ID A0A3P1VZG7_9FUSO Unreviewed; 524 AA.
AC A0A3P1VZG7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ECO:0000313|EMBL:RRD38967.1};
GN ORFNames=EII29_09225 {ECO:0000313|EMBL:RRD38967.1};
OS Leptotrichia sp. OH3620_COT-345.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=2491048 {ECO:0000313|EMBL:RRD38967.1, ECO:0000313|Proteomes:UP000280115};
RN [1] {ECO:0000313|EMBL:RRD38967.1, ECO:0000313|Proteomes:UP000280115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH3620_COT-345 {ECO:0000313|EMBL:RRD38967.1,
RC ECO:0000313|Proteomes:UP000280115};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {ECO:0000256|HAMAP-Rule:MF_00335}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
CC Single-pass membrane protein {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:RRD38967.1}.
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DR EMBL; RQYW01000016; RRD38967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1VZG7; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000280115; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 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 Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
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 Membrane {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}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00335};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00335}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 339..433
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 36..156
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 524 AA; 59481 MW; 1D139321B028D175 CRC64;
MPLLIAILLI VIFSFLAFFI AYFFGSSVFK KKYGELSELE LRIVDAKRRL ESSKKEVERE
IESFKKEETL KVKETLLNEK KKADEEIKKM KSEILSKEER LSKKEEVLET KIERLEEREL
KIEKQREKIS RKETELSELI QKEEKELERI SELTKEDASK IILTRLENEL DHDKAILIRD
FEHSLDREKD RISKRIISTA IGKASADYVV DSTISVIQLP SEEMKGRIIG REGRNIRAIE
AATGVDLIID DTPEAVVLSS FDGVRREVAR IALEKLISDG RIHPTKIEEV VQKAQEEVEE
SVMDAAEQAI LEVGIPTLPR EVLKVFGRLK FRTSFGQNIL QHSIEVAHIA AALAAEVGAN
IDIAKRAGLL HDIGKAFSHE QEGSHAINGG EFLRKFSKEN ETVINAVEAH HNEVEQLSVE
AVLVQAADSI SASRPGARRE TLSNYLKRLE QLEEIANSHE GIESSYAIQA GRELRLIVHP
DQINDDKAII LSREVAKEIE EKMQYPGQIK VTVIRETRAV EYAK
//
