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Database: UniProt
Entry: G0GBQ0_SPITZ
LinkDB: G0GBQ0_SPITZ
Original site: G0GBQ0_SPITZ 
ID   G0GBQ0_SPITZ            Unreviewed;       509 AA.
AC   G0GBQ0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   OrderedLocusNames=Spith_0853 {ECO:0000313|EMBL:AEJ61128.1};
OS   Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=869211 {ECO:0000313|EMBL:AEJ61128.1, ECO:0000313|Proteomes:UP000007254};
RN   [1] {ECO:0000313|EMBL:AEJ61128.1, ECO:0000313|Proteomes:UP000007254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700085 / DSM 6578 / Z-1203
RC   {ECO:0000313|Proteomes:UP000007254};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Spirochaeta thermophila DSM 6578.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC       {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; CP002903; AEJ61128.1; -; Genomic_DNA.
DR   RefSeq; WP_013314085.1; NC_017583.1.
DR   AlphaFoldDB; G0GBQ0; -.
DR   STRING; 869211.Spith_0853; -.
DR   KEGG; stq:Spith_0853; -.
DR   HOGENOM; CLU_028328_1_0_12; -.
DR   OrthoDB; 9803205at2; -.
DR   Proteomes; UP000007254; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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   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   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007254};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00335}.
FT   DOMAIN          325..418
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   COILED          29..177
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   509 AA;  57610 MW;  D7944D698CF6247E CRC64;
     MNVLLSVALP LLGLALGWTA RWLYARFQLT SAEQRAERIK DEAVKEAEAR KKEILFEAQE
     QIHKERLQLE KELRERRAEL QRTERRLLQK EETLERKLAA VERRNEALAD RERLLAEKET
     ELGRREQEIE SELERISGLT REEARSLIIS RLEEEAKRDA QILVNKIEEE ARATAERKAR
     DVLVSTMQRI ATDVTAEVTV TTVSLPNDEM KGRIIGREGR NIRTLETLTG VDIIIDDTPE
     AVVLSCFDPV RKEIARISLE RLIADGRIHP ARIEEVVHKV TKELSQTIYE EGEKVLFELG
     IHDFPPEAVQ ALGRLKYRTS YGQNVLAHTK EVAVLAGMIA AEVGGDPMIA KRGALLHDIG
     KAIESDDDST HIELGIELAK RMGEDSRVIN CIAAHHGDVP HTCPESVIVQ IADAISASRP
     GARRESLENY IKRLEQLEKI AEGFSGVDKA FAIQAGREIR IMVNNDLVDD AGARELAREI
     ARKIEEDLRY PGRIKVTIIR ETRVVEYAR
//
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