; 1300222.I532_00780; -.
DR   PATRIC; fig|1300222.3.peg.167; -.
DR   Proteomes; UP000012081; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd22431; KH-I_RNaseY; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 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   NCBIfam; TIGR00277; HDIG; 1.
DR   NCBIfam; TIGR03319; RNase_Y; 1.
DR   PANTHER; PTHR12826; RIBONUCLEASE Y; 1.
DR   PANTHER; PTHR12826:SF15; RIBONUCLEASE Y; 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; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00335};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00335};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012081};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00335}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          324..417
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   COILED          21..120
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   508 AA;  57515 MW;  B6E820ED5DB0040E CRC64;
     MMIVLVAVLL VGLAIGYFVR KSIAEAKISS AEEAARQIVE EAKRDAEAVK KEKVLEAKDE
     VFKLRSEAET ELRERRNEIQ RQERRILQKE EALDRKMEQL ERKEEELAER DRTIADMQSK
     VEHLYKEQVS ELERISGLTQ EEAKTIILTE VEHTVRHEMA VMIKEIETQA KEEADKRARE
     IITTSIQRCA ADHVAETTVS VVTLPNDEMK GRIIGREGRN IRALETLTGI DLIIDDTPEA
     VILSGFDPIR REIAKTALDK LVADGRIHPA RIEEMVEKAR REVDERIREY GEQATFETGV
     HGLHPDLIKI LGRLRYRTSY GQNVLKHSME VAHLAGLMAA ELKEDVKLAK RAGLLHDIGK
     AIDHEVEGSH VEIGVELAKK YNEHPVVINS IASHHGDTEP TSVIAMLVGA ADALSAARPG
     ARRETLETYI KRLEKLEEIS ESFDGVEKSY AIQAGREIRV MVQPEKIDDA EATRLAREIT
     KRIENELDYP GHIKVTVIRE TRAVEYAK
//
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