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Database: UniProt
Entry: A0A0G1TZ09_9BACT
LinkDB: A0A0G1TZ09_9BACT
Original site: A0A0G1TZ09_9BACT 
ID   A0A0G1TZ09_9BACT        Unreviewed;       509 AA.
AC   A0A0G1TZ09;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 30.
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=UX81_C0010G0011 {ECO:0000313|EMBL:KKU59348.1};
OS   Parcubacteria group bacterium GW2011_GWA2_47_12.
OC   Bacteria.
OX   NCBI_TaxID=1618841 {ECO:0000313|EMBL:KKU59348.1, ECO:0000313|Proteomes:UP000034388};
RN   [1] {ECO:0000313|EMBL:KKU59348.1, ECO:0000313|Proteomes:UP000034388}
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:KKU59348.1}.
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DR   EMBL; LCNP01000010; KKU59348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1TZ09; -.
DR   PATRIC; fig|1618841.3.peg.324; -.
DR   Proteomes; UP000034388; 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          325..418
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   COILED          56..142
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   509 AA;  56312 MW;  3EC00F5301A5EF4F CRC64;
     MSLKLVLALA AASGLLGVGL GAYLRFLISI GKKGSMELKL KEIELKGQEE SKKLTLKAEE
     EAARILKEAR SEARVKEDSV KKSEERLVKR EDTLDKRQSD LDKETEELKA RIVEIKKIKE
     RADALEAEKR AALERAARLS EEDAKKELIA AVEKKNEEDI LMRMQKLEQG GEEKLERRAQ
     EIITSAIQRL GTNIAADSLT TSVSIPSDDA KGKIIGKEGR NIKAFERATG VEVIVDDTPG
     SITISSFNPI RRQIARVALE NLILDGRIQP AKIEQMVEKA EQEINKIIKD KGTQAAFECG
     VINLPPQVIA ILGRLHFRTS YGQNVLHHSI EMAHIAGMIA SELGVNIAVA KAGALLHDIG
     KAMDHEVQGT HVEIGRRILQ KFGVDEAVVK AMQAHHGEYP FETPESVIVQ VADAISGARP
     GARRDTVENY LKRLEDLERI ATSSPGIEKA YALQAGREIR IFVKSAEVSD LEAKNIAKNT
     AKKIEDELKY PGEIKVTVIR ENRVVEYAR
//
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