ID A0A1W9RCK5_9BACT Unreviewed; 514 AA.
AC A0A1W9RCK5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=B6D64_00870 {ECO:0000313|EMBL:OQX82274.1};
OS Bacteroidetes bacterium 4484_276.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1970779 {ECO:0000313|EMBL:OQX82274.1, ECO:0000313|Proteomes:UP000192605};
RN [1] {ECO:0000313|Proteomes:UP000192605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) 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:OQX82274.1}.
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DR EMBL; NATG01000009; OQX82274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9RCK5; -.
DR Proteomes; UP000192605; 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..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 330..423
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 31..58
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 514 AA; 57528 MW; BD8428C1C47EC6A7 CRC64;
MEGTLIIVVI GVVGFALGVL LSATVLRKVL QKKSEVLLKE AQEKAEVIKK EKILQAKEKF
LQLKSEHEKT VNQRNSALQK NENRVKQKES SVSHRIEEFR KKEKEVDSLK VNLSSQLKIL
NQKQEDVNKF HSKQVKQLEE MSGLSAEEAK SQLMETLKDE AKSDAMVHIQ EVLEEAKITA
HMEARKIIVE TIQRTAAEQT IENSVSVFNI DNDEIKGRII GREGRNIRAL EALTGIEIII
DDSPDAILLS GFDPVRREIA RLSLHKLVTD GRIHPARIEE VVSKTKKQIE QEIIETGKRT
CIDLGIHGMH HELVRMVGRM KYRSSYGQNL LQHSREVANL CATMAAELGL NTKKAKRAGL
LHDIGKVPDN ESELPHALLG MKLAEKFKEQ PDVANAVGAH HDEVEMTTLI APIVQVCDAI
SGARPGARRE VVEAYIQRLK NLEGIALSYP GVVKTYAIQA GRELRVIVGA DKVSDEEANV
LSYDLSKKIQ DEMTYPGQVK ITVIRETRAI SYAK
//
