ID A0A1B8U0G8_9FLAO Unreviewed; 522 AA.
AC A0A1B8U0G8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=LPB3_03090 {ECO:0000313|EMBL:OBY65360.1};
OS Polaribacter vadi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1774273 {ECO:0000313|EMBL:OBY65360.1, ECO:0000313|Proteomes:UP000092584};
RN [1] {ECO:0000313|Proteomes:UP000092584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0003 {ECO:0000313|Proteomes:UP000092584};
RA Shin S.-K., Yi H., Kim E.;
RL Submitted (FEB-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}.
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:OBY65360.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSFM01000018; OBY65360.1; -; Genomic_DNA.
DR RefSeq; WP_065318138.1; NZ_LSFM01000018.1.
DR AlphaFoldDB; A0A1B8U0G8; -.
DR STRING; 1774273.LPB03_02020; -.
DR KEGG; pob:LPB03_02020; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000092584; 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..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 338..431
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 100..148
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 522 AA; 58648 MW; A4CB7FF376197C5A CRC64;
MEGIILPIIM GVLIGVALGF IIFRSMEKAK GKKMLNGVRK EAATILKEAK IDAESVKKDK
ILQAKEKFIE LKSEHEKVII SREKKISDVE KRIRDRESKV ASEYDKNKRL NQSLEQKEKD
YDFKIDFLEK KEDDLDKMHK RHVDMLEQIS GLSAEEAKKE LVSSLKEEAK SEAMAFVQTS
IEEAKLTAEQ EARKVVLGTI QRVGVEQAVE NCVSVFNLES DDVKGRIIGR EGRNIRALEA
ATGVEIIVDD TPEAIILSCF DPVRREIARL SMHKLVTDGR IHPARIEEIV KKTENQIHQE
IIEVGKRTVI DLGIHGLHPE LIKTVGRMKY RSSYGQNLLQ HSREVSNLCG IMASEMGLNA
KLAKRAGLLH DIGKVPNEES ELPHALLGMQ WAEKYGEKEE VCNAIGAHHD EIEMKSLLSP
IVQVCDAISG ARPGARRQVL DSYIQRLKDL EEIAFGFTGV QKAYAIQAGR ELRVMVESDK
VNDTKAAELS FSISQKIQND MTYPGQVKVT VIRETRAVNV AK
//