ID A0A3A9SJW0_9FIRM Unreviewed; 515 AA.
AC A0A3A9SJW0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ECO:0000313|EMBL:RKM57573.1};
GN ORFNames=D6855_13585 {ECO:0000313|EMBL:RKM57573.1};
OS Butyrivibrio sp. CB08.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=2364879 {ECO:0000313|EMBL:RKM57573.1, ECO:0000313|Proteomes:UP000281491};
RN [1] {ECO:0000313|Proteomes:UP000281491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB08 {ECO:0000313|Proteomes:UP000281491};
RA Hivarkar S., Lanjekar V.B., Dhakephalkar P.K., Dagar S.;
RL Submitted (SEP-2018) 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:RKM57573.1}.
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DR EMBL; RAIR01000008; RKM57573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9SJW0; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000281491; 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 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 Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW Reference proteome {ECO:0000313|Proteomes:UP000281491};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00335}.
FT DOMAIN 331..424
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 95..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57837 MW; E8944DC190B1593F CRC64;
MTTVIIAVVA TLVITALITW ILASNYHKKV ADGKIGSAEE RARKIIDEAL KTAEDTKREK
LLEVKEESLK TRNDLEKEVK DRRNEIQRAE RRIQQKEENV EKRSEAIERR EQSLSAREEN
LNKKTEEVAK LNEQRLQELE KISGLTSEQA KEYLLKIVED DVKHESAIMI KNMEAEAKEE
ADKRAKEIVV GAIQRCAADH VSETTISVVQ LPNDEMKGRI IGREGRNIRT LETMTGVDLI
IDDTPEAVVI SGFDPIRREV ARIALEKLIV DGRIHPARIE EMVEKAQKEV AAKIKEEGEN
AAIEAGVHGL HPEVTKILGR MMFRTSYGQN VLKHSVEVAQ LCGLMASELG LDVRVAKRAG
LLHDIGKAVD HELEGSHIQL GVDICRKYKE SQVVINAVEA HHGDVEPQSL IAVLVQAADT
ISSARPGARR ETLETYTSRL KELEDITNSF KGVDHSFAIQ AGREVRVMVV PEQVTDEDMV
IMARDIAKKI EDEMEYPGQI KVNIIRESRA TDYAK
//
