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Database: UniProt
Entry: A0A420ETU4_9ACTN
LinkDB: A0A420ETU4_9ACTN
Original site: A0A420ETU4_9ACTN 
ID   A0A420ETU4_9ACTN        Unreviewed;       588 AA.
AC   A0A420ETU4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
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:RKF24102.1};
GN   ORFNames=D7I43_27845 {ECO:0000313|EMBL:RKF24102.1};
OS   Micromonospora globbae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1894969 {ECO:0000313|EMBL:RKF24102.1, ECO:0000313|Proteomes:UP000285744};
RN   [1] {ECO:0000313|EMBL:RKF24102.1, ECO:0000313|Proteomes:UP000285744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WPS1-2 {ECO:0000313|EMBL:RKF24102.1,
RC   ECO:0000313|Proteomes:UP000285744};
RX   PubMed=29458491; DOI=.1099/ijsem.0.002625;
RA   Kuncharoen N., Pittayakhajonwut P., Tanasupawat S.;
RT   "Micromonospora globbae sp. nov., an endophytic actinomycete isolated from
RT   roots of Globba winitii C. H. Wright.";
RL   Int. J. Syst. Evol. Microbiol. 68:1073-1077(2018).
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:RKF24102.1}.
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DR   EMBL; RAQQ01000027; RKF24102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420ETU4; -.
DR   OrthoDB; 9803205at2; -.
DR   Proteomes; UP000285744; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000285744};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00335}.
FT   DOMAIN          404..497
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   COILED          48..162
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          187..221
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   588 AA;  64349 MW;  7FB0C22BDD8AC97F CRC64;
     MSAFDTVLLV AVLLLTLVVA GAMVVGLRTL RRIGTAPAAA DPAFIAEKDR QEQSLAALRS
     AADEANSTID VAKSAAAAAR AEAAAAKAEA KAARAEARRM LDDARAEADT ILERAHKQAE
     ADAEQLRATA RRSGEREVAV LAATTREQAA EVERRAARMD ERERLHTEEV ERLAERERQL
     TAASAALAAR EAALDQREAE LAEAEERRRR ELERVAGLTA EAARAELIEA IESQAKREAA
     LLVRDIEADA RSTAEERARH IVVDAIQRVA SEQTAESVVS VLHLPGDEMK GRIIGREGRN
     IRAFESVTGV NLIIDDTPEA VLLSCFDPVR REVGRLTLEK LVLDGRIHPH RIEEVYDLAR
     QEVEQLCRRA AEDALVEVGI TEIHPELVTL LGRLRYRTSY GQNVLKHLVE TAHIAGVMAA
     ELRLDVPLIK RSAFLHDIGK ALTHEVEGSH AIIGADLARK YGESEEVVHA IEAHHNEVPP
     QTVEAVLTQA SDACSGGRPG ARRESLEAYV KRLERIEEIA AGKLGVEKVF AMQAGREIRV
     MVKPEDVDDI GAAVLARDVA KQIEEELTYP GQIRVTVVRE SRVTEIAR
//
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