ID A0A180FRC6_9BACT Unreviewed; 466 AA.
AC A0A180FRC6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 23.
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:OAV74684.1};
GN ORFNames=Barb7_01782 {ECO:0000313|EMBL:OAV74684.1};
OS Bacteroidales bacterium Barb7.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1633203 {ECO:0000313|EMBL:OAV74684.1, ECO:0000313|Proteomes:UP000078281};
RN [1] {ECO:0000313|EMBL:OAV74684.1, ECO:0000313|Proteomes:UP000078281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Barb7 {ECO:0000313|EMBL:OAV74684.1,
RC ECO:0000313|Proteomes:UP000078281};
RA Tai V., Carpenter K.J., Weber P.K., Nalepa C.A., Perlman S.J.,
RA Keeling P.J.;
RT "Genomic and NanoSIMS analyses of nitrogen-fixing bacterial ectosymbionts
RT of a protist inhabiting a wood-eating cockroach.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:OAV74684.1}.
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DR EMBL; LBCZ01000235; OAV74684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180FRC6; -.
DR PATRIC; fig|1633203.3.peg.1738; -.
DR Proteomes; UP000078281; 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 Reference proteome {ECO:0000313|Proteomes:UP000078281};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00335}.
FT DOMAIN 282..375
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 9..89
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 466 AA; 52237 MW; 0A2F6A03BCB3834C CRC64;
MKEKFLHLQA DLEKQVSQRN AKLQSTEAKL KQKEMAVAQR QEELQRKNGE VEVIKENLAA
QLELIEKKKQ EIEKNKQELE KMHQSEIEHL EAISGLSADE ARERLIDSLK DTAKADAAAY
VNDIVEEAKM TANKEAKKIV IQSIQRVATE TAIENSITVF HIDSDEIKGR IIGREGRNIR
ALEAATGIEI VVDDTPEAIV LSGFDPVRRE IARLALHQLV QDGRIHPARI EEVVNKVKKQ
VEEEVIETGK RTTIDLGVHG LHPELIRMIG KMKYRSSYGQ NLLQHARETA NLCSVMASEL
GLNPKKAKRA GLLHDIGKVP DDEPELPHAI LGMKLCEKYK EKPDISNAVG AHHDEMEMQT
LLAPIVQVCD AISGARPGAR REIVEAYIKR LNDLEQLALA YPGVVKTYAI QAGRELRVIV
GADKIDDKET ENLSNEIAKK IQDEMTYPGQ VKITVIRETR AVSYAK
//
