ID A0A1T1BHT0_9DEIO Unreviewed; 572 AA.
AC A0A1T1BHT0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=BXU09_06540 {ECO:0000313|EMBL:OOV15870.1};
OS Deinococcus sp. LM3.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1938608 {ECO:0000313|EMBL:OOV15870.1, ECO:0000313|Proteomes:UP000191141};
RN [1] {ECO:0000313|EMBL:OOV15870.1, ECO:0000313|Proteomes:UP000191141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM3 {ECO:0000313|EMBL:OOV15870.1,
RC ECO:0000313|Proteomes:UP000191141};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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:OOV15870.1}.
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DR EMBL; MUFV01000001; OOV15870.1; -; Genomic_DNA.
DR RefSeq; WP_055362089.1; NZ_MUFV01000001.1.
DR AlphaFoldDB; A0A1T1BHT0; -.
DR STRING; 1938608.BXU09_06540; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000191141; 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 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00335}.
FT DOMAIN 388..481
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 48..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 63459 MW; 45FCB0BD84F95526 CRC64;
MTMIWIIVAL LIGLVGGFLG GQSRGARQRA EVDDRLQREA SAEAQRIRAQ AEADAQRIRE
QADQARQDAG RRTQEAADRE AQAGVQLAQL DGQREQLNSQ REQIAALRAQ VEAERAQAKQ
DAAREREALS SDRQETRRER DELKREIERL NRRAEQLDAR GEKLDALEDR LEERSRTLTD
HEAEITARLH QADLKLFEVA NLSPEAAREE ILGRLDAELE EEKAIRVKAM QERASADARR
TARHVIAQAI QRSASETSAA LSVSVVPIPN DAMKGRLIGR EGRNIRAFEA LTGVDLIIDD
TPEAVILSSF NPVRREVAKH VLDALVADGR IHPTRIEEMV HKAQEEMKTF MHAQGEEAAI
EAGVVGIKPG LVQLLGRMYF RTSYGQNVLK HSIQVAHLTG IMAGELGLDA GMARRAGLMH
DVGKSIDREI DGTHVDIGIN LAKRFGEPHE VIDAIAHHHD PENGETLYSV LVAAADAISA
ARPGARREEL ESYVRRLEQL EQIAVSFPGV QQAYAIQAGR EVRVIVQPEK VTDAQATLLA
REIAGRVEQD MEYPGQVQVT VVRESRAVEV AR
//
