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
//