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Database: UniProt
Entry: A0A1G2PMU2_9BACT
LinkDB: A0A1G2PMU2_9BACT
Original site: A0A1G2PMU2_9BACT 
ID   A0A1G2PMU2_9BACT        Unreviewed;       508 AA.
AC   A0A1G2PMU2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 19.
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=A2806_04645 {ECO:0000313|EMBL:OHA48951.1};
OS   Candidatus Terrybacteria bacterium RIFCSPHIGHO2_01_FULL_48_17.
OC   Bacteria; Candidatus Terrybacteria.
OX   NCBI_TaxID=1802362 {ECO:0000313|EMBL:OHA48951.1, ECO:0000313|Proteomes:UP000177629};
RN   [1] {ECO:0000313|EMBL:OHA48951.1, ECO:0000313|Proteomes:UP000177629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHA48951.1}.
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DR   EMBL; MHSS01000002; OHA48951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2PMU2; -.
DR   STRING; 1802362.A2806_04645; -.
DR   Proteomes; UP000177629; 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   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   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00335}.
FT   DOMAIN          324..417
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   COILED          54..120
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          149..176
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   508 AA;  56878 MW;  5AA2986A69939E9F CRC64;
     MTFGIVIAAA LALAAGLGIG WYLWSSLPAK QKEKAEASAK SIRERAEADA KSFILSAKDE
     AHKLLEEAKQ EERERLRALE RRESEFVVRE RELLSDRKRI DQERDALQRK QGELDNRAKE
     IEILHAQELK KLEEVAHLSV EEAHSKLLEQ IEKQHAEEFE RKLQQFERQA QQDLQERARD
     ILITAIQRYG ASHASEVTTT SVALPSEELK GRIIGKEGRN IKAFERASGC ELLVDDTPGA
     VVISGFDPVR REVAKRALEK LLVDGRMQPA RIEEVVAGCQ GEVDEIIRKA GEDAIQEVGV
     VGLDPRLVYL LGRLRFRTSF GQHVLQHSIE AAHLAGMIAA EIGANVQVAK KGALFHDIGK
     AIDHEVEGTH VEIGRKLLAR FGVEEPVIKA MQSHHEEYPF ETPESVIVKV AESISAARPG
     ARRDTVENYL RRLSDLERIA TSFPGVEKAY AIQAGREVRV FVVPEEVDDL AAKKLARAVA
     DQIEQELQYP GEIKVNVVRE TRVAEFAR
//
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