ID A0A1V2ACE2_9BACI Unreviewed; 519 AA.
AC A0A1V2ACE2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BTO28_01030 {ECO:0000313|EMBL:OMP68665.1};
OS Domibacillus epiphyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714355 {ECO:0000313|EMBL:OMP68665.1, ECO:0000313|Proteomes:UP000188613};
RN [1] {ECO:0000313|EMBL:OMP68665.1, ECO:0000313|Proteomes:UP000188613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAB 38 {ECO:0000313|EMBL:OMP68665.1,
RC ECO:0000313|Proteomes:UP000188613};
RA Verma A., Ojha A.K., Krishnamurthi S.;
RT "Domibacillus sp. SAB 38T whole genome sequencing.";
RL Submitted (DEC-2016) 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:OMP68665.1}.
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DR EMBL; MSFI01000001; OMP68665.1; -; Genomic_DNA.
DR RefSeq; WP_076763142.1; NZ_MSFI01000001.1.
DR AlphaFoldDB; A0A1V2ACE2; -.
DR STRING; 1714355.BTO28_01030; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000188613; 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:UP000188613};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 335..428
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 72..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 58669 MW; E6EE61418E345B89 CRC64;
MEPITIISIL LGLIIGVVVG YFVRKSIAES KIAGAKNAAD QIVDDAKREA EASKKEALLE
AKDEIHKLRT ETEHELRERR NELQKQENRL LQKEENLDRK DDSLNKREET LEHKEAALQT
RQQHIEEMDS KVDEMVKKQQ SELERISALT RDEARSIILE RTEQELSHDI AIMVKENEHR
AKEESDKKAR EVLSLAIQRC AADHVAETTV SVVALPNDEM KGRIIGREGR NIRTLETLTG
IDLIIDDTPE AVILSGFDPI RRETARIALE KLVQDGRIHP ARIEEMVDKA RREVDEHIRE
IGEQTTFEVG VHGLHPDLIK ILGRLKYRTS YGQNVLKHSI EVAYLSGLLA AELGEDEMLA
RRAGLLHDIG KAVDHEVEGS HVEIGVELGQ KYKEHPVVIN SIASHHGDTE PTSVIAVLVA
AADALSAARP GARSETLENY IRRLEKLEDI SESYDGVEKS FAIQAGREVR IMVKPEQIDD
LQAHRLARDI RKRIESELDY PGHIKVTVIR ETRAVEYAK
//
