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Database: UniProt
Entry: A0A0G1GA45_9BACT
LinkDB: A0A0G1GA45_9BACT
Original site: A0A0G1GA45_9BACT 
ID   A0A0G1GA45_9BACT        Unreviewed;       549 AA.
AC   A0A0G1GA45;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 34.
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=UW18_C0005G0020 {ECO:0000313|EMBL:KKT31248.1};
OS   Microgenomates group bacterium GW2011_GWF1_44_10.
OC   Bacteria.
OX   NCBI_TaxID=1618537 {ECO:0000313|EMBL:KKT31248.1, ECO:0000313|Proteomes:UP000034538};
RN   [1] {ECO:0000313|EMBL:KKT31248.1, ECO:0000313|Proteomes:UP000034538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT31248.1}.
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DR   EMBL; LCHI01000005; KKT31248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1GA45; -.
DR   PATRIC; fig|1618537.3.peg.683; -.
DR   Proteomes; UP000034538; 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; 3.30.310.210; -; 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   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00335}.
FT   DOMAIN          366..458
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   REGION          15..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          96..225
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        15..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  62239 MW;  96BAF4945763299E CRC64;
     MSFFSKLSTL FSNTQNAPAD THAQAKSTTQ LQPQPQAQLS RQPVMQPRVA HPHQTHQQNR
     QPKQQPPHQQ TQQTQPNQQQ LDSAVREAQA RAKEIIVEAK DEALQIREKA EKESREQRRE
     LSDKEKIVDQ KIFSIDSRLK ALDEKEETLE KKKADIAKLQ TQAEETQQKL LDKLEKVAGL
     TRDQAKQQIL EGVEKSLTQE VARRIQEAEN KAKEEADEKA QEILIDAMRH GATDYVAEYT
     VSTVILPDDE VKGRIIGKDG RNIRSFEQAT GVDVDLDDTP GQVRLSSFNP VRREIARITL
     ERLIKDGRIQ PTRIEETVKK VTEELQKIMF EEGKKLCHAV GVYNMPSELI QMLGKFKYRF
     SYGQNLIAHT LEETQIGIKL ARETGANVET VKLGCLLHDI GKVVDSEEGS HIELGVELLK
     KYRIPKVVID CVEQHHEDVP FSSVESVLVY IADAISGSRP GARYENYDEY VKRLTKLEDI
     AKGYEQVQSA YAIQAGREVR VILKGDASKD DDVIVLSHTI KDRVQKEMTY PGTVTVTVIR
     EMRGVDIAK
//
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