ID A0A1H1PID1_9BACT Unreviewed; 543 AA.
AC A0A1H1PID1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, 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 ORFNames=SAMN05444173_1918 {ECO:0000313|EMBL:SDS11038.1};
OS Opitutus sp. GAS368.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=1882749 {ECO:0000313|EMBL:SDS11038.1, ECO:0000313|Proteomes:UP000199432};
RN [1] {ECO:0000313|EMBL:SDS11038.1, ECO:0000313|Proteomes:UP000199432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS368 {ECO:0000313|EMBL:SDS11038.1,
RC ECO:0000313|Proteomes:UP000199432};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; LT629735; SDS11038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1PID1; -.
DR STRING; 1882749.SAMN05444173_1918; -.
DR Proteomes; UP000199432; Chromosome i.
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; 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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
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 Reference proteome {ECO:0000313|Proteomes:UP000199432};
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 36..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 359..452
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
SQ SEQUENCE 543 AA; 60863 MW; B74C76331B8C8C51 CRC64;
MVAKPPGPRR FATPEMLTII AAITKPALTS SAAEPYLWAL LAAGLVGVMG GFFGVWFIMR
QSRRLAEQSA ASHLELARRE AAVTAQEMIG KAEEDIRARE AEMNRDFDRR KIEIELMLRE
IRSHEESLAL LDYQLEQRQE RLAREASAIK QARDAMRDLS KSLRKRLEGV ASLDGEEVRK
QLREEVVFEC QEELRALRKE LLERSEQEVV QESKRILVAT MQRLASKPNN DITATIVQLP
SEEMKGRIIG REGRNIKSFE AATATTLLID ESPQMVLISS FDPVRREIAK LALESLVKDG
RIHPASIEEF VNRARQDMDL HVAQIGEEAV DRLKISGLHP EIIKLLGRLR FRFSYTQNVL
DHSIEVAQLC SMLASELGLE PNVAKRAGLL HDIGKSIEGE YEGSHALIGA DFIRRYGETT
IVVNAVAAHH AEVKPETIYA GLVILADAIS ASRPGARAES MTSYIERLGR LEKLAMTMPG
VQQAFAIQAG REVRVVVQPS VVTDEQAHLL AKNLRKKIEE ELDYPSTIKV TVIREQRYTE
TAT
//