ID A0A0G0K7V0_9BACT Unreviewed; 523 AA.
AC A0A0G0K7V0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 36.
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=US90_C0002G0038 {ECO:0000313|EMBL:KKQ71555.1};
OS Candidatus Shapirobacteria bacterium GW2011_GWE2_38_30.
OC Bacteria; Candidatus Shapirobacteria.
OX NCBI_TaxID=1618490 {ECO:0000313|EMBL:KKQ71555.1, ECO:0000313|Proteomes:UP000034406};
RN [1] {ECO:0000313|EMBL:KKQ71555.1, ECO:0000313|Proteomes:UP000034406}
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:KKQ71555.1}.
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DR EMBL; LBUT01000002; KKQ71555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0K7V0; -.
DR STRING; 1618490.US90_C0002G0038; -.
DR PATRIC; fig|1618490.4.peg.122; -.
DR Proteomes; UP000034406; 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; 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 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 327..419
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 13..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 58802 MW; 9E586ED5FF2E6B5B CRC64;
MFSSIFSKVS DLLGNKTLPS QPTQTKLDDS GKNRVSFQPK PDQSPKVVKK TIKKQKTVSQ
EDIIASQKTQ QALENASRLE AEARKKEAEI FQRLASLDEK EKYLIQKEKN LDTQSNDLKT
KYAQVDELYK KQLDKLEQIS GIDVEKAKQI IINSTEKKMV NWIAKKVTDA KEQIKQKEEE
ASKEILVDAI RHGVTDYVAE YTVSTITLPD EKIKGKIIGR EGRNIRSFEK VTGVELELDE
TNDVRISSFD STRREIARIS LEKLIKDGRI QPVKIETIVA QTKLEMDKIL LNEGKKICQE
VGVFNLPIDL MKYIGKYKFR FSYGQNLAKH TIEATKIAVA LAYELHADVN TVRLGALLHD
IGKVISDQEG THIDLGVDLL RQFRLPESVI NAVAEHHEDK EFSSPESVIV YLGDASSGAR
PGARYEVHEE YLKRMTNIEE VAKSFSGVIN VAAYQAGREV MVIVDPGQVS DSEAEVLSQN
IAEKLEEEAK WAGQIKVTVI REMRTSSVIV GSKISKNAVK ISD
//
