ID A0A0A6Y2Q9_9BACI Unreviewed; 520 AA.
AC A0A0A6Y2Q9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=NG54_02685 {ECO:0000313|EMBL:KHD86577.1};
OS Heyndrickxia ginsengihumi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=363870 {ECO:0000313|EMBL:KHD86577.1, ECO:0000313|Proteomes:UP000030588};
RN [1] {ECO:0000313|EMBL:KHD86577.1, ECO:0000313|Proteomes:UP000030588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2.11 {ECO:0000313|EMBL:KHD86577.1,
RC ECO:0000313|Proteomes:UP000030588};
RA Toymentseva A., Boulygina E.A., Kazakov S.V., Kayumov I., Suleimanova A.D.,
RA Mardanova A.M., Maria S.N., Sergey M.Y., Sharipova M.R.;
RT "Draft genome of phytase producing Bacillus ginsengihumi strain M2.11.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {ECO:0000256|HAMAP-Rule:MF_00335}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
CC Single-pass membrane protein {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:KHD86577.1}.
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DR EMBL; JRUN01000004; KHD86577.1; -; Genomic_DNA.
DR RefSeq; WP_035353011.1; NZ_JRUN01000004.1.
DR AlphaFoldDB; A0A0A6Y2Q9; -.
DR STRING; 363870.NG54_02685; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000030588; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
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|HAMAP-Rule:MF_00335};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW Reference proteome {ECO:0000313|Proteomes:UP000030588};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00335};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00335};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00335}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 336..429
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 88..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 59250 MW; 0163CB7B0935C7F1 CRC64;
MEPIIWIISL LLVLIVGVVV GYFIRRSIFE AKVTAAKNVS DQIIDDAKRE ADRLKKEALL
EAKDENHKLR TDIERELRER RNELQKQENR LLQKEENLDR KDESLDKRDA VLDKKEESLN
QRQQHIEEME SKLEEMVKKQ EFELERISGL NRDQAKAIII EKLENELSHE LAIMVKESEN
RAKEEADKKA KNILSLAIQR CAAEHVAETT VSVVNLPNDE MKGRIIGREG RNIRTLETLT
GIDLIIDDTP EAVILSGFDP VRRETARIAL EKLVQDGRIH PARIEEMVDK ARREVDEYIR
EVGEQTTFEV GVHGLHPDLI KILGRLKFRT SYGQNVLKHS IEVAFLSGLL AAELGEDEIL
ARRAGLLHDI GKAVDHEVEG SHVEIGIDLA KKYKEHPVVI NSIASHHGDT EPTSIIAVLV
AAADALSAAR PGARSETLEH YIRRLEKLED IAESYEGVEK SFAIQAGREV RIMVKPDQIN
DLEAHRLARD IRKRIESELD YPDHIKVTVI RETRAVEYAK
//
