ID A0A0G1PJN0_9BACT Unreviewed; 524 AA.
AC A0A0G1PJN0;
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=UX47_C0007G0146 {ECO:0000313|EMBL:KKU32902.1};
OS Candidatus Collierbacteria bacterium GW2011_GWA2_46_26.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1618381 {ECO:0000313|EMBL:KKU32902.1, ECO:0000313|Proteomes:UP000034794};
RN [1] {ECO:0000313|EMBL:KKU32902.1, ECO:0000313|Proteomes:UP000034794}
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:KKU32902.1}.
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DR EMBL; LCMI01000007; KKU32902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1PJN0; -.
DR PATRIC; fig|1618381.3.peg.901; -.
DR Proteomes; UP000034794; 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; 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 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 342..433
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 15..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..187
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 58375 MW; 54F6036B67619A34 CRC64;
MSILSIFRSN IFKGSDTPSK SKAVSSATPQ TVKETEKTNT KEAPAVQAPS VDTAAILAAA
QATAQSQARE IIISAKDEAF KIKDQAIKDA RIQLEEIEVR AKNLAQKQQS NATIEEQLKR
EKANIDLQTQ QIEELKAKIA SQADSMVEKL EKIASLTTEQ AKKELIAQVE KRSAAEAARA
IKEAEEKSKM ECEDLAREIL IDAMKAGATD YVAEYTISTV PIPDEETKGR IIGKDGRNIR
IFEKVSGCDV SMDDSPDEVK LSSFDPVRRE IARLTLIHLI KDGRIHPARI EEYFERSKRD
VEQIMFLEGQ KLCHAVGVYN MNREIIAMLG RFKFRTSYGQ NMISHTLEET RIGIKMANEI
GANVDTVRMG CLLHDIGKIL EGEGNHVELG VQYLKKFNIP QGIIDCVAQH HEDEEFTSNE
SMIVYISDAI SGSRPGARHE NTEEYGKRIR HLEEIAKKHP EVDDAYAISA GREIRVIVNP
GKAGDDQLTI LAQAIRDEIR DTMTFPGTVK VNCIRETRAS EIAS
//
