ID A0A1I4A2T2_9FIRM Unreviewed; 517 AA.
AC A0A1I4A2T2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN05216390_101379 {ECO:0000313|EMBL:SFK50241.1};
OS Lachnospiraceae bacterium KH1T2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1855374 {ECO:0000313|EMBL:SFK50241.1, ECO:0000313|Proteomes:UP000198626};
RN [1] {ECO:0000313|EMBL:SFK50241.1, ECO:0000313|Proteomes:UP000198626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1T2 {ECO:0000313|EMBL:SFK50241.1,
RC ECO:0000313|Proteomes:UP000198626};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOSY01000001; SFK50241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4A2T2; -.
DR STRING; 1855374.SAMN05216390_101379; -.
DR Proteomes; UP000198626; 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:UP000198626};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00335}.
FT DOMAIN 333..426
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 74..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 58240 MW; 9A828AE694CBD6B2 CRC64;
MGGMAIVIAV LVTLVIAVPL AWVIATNLHE QKIKRIIGDA DTKAKEITEK AEKAAEDLKR
EKLLEVKEES IRQKNELERE SKERRSELQR MERRAQQKEE SVDKKSELLE KREASCIAKE
NELNRQKEKI AKLNEERVQE LERISGLTSE QAKEYLLKIV EDDVKHESAL MIKEYESRAK
EEADKKAKEL VVNAIQRCAA DHVAETTISV VQLPNDEMKG RIIGREGRNI RTLETLTGVD
LIIDDTPEAV ILSGFDPIRR EVARIALEKL IVDGRIHPAK IEEMVEKARK EVDNTIREEG
EAATLEAGVP NLHPELIRLL GRMKYRTSYG QNALKHSIEV AILTGLFASE MGLDVRLAKR
AGLLHDIGKS VDHEMEGSHI QLGADLCRKY KESPIVINAV EAHHGDVEPT SLIACLVQAA
DTISAARPGA RRETLDAYTN RLKQLEDITN SFKGVEKSFA IQAGREVRVM VVPDQVNDTE
MVLMARDIAK KIENEMEYPG QIKVNIIRES RVTDYAK
//
