ID A0A1F8PBJ5_9CHLR Unreviewed; 509 AA.
AC A0A1F8PBJ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 20.
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=A2Z14_13580 {ECO:0000313|EMBL:OGO20508.1};
OS Chloroflexi bacterium RBG_16_48_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797641 {ECO:0000313|EMBL:OGO20508.1, ECO:0000313|Proteomes:UP000177106};
RN [1] {ECO:0000313|EMBL:OGO20508.1, ECO:0000313|Proteomes:UP000177106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO20508.1}.
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DR EMBL; MGNI01000025; OGO20508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8PBJ5; -.
DR STRING; 1797641.A2Z14_13580; -.
DR Proteomes; UP000177106; 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; 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 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 325..418
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 37..111
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 509 AA; 57351 MW; DD87A766F2E8D18C CRC64;
MGYTWTIIIG LTALVSGVLI GFFIRQFQLY RDKKNQQAEV EGMLEKAHAK ARELELRARD
EALRYRDEAE AEISRRRAEL NREEERVQSR REDLDKRLEN IERRDQALNK RQSSLDRRSN
ELEKQHNDII TELERISSMT QDEAKVQLLE EVERDARADM LRIIRQIEEE AQMEGERRAR
ELIADAIQRV ASDHVSEVTV SIVPLPSDDM KGRIIGRNGR NIRAFEQAAG VDVVVDDTPE
AVTISCFDPV RREVARKAME KLVLDGRIHP AHIEKILEQM NEEVQRVILE EGESAAYDAG
VPGLHPEIVK KLGRLKFRTS YGQNQLAHAV ETAQLAGVIA AELGADPDVA KAGGLLHDIG
KAMDHEVEGT HSAIGAEFCR RHGVNEKIIN TIASHHHETE QESVEAVIVE AADAISGARP
GARRESLEQY IKRIKALEEV ANSFTGVSES YALQAGREIR VIVKPDDIDD LDATRLARDV
AKKIEEGMQY PGQIKVTVIR ETRAVDYAK
//
