GenomeNet

Database: UniProt
Entry: A0A0F7HK16_9STAP
LinkDB: A0A0F7HK16_9STAP
Original site: A0A0F7HK16_9STAP 
ID   A0A0F7HK16_9STAP        Unreviewed;       519 AA.
AC   A0A0F7HK16;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=AAT16_05970 {ECO:0000313|EMBL:AKG73809.1}, SAMN05216235_0433
GN   {ECO:0000313|EMBL:SFK56240.1};
OS   Salinicoccus halodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX   NCBI_TaxID=407035 {ECO:0000313|EMBL:AKG73809.1, ECO:0000313|Proteomes:UP000034029};
RN   [1] {ECO:0000313|EMBL:AKG73809.1, ECO:0000313|Proteomes:UP000034029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3B36 {ECO:0000313|EMBL:AKG73809.1,
RC   ECO:0000313|Proteomes:UP000034029};
RX   PubMed=26634017;
RA   Jiang K., Xue Y., Ma Y.;
RT   "Complete genome sequence of Salinicoccus halodurans H3B36, isolated from
RT   the Qaidam Basin in China.";
RL   Stand. Genomic Sci. 10:116-116(2015).
RN   [2] {ECO:0000313|Proteomes:UP000034029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3B36 {ECO:0000313|Proteomes:UP000034029};
RA   Ma Y., Jiang K., Xue Y.;
RT   "Complete genome sequence of Salinicoccus halodurans strain H3B36, isolated
RT   from the Qaidam basin of China.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SFK56240.1, ECO:0000313|Proteomes:UP000183090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6501 {ECO:0000313|EMBL:SFK56240.1,
RC   ECO:0000313|Proteomes:UP000183090};
RA   Varghese N., Submissions S.;
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}.
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; CP011366; AKG73809.1; -; Genomic_DNA.
DR   EMBL; FOTB01000001; SFK56240.1; -; Genomic_DNA.
DR   RefSeq; WP_046789997.1; NZ_FOTB01000001.1.
DR   AlphaFoldDB; A0A0F7HK16; -.
DR   STRING; 407035.AAT16_05970; -.
DR   KEGG; shv:AAT16_05970; -.
DR   PATRIC; fig|407035.3.peg.1240; -.
DR   OrthoDB; 9803205at2; -.
DR   Proteomes; UP000034029; Chromosome.
DR   Proteomes; UP000183090; 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   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};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00335};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00335}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT   DOMAIN          335..428
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   REGION          65..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  58788 MW;  09A008B09E72F571 CRC64;
     MDMIDIFLIL LGIILGVVIG YFIVRNTLTK RQQEARTSAE HIINEAEKEA ESLKKEKLLE
     AKEENQNLKD AFERDSSEKR EDLKAQESRL LQREQTLDRK SEVLDKKDEA LESKEAKIEE
     KQQMVDAEDQ KIKEIISRQE EELSRISGLT RDEARNEIFT EVERELSHDM AVMVKEKEDQ
     MKLEVDKKAK ELLAVTAQRY AAEYTSESTV SVVNLPNDEM KGRIIGREGR NIRTLETLTG
     VDLIIDDTPE AVILSGFDPI RRAIAKNALE ALVQDGRIHP GRIEEMVDKA KRNMEADIRD
     AGEAAAFELD IHNLHPELVK HLGKMKYRLS YGQNVLKHSV EVGYLAGMLA SELGEDVQLA
     RRAGLLHDIG KAIDHEVEGS HVEIGVELAK RYKEHPTVIN AIHSHHGDVE PTSIISIIVA
     AADALSAARP GARRETLENY VKRLERLESI AEGYEGVEKT FAIQAGREIR VMVKPDELDD
     LSAHRLARDI KKQVEDELQY PGHIKVTVVR EMRAVEYAK
//
DBGET integrated database retrieval system